annotation_CSV/PMC4784909.csv

anno_start	anno_end	anno_text	entity_type	sentence	section
24	34	Coenzyme A	chemical	The Structural Basis of Coenzyme A Recycling in a Bacterial Organelle	TITLE
50	59	Bacterial	taxonomy_domain	The Structural Basis of Coenzyme A Recycling in a Bacterial Organelle	TITLE
0	9	Bacterial	taxonomy_domain	Bacterial Microcompartments (BMCs) are proteinaceous organelles that encapsulate critical segments of autotrophic and heterotrophic metabolic pathways; they are functionally diverse and are found across 23 different phyla.	ABSTRACT
10	27	Microcompartments	complex_assembly	Bacterial Microcompartments (BMCs) are proteinaceous organelles that encapsulate critical segments of autotrophic and heterotrophic metabolic pathways; they are functionally diverse and are found across 23 different phyla.	ABSTRACT
29	33	BMCs	complex_assembly	Bacterial Microcompartments (BMCs) are proteinaceous organelles that encapsulate critical segments of autotrophic and heterotrophic metabolic pathways; they are functionally diverse and are found across 23 different phyla.	ABSTRACT
16	25	catabolic	protein_state	The majority of catabolic BMCs (metabolosomes) compartmentalize a common core of enzymes to metabolize compounds via a toxic and/or volatile aldehyde intermediate.	ABSTRACT
26	30	BMCs	complex_assembly	The majority of catabolic BMCs (metabolosomes) compartmentalize a common core of enzymes to metabolize compounds via a toxic and/or volatile aldehyde intermediate.	ABSTRACT
32	45	metabolosomes	complex_assembly	The majority of catabolic BMCs (metabolosomes) compartmentalize a common core of enzymes to metabolize compounds via a toxic and/or volatile aldehyde intermediate.	ABSTRACT
141	149	aldehyde	chemical	The majority of catabolic BMCs (metabolosomes) compartmentalize a common core of enzymes to metabolize compounds via a toxic and/or volatile aldehyde intermediate.	ABSTRACT
16	35	phosphotransacylase	protein_type	The core enzyme phosphotransacylase (PTAC) recycles Coenzyme A and generates an acyl phosphate that can serve as an energy source.	ABSTRACT
37	41	PTAC	protein_type	The core enzyme phosphotransacylase (PTAC) recycles Coenzyme A and generates an acyl phosphate that can serve as an energy source.	ABSTRACT
52	62	Coenzyme A	chemical	The core enzyme phosphotransacylase (PTAC) recycles Coenzyme A and generates an acyl phosphate that can serve as an energy source.	ABSTRACT
80	94	acyl phosphate	chemical	The core enzyme phosphotransacylase (PTAC) recycles Coenzyme A and generates an acyl phosphate that can serve as an energy source.	ABSTRACT
4	8	PTAC	protein_type	The PTAC predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta).	ABSTRACT
39	52	metabolosomes	complex_assembly	The PTAC predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta).	ABSTRACT
54	58	PduL	protein_type	The PTAC predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta).	ABSTRACT
92	96	PTAC	protein_type	The PTAC predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta).	ABSTRACT
114	135	fermentative bacteria	taxonomy_domain	The PTAC predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta).	ABSTRACT
137	140	Pta	protein_type	The PTAC predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta).	ABSTRACT
36	40	PduL	protein_type	Here, we report two high-resolution PduL crystal structures with bound substrates.	ABSTRACT
41	59	crystal structures	evidence	Here, we report two high-resolution PduL crystal structures with bound substrates.	ABSTRACT
60	81	with bound substrates	protein_state	Here, we report two high-resolution PduL crystal structures with bound substrates.	ABSTRACT
4	8	PduL	protein_type	The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC.	ABSTRACT
9	13	fold	structure_element	The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC.	ABSTRACT
30	34	that	structure_element	The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC.	ABSTRACT
38	41	Pta	protein_type	The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC.	ABSTRACT
57	76	dimetal active site	site	The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC.	ABSTRACT
137	149	housekeeping	protein_state	The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC.	ABSTRACT
150	154	PTAC	protein_type	The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC.	ABSTRACT
13	17	PduL	protein_type	Accordingly, PduL and Pta exemplify functional, but not structural, convergent evolution.	ABSTRACT
22	25	Pta	protein_type	Accordingly, PduL and Pta exemplify functional, but not structural, convergent evolution.	ABSTRACT
4	8	PduL	protein_type	The PduL structure, in the context of the catalytic core, completes our understanding of the structural basis of cofactor recycling in the metabolosome lumen.	ABSTRACT
9	18	structure	evidence	The PduL structure, in the context of the catalytic core, completes our understanding of the structural basis of cofactor recycling in the metabolosome lumen.	ABSTRACT
139	151	metabolosome	complex_assembly	The PduL structure, in the context of the catalytic core, completes our understanding of the structural basis of cofactor recycling in the metabolosome lumen.	ABSTRACT
25	34	structure	evidence	This study describes the structure of a novel phosphotransacylase enzyme that facilitates the recycling of the essential cofactor acetyl-CoA within a bacterial organelle and discusses the properties of the enzyme's active site and how it is packaged into the organelle.	ABSTRACT
46	65	phosphotransacylase	protein_type	This study describes the structure of a novel phosphotransacylase enzyme that facilitates the recycling of the essential cofactor acetyl-CoA within a bacterial organelle and discusses the properties of the enzyme's active site and how it is packaged into the organelle.	ABSTRACT
130	140	acetyl-CoA	chemical	This study describes the structure of a novel phosphotransacylase enzyme that facilitates the recycling of the essential cofactor acetyl-CoA within a bacterial organelle and discusses the properties of the enzyme's active site and how it is packaged into the organelle.	ABSTRACT
150	159	bacterial	taxonomy_domain	This study describes the structure of a novel phosphotransacylase enzyme that facilitates the recycling of the essential cofactor acetyl-CoA within a bacterial organelle and discusses the properties of the enzyme's active site and how it is packaged into the organelle.	ABSTRACT
215	226	active site	site	This study describes the structure of a novel phosphotransacylase enzyme that facilitates the recycling of the essential cofactor acetyl-CoA within a bacterial organelle and discusses the properties of the enzyme's active site and how it is packaged into the organelle.	ABSTRACT
57	60	ATP	chemical	In metabolism, molecules with “high-energy” bonds (e.g., ATP and Acetyl~CoA) are critical for both catabolic and anabolic processes.	ABSTRACT
65	75	Acetyl~CoA	chemical	In metabolism, molecules with “high-energy” bonds (e.g., ATP and Acetyl~CoA) are critical for both catabolic and anabolic processes.	ABSTRACT
4	23	phosphotransacylase	protein_type	The phosphotransacylase (Pta) enzyme catalyzes the conversion between acyl-CoA and acyl-phosphate.	ABSTRACT
25	28	Pta	protein_type	The phosphotransacylase (Pta) enzyme catalyzes the conversion between acyl-CoA and acyl-phosphate.	ABSTRACT
70	78	acyl-CoA	chemical	The phosphotransacylase (Pta) enzyme catalyzes the conversion between acyl-CoA and acyl-phosphate.	ABSTRACT
83	97	acyl-phosphate	chemical	The phosphotransacylase (Pta) enzyme catalyzes the conversion between acyl-CoA and acyl-phosphate.	ABSTRACT
32	40	acyl-CoA	chemical	This reaction directly links an acyl-CoA with ATP generation via substrate-level phosphorylation, producing short-chain fatty acids (e.g., acetate), and also provides a path for short-chain fatty acids to enter central metabolism.	ABSTRACT
46	49	ATP	chemical	This reaction directly links an acyl-CoA with ATP generation via substrate-level phosphorylation, producing short-chain fatty acids (e.g., acetate), and also provides a path for short-chain fatty acids to enter central metabolism.	ABSTRACT
108	131	short-chain fatty acids	chemical	This reaction directly links an acyl-CoA with ATP generation via substrate-level phosphorylation, producing short-chain fatty acids (e.g., acetate), and also provides a path for short-chain fatty acids to enter central metabolism.	ABSTRACT
139	146	acetate	chemical	This reaction directly links an acyl-CoA with ATP generation via substrate-level phosphorylation, producing short-chain fatty acids (e.g., acetate), and also provides a path for short-chain fatty acids to enter central metabolism.	ABSTRACT
178	201	short-chain fatty acids	chemical	This reaction directly links an acyl-CoA with ATP generation via substrate-level phosphorylation, producing short-chain fatty acids (e.g., acetate), and also provides a path for short-chain fatty acids to enter central metabolism.	ABSTRACT
33	42	conserved	protein_state	Due to this key function, Pta is conserved across the bacterial kingdom.	ABSTRACT
54	71	bacterial kingdom	taxonomy_domain	Due to this key function, Pta is conserved across the bacterial kingdom.	ABSTRACT
24	43	phosphotransacylase	protein_type	Recently, a new type of phosphotransacylase was described that shares no evolutionary relation to Pta.	ABSTRACT
98	101	Pta	protein_type	Recently, a new type of phosphotransacylase was described that shares no evolutionary relation to Pta.	ABSTRACT
13	17	PduL	protein_type	This enzyme, PduL, is exclusively associated with organelles called bacterial microcompartments, which are used to catabolize various compounds.	ABSTRACT
22	33	exclusively	protein_state	This enzyme, PduL, is exclusively associated with organelles called bacterial microcompartments, which are used to catabolize various compounds.	ABSTRACT
68	77	bacterial	taxonomy_domain	This enzyme, PduL, is exclusively associated with organelles called bacterial microcompartments, which are used to catabolize various compounds.	ABSTRACT
78	95	microcompartments	complex_assembly	This enzyme, PduL, is exclusively associated with organelles called bacterial microcompartments, which are used to catabolize various compounds.	ABSTRACT
14	18	PduL	protein_type	Not only does PduL facilitate substrate level phosphorylation, but it also is critical for cofactor recycling within, and product efflux from, the organelle.	ABSTRACT
3	9	solved	experimental_method	We solved the structure of this convergent phosphotransacylase and show that it is completely structurally different from Pta, including its active site architecture.	ABSTRACT
14	23	structure	evidence	We solved the structure of this convergent phosphotransacylase and show that it is completely structurally different from Pta, including its active site architecture.	ABSTRACT
32	42	convergent	protein_state	We solved the structure of this convergent phosphotransacylase and show that it is completely structurally different from Pta, including its active site architecture.	ABSTRACT
43	62	phosphotransacylase	protein_type	We solved the structure of this convergent phosphotransacylase and show that it is completely structurally different from Pta, including its active site architecture.	ABSTRACT
122	125	Pta	protein_type	We solved the structure of this convergent phosphotransacylase and show that it is completely structurally different from Pta, including its active site architecture.	ABSTRACT
141	152	active site	site	We solved the structure of this convergent phosphotransacylase and show that it is completely structurally different from Pta, including its active site architecture.	ABSTRACT
0	9	Bacterial	taxonomy_domain	Bacterial Microcompartments (BMCs) are organelles that encapsulate enzymes for sequential biochemical reactions within a protein shell.	INTRO
10	27	Microcompartments	complex_assembly	Bacterial Microcompartments (BMCs) are organelles that encapsulate enzymes for sequential biochemical reactions within a protein shell.	INTRO
29	33	BMCs	complex_assembly	Bacterial Microcompartments (BMCs) are organelles that encapsulate enzymes for sequential biochemical reactions within a protein shell.	INTRO
129	134	shell	structure_element	Bacterial Microcompartments (BMCs) are organelles that encapsulate enzymes for sequential biochemical reactions within a protein shell.	INTRO
4	9	shell	structure_element	The shell is typically composed of three types of protein subunits, which form either hexagonal (BMC-H and BMC-T) or pentagonal (BMC-P) tiles that assemble into a polyhedral shell.	INTRO
86	95	hexagonal	protein_state	The shell is typically composed of three types of protein subunits, which form either hexagonal (BMC-H and BMC-T) or pentagonal (BMC-P) tiles that assemble into a polyhedral shell.	INTRO
97	102	BMC-H	complex_assembly	The shell is typically composed of three types of protein subunits, which form either hexagonal (BMC-H and BMC-T) or pentagonal (BMC-P) tiles that assemble into a polyhedral shell.	INTRO
107	112	BMC-T	complex_assembly	The shell is typically composed of three types of protein subunits, which form either hexagonal (BMC-H and BMC-T) or pentagonal (BMC-P) tiles that assemble into a polyhedral shell.	INTRO
117	127	pentagonal	protein_state	The shell is typically composed of three types of protein subunits, which form either hexagonal (BMC-H and BMC-T) or pentagonal (BMC-P) tiles that assemble into a polyhedral shell.	INTRO
129	134	BMC-P	complex_assembly	The shell is typically composed of three types of protein subunits, which form either hexagonal (BMC-H and BMC-T) or pentagonal (BMC-P) tiles that assemble into a polyhedral shell.	INTRO
163	173	polyhedral	protein_state	The shell is typically composed of three types of protein subunits, which form either hexagonal (BMC-H and BMC-T) or pentagonal (BMC-P) tiles that assemble into a polyhedral shell.	INTRO
174	179	shell	structure_element	The shell is typically composed of three types of protein subunits, which form either hexagonal (BMC-H and BMC-T) or pentagonal (BMC-P) tiles that assemble into a polyhedral shell.	INTRO
18	23	shell	structure_element	The facets of the shell are composed primarily of hexamers that are typically perforated by pores lined with highly conserved, polar residues that presumably function as the conduits for metabolites into and out of the shell.	INTRO
50	58	hexamers	oligomeric_state	The facets of the shell are composed primarily of hexamers that are typically perforated by pores lined with highly conserved, polar residues that presumably function as the conduits for metabolites into and out of the shell.	INTRO
92	97	pores	site	The facets of the shell are composed primarily of hexamers that are typically perforated by pores lined with highly conserved, polar residues that presumably function as the conduits for metabolites into and out of the shell.	INTRO
109	125	highly conserved	protein_state	The facets of the shell are composed primarily of hexamers that are typically perforated by pores lined with highly conserved, polar residues that presumably function as the conduits for metabolites into and out of the shell.	INTRO
127	132	polar	protein_state	The facets of the shell are composed primarily of hexamers that are typically perforated by pores lined with highly conserved, polar residues that presumably function as the conduits for metabolites into and out of the shell.	INTRO
133	141	residues	structure_element	The facets of the shell are composed primarily of hexamers that are typically perforated by pores lined with highly conserved, polar residues that presumably function as the conduits for metabolites into and out of the shell.	INTRO
219	224	shell	structure_element	The facets of the shell are composed primarily of hexamers that are typically perforated by pores lined with highly conserved, polar residues that presumably function as the conduits for metabolites into and out of the shell.	INTRO
4	57	vitamin B12-dependent propanediol-utilizing (PDU) BMC	complex_assembly	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
106	115	catabolic	protein_state	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
116	120	BMCs	complex_assembly	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
191	203	ethanolamine	chemical	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
205	212	choline	chemical	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
214	220	fucose	chemical	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
222	230	rhamnose	chemical	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
236	243	ethanol	chemical	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
276	284	aldehyde	chemical	The vitamin B12-dependent propanediol-utilizing (PDU) BMC was one of the first functionally characterized catabolic BMCs; subsequently, other types have been implicated in the degradation of ethanolamine, choline, fucose, rhamnose, and ethanol, all of which produce different aldehyde intermediates (Table 1).	INTRO
15	36	bioinformatic studies	experimental_method	More recently, bioinformatic studies have demonstrated the widespread distribution of BMCs among diverse bacterial phyla and grouped them into 23 different functional types.	INTRO
86	90	BMCs	complex_assembly	More recently, bioinformatic studies have demonstrated the widespread distribution of BMCs among diverse bacterial phyla and grouped them into 23 different functional types.	INTRO
105	120	bacterial phyla	taxonomy_domain	More recently, bioinformatic studies have demonstrated the widespread distribution of BMCs among diverse bacterial phyla and grouped them into 23 different functional types.	INTRO
45	54	catabolic	protein_state	The reactions carried out in the majority of catabolic BMCs (also known as metabolosomes) fit a generalized biochemical paradigm for the oxidation of aldehydes (Fig 1).	INTRO
55	59	BMCs	complex_assembly	The reactions carried out in the majority of catabolic BMCs (also known as metabolosomes) fit a generalized biochemical paradigm for the oxidation of aldehydes (Fig 1).	INTRO
75	88	metabolosomes	complex_assembly	The reactions carried out in the majority of catabolic BMCs (also known as metabolosomes) fit a generalized biochemical paradigm for the oxidation of aldehydes (Fig 1).	INTRO
150	159	aldehydes	chemical	The reactions carried out in the majority of catabolic BMCs (also known as metabolosomes) fit a generalized biochemical paradigm for the oxidation of aldehydes (Fig 1).	INTRO
16	19	BMC	complex_assembly	This involves a BMC-encapsulated signature enzyme that generates a toxic and/or volatile aldehyde that the BMC shell sequesters from the cytosol.	INTRO
89	97	aldehyde	chemical	This involves a BMC-encapsulated signature enzyme that generates a toxic and/or volatile aldehyde that the BMC shell sequesters from the cytosol.	INTRO
107	110	BMC	complex_assembly	This involves a BMC-encapsulated signature enzyme that generates a toxic and/or volatile aldehyde that the BMC shell sequesters from the cytosol.	INTRO
111	116	shell	structure_element	This involves a BMC-encapsulated signature enzyme that generates a toxic and/or volatile aldehyde that the BMC shell sequesters from the cytosol.	INTRO
4	12	aldehyde	chemical	The aldehyde is subsequently converted into an acyl-CoA by aldehyde dehydrogenase, which uses NAD+ and CoA as cofactors.	INTRO
47	55	acyl-CoA	chemical	The aldehyde is subsequently converted into an acyl-CoA by aldehyde dehydrogenase, which uses NAD+ and CoA as cofactors.	INTRO
59	81	aldehyde dehydrogenase	protein_type	The aldehyde is subsequently converted into an acyl-CoA by aldehyde dehydrogenase, which uses NAD+ and CoA as cofactors.	INTRO
94	98	NAD+	chemical	The aldehyde is subsequently converted into an acyl-CoA by aldehyde dehydrogenase, which uses NAD+ and CoA as cofactors.	INTRO
103	106	CoA	chemical	The aldehyde is subsequently converted into an acyl-CoA by aldehyde dehydrogenase, which uses NAD+ and CoA as cofactors.	INTRO
73	86	protein shell	structure_element	These two cofactors are relatively large, and their diffusion across the protein shell is thought to be restricted, necessitating their regeneration within the BMC lumen.	INTRO
160	163	BMC	complex_assembly	These two cofactors are relatively large, and their diffusion across the protein shell is thought to be restricted, necessitating their regeneration within the BMC lumen.	INTRO
0	4	NAD+	chemical	NAD+ is recycled via alcohol dehydrogenase, and CoA is recycled via phosphotransacetylase (PTAC) (Fig 1).	INTRO
21	42	alcohol dehydrogenase	protein_type	NAD+ is recycled via alcohol dehydrogenase, and CoA is recycled via phosphotransacetylase (PTAC) (Fig 1).	INTRO
48	51	CoA	chemical	NAD+ is recycled via alcohol dehydrogenase, and CoA is recycled via phosphotransacetylase (PTAC) (Fig 1).	INTRO
68	89	phosphotransacetylase	protein_type	NAD+ is recycled via alcohol dehydrogenase, and CoA is recycled via phosphotransacetylase (PTAC) (Fig 1).	INTRO
91	95	PTAC	protein_type	NAD+ is recycled via alcohol dehydrogenase, and CoA is recycled via phosphotransacetylase (PTAC) (Fig 1).	INTRO
25	28	BMC	complex_assembly	The final product of the BMC, an acyl-phosphate, can then be used to generate ATP via acyl kinase, or revert back to acyl-CoA by Pta for biosynthesis.	INTRO
33	47	acyl-phosphate	chemical	The final product of the BMC, an acyl-phosphate, can then be used to generate ATP via acyl kinase, or revert back to acyl-CoA by Pta for biosynthesis.	INTRO
78	81	ATP	chemical	The final product of the BMC, an acyl-phosphate, can then be used to generate ATP via acyl kinase, or revert back to acyl-CoA by Pta for biosynthesis.	INTRO
86	97	acyl kinase	protein_type	The final product of the BMC, an acyl-phosphate, can then be used to generate ATP via acyl kinase, or revert back to acyl-CoA by Pta for biosynthesis.	INTRO
117	125	acyl-CoA	chemical	The final product of the BMC, an acyl-phosphate, can then be used to generate ATP via acyl kinase, or revert back to acyl-CoA by Pta for biosynthesis.	INTRO
129	132	Pta	protein_type	The final product of the BMC, an acyl-phosphate, can then be used to generate ATP via acyl kinase, or revert back to acyl-CoA by Pta for biosynthesis.	INTRO
18	53	aldehyde and alcohol dehydrogenases	protein_type	Collectively, the aldehyde and alcohol dehydrogenases, as well as the PTAC, constitute the common metabolosome core.	INTRO
70	74	PTAC	protein_type	Collectively, the aldehyde and alcohol dehydrogenases, as well as the PTAC, constitute the common metabolosome core.	INTRO
98	110	metabolosome	complex_assembly	Collectively, the aldehyde and alcohol dehydrogenases, as well as the PTAC, constitute the common metabolosome core.	INTRO
29	47	aldehyde-degrading	protein_state	General biochemical model of aldehyde-degrading BMCs (metabolosomes) illustrating the common metabolosome core enzymes and reactions.	FIG
48	52	BMCs	complex_assembly	General biochemical model of aldehyde-degrading BMCs (metabolosomes) illustrating the common metabolosome core enzymes and reactions.	FIG
54	67	metabolosomes	complex_assembly	General biochemical model of aldehyde-degrading BMCs (metabolosomes) illustrating the common metabolosome core enzymes and reactions.	FIG
93	105	metabolosome	complex_assembly	General biochemical model of aldehyde-degrading BMCs (metabolosomes) illustrating the common metabolosome core enzymes and reactions.	FIG
39	43	PTAC	protein_type	Substrates and cofactors involving the PTAC reaction are shown in red; other substrates and enzymes are shown in black, and other cofactors are shown in gray.	FIG
28	37	catabolic	protein_state	Characterized and predicted catabolic BMC (metabolosome) types that represent the aldehyde-degrading paradigm (for definition of types see Kerfeld and Erbilgin).	TABLE
38	41	BMC	complex_assembly	Characterized and predicted catabolic BMC (metabolosome) types that represent the aldehyde-degrading paradigm (for definition of types see Kerfeld and Erbilgin).	TABLE
43	55	metabolosome	complex_assembly	Characterized and predicted catabolic BMC (metabolosome) types that represent the aldehyde-degrading paradigm (for definition of types see Kerfeld and Erbilgin).	TABLE
82	90	aldehyde	chemical	Characterized and predicted catabolic BMC (metabolosome) types that represent the aldehyde-degrading paradigm (for definition of types see Kerfeld and Erbilgin).	TABLE
5	9	PTAC	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
27	35	Aldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
38	41	PDU	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
43	47	PduL	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
48	63	propionaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
66	70	EUT1	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
71	78	PTA_PTB	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
79	91	acetaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
94	98	EUT2	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
99	103	PduL	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
104	116	acetaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
119	122	ETU	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
128	140	acetaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
143	151	GRM1/CUT	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
152	156	PduL	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
157	169	acetaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
172	176	GRM2	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
177	181	PduL	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
182	194	acetaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
197	204	GRM3*,4	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
205	209	PduL	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
210	225	propionaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
228	236	GRM5/GRP	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
237	241	PduL	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
242	257	propionaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
260	263	PVM	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
265	269	PduL	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
270	282	lactaldehyde	chemical	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
285	291	RMM1,2	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
307	310	SPU	complex_assembly	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
311	315	PduL	protein_type	"Name	PTAC Type	Sequestered Aldehyde	 	PDU*	PduL	propionaldehyde	 	EUT1	PTA_PTB	acetaldehyde	 	EUT2	PduL	acetaldehyde	 	ETU	None	acetaldehyde	 	GRM1/CUT	PduL	acetaldehyde	 	GRM2	PduL	acetaldehyde	 	GRM3*,4	PduL	propionaldehyde	 	GRM5/GRP	PduL	propionaldehyde	 	PVM*	PduL	lactaldehyde	 	RMM1,2	None	unknown	 	SPU	PduL	unknown	 	"	TABLE
2	6	PduL	protein_type	* PduL from these functional types of metabolosomes were purified in this study.	TABLE
38	51	metabolosomes	complex_assembly	* PduL from these functional types of metabolosomes were purified in this study.	TABLE
51	54	BMC	complex_assembly	The activities of core enzymes are not confined to BMC-associated functions: aldehyde and alcohol dehydrogenases are utilized in diverse metabolic reactions, and PTAC catalyzes a key biochemical reaction in the process of obtaining energy during fermentation.	INTRO
77	112	aldehyde and alcohol dehydrogenases	protein_type	The activities of core enzymes are not confined to BMC-associated functions: aldehyde and alcohol dehydrogenases are utilized in diverse metabolic reactions, and PTAC catalyzes a key biochemical reaction in the process of obtaining energy during fermentation.	INTRO
162	166	PTAC	protein_type	The activities of core enzymes are not confined to BMC-associated functions: aldehyde and alcohol dehydrogenases are utilized in diverse metabolic reactions, and PTAC catalyzes a key biochemical reaction in the process of obtaining energy during fermentation.	INTRO
31	35	PTAC	protein_type	The concerted functioning of a PTAC and an acetate kinase (Ack) is crucial for ATP generation in the fermentation of pyruvate to acetate (see Reactions 1 and 2).	INTRO
43	57	acetate kinase	protein_type	The concerted functioning of a PTAC and an acetate kinase (Ack) is crucial for ATP generation in the fermentation of pyruvate to acetate (see Reactions 1 and 2).	INTRO
59	62	Ack	protein_type	The concerted functioning of a PTAC and an acetate kinase (Ack) is crucial for ATP generation in the fermentation of pyruvate to acetate (see Reactions 1 and 2).	INTRO
79	82	ATP	chemical	The concerted functioning of a PTAC and an acetate kinase (Ack) is crucial for ATP generation in the fermentation of pyruvate to acetate (see Reactions 1 and 2).	INTRO
117	125	pyruvate	chemical	The concerted functioning of a PTAC and an acetate kinase (Ack) is crucial for ATP generation in the fermentation of pyruvate to acetate (see Reactions 1 and 2).	INTRO
129	136	acetate	chemical	The concerted functioning of a PTAC and an acetate kinase (Ack) is crucial for ATP generation in the fermentation of pyruvate to acetate (see Reactions 1 and 2).	INTRO
45	67	fermentative organisms	taxonomy_domain	Both enzymes are, however, not restricted to fermentative organisms.	INTRO
56	63	acetate	chemical	They can also work in the reverse direction to activate acetate to the CoA-thioester.	INTRO
71	84	CoA-thioester	chemical	They can also work in the reverse direction to activate acetate to the CoA-thioester.	INTRO
68	76	archaeal	taxonomy_domain	This occurs, for example, during acetoclastic methanogenesis in the archaeal Methanosarcina species.	INTRO
77	99	Methanosarcina species	taxonomy_domain	This occurs, for example, during acetoclastic methanogenesis in the archaeal Methanosarcina species.	INTRO
13	25	acetyl-S-CoA	chemical	 Reaction 1: acetyl-S-CoA + Pi ←→ acetyl phosphate + CoA-SH (PTAC)	INTRO
28	30	Pi	chemical	 Reaction 1: acetyl-S-CoA + Pi ←→ acetyl phosphate + CoA-SH (PTAC)	INTRO
34	50	acetyl phosphate	chemical	 Reaction 1: acetyl-S-CoA + Pi ←→ acetyl phosphate + CoA-SH (PTAC)	INTRO
53	59	CoA-SH	chemical	 Reaction 1: acetyl-S-CoA + Pi ←→ acetyl phosphate + CoA-SH (PTAC)	INTRO
61	65	PTAC	protein_type	 Reaction 1: acetyl-S-CoA + Pi ←→ acetyl phosphate + CoA-SH (PTAC)	INTRO
13	29	acetyl phosphate	chemical	 Reaction 2: acetyl phosphate + ADP ←→ acetate + ATP (Ack)	INTRO
32	35	ADP	chemical	 Reaction 2: acetyl phosphate + ADP ←→ acetate + ATP (Ack)	INTRO
39	46	acetate	chemical	 Reaction 2: acetyl phosphate + ADP ←→ acetate + ATP (Ack)	INTRO
49	52	ATP	chemical	 Reaction 2: acetyl phosphate + ADP ←→ acetate + ATP (Ack)	INTRO
54	57	Ack	protein_type	 Reaction 2: acetyl phosphate + ADP ←→ acetate + ATP (Ack)	INTRO
14	18	PTAC	protein_type	The canonical PTAC, Pta, is an ancient enzyme found in some eukaryotes and archaea, and widespread among the bacteria; 90% of the bacterial genomes in the Integrated Microbial Genomes database contain a gene encoding the PTA_PTB phosphotransacylase (Pfam domain PF01515).	INTRO
20	23	Pta	protein_type	The canonical PTAC, Pta, is an ancient enzyme found in some eukaryotes and archaea, and widespread among the bacteria; 90% of the bacterial genomes in the Integrated Microbial Genomes database contain a gene encoding the PTA_PTB phosphotransacylase (Pfam domain PF01515).	INTRO
60	70	eukaryotes	taxonomy_domain	The canonical PTAC, Pta, is an ancient enzyme found in some eukaryotes and archaea, and widespread among the bacteria; 90% of the bacterial genomes in the Integrated Microbial Genomes database contain a gene encoding the PTA_PTB phosphotransacylase (Pfam domain PF01515).	INTRO
75	82	archaea	taxonomy_domain	The canonical PTAC, Pta, is an ancient enzyme found in some eukaryotes and archaea, and widespread among the bacteria; 90% of the bacterial genomes in the Integrated Microbial Genomes database contain a gene encoding the PTA_PTB phosphotransacylase (Pfam domain PF01515).	INTRO
109	117	bacteria	taxonomy_domain	The canonical PTAC, Pta, is an ancient enzyme found in some eukaryotes and archaea, and widespread among the bacteria; 90% of the bacterial genomes in the Integrated Microbial Genomes database contain a gene encoding the PTA_PTB phosphotransacylase (Pfam domain PF01515).	INTRO
130	139	bacterial	taxonomy_domain	The canonical PTAC, Pta, is an ancient enzyme found in some eukaryotes and archaea, and widespread among the bacteria; 90% of the bacterial genomes in the Integrated Microbial Genomes database contain a gene encoding the PTA_PTB phosphotransacylase (Pfam domain PF01515).	INTRO
221	248	PTA_PTB phosphotransacylase	protein_type	The canonical PTAC, Pta, is an ancient enzyme found in some eukaryotes and archaea, and widespread among the bacteria; 90% of the bacterial genomes in the Integrated Microbial Genomes database contain a gene encoding the PTA_PTB phosphotransacylase (Pfam domain PF01515).	INTRO
262	269	PF01515	structure_element	The canonical PTAC, Pta, is an ancient enzyme found in some eukaryotes and archaea, and widespread among the bacteria; 90% of the bacterial genomes in the Integrated Microbial Genomes database contain a gene encoding the PTA_PTB phosphotransacylase (Pfam domain PF01515).	INTRO
0	3	Pta	protein_type	Pta has been extensively characterized due to its key role in fermentation.	INTRO
32	36	PTAC	protein_type	More recently, a second type of PTAC without any sequence homology to Pta was identified.	INTRO
70	73	Pta	protein_type	More recently, a second type of PTAC without any sequence homology to Pta was identified.	INTRO
14	18	PduL	protein_type	This protein, PduL (Pfam domain PF06130), was shown to catalyze the conversion of propionyl-CoA to propionyl-phosphate and is associated with a BMC involved in propanediol utilization, the PDU BMC.	INTRO
32	39	PF06130	structure_element	This protein, PduL (Pfam domain PF06130), was shown to catalyze the conversion of propionyl-CoA to propionyl-phosphate and is associated with a BMC involved in propanediol utilization, the PDU BMC.	INTRO
82	95	propionyl-CoA	chemical	This protein, PduL (Pfam domain PF06130), was shown to catalyze the conversion of propionyl-CoA to propionyl-phosphate and is associated with a BMC involved in propanediol utilization, the PDU BMC.	INTRO
99	118	propionyl-phosphate	chemical	This protein, PduL (Pfam domain PF06130), was shown to catalyze the conversion of propionyl-CoA to propionyl-phosphate and is associated with a BMC involved in propanediol utilization, the PDU BMC.	INTRO
144	147	BMC	complex_assembly	This protein, PduL (Pfam domain PF06130), was shown to catalyze the conversion of propionyl-CoA to propionyl-phosphate and is associated with a BMC involved in propanediol utilization, the PDU BMC.	INTRO
189	196	PDU BMC	complex_assembly	This protein, PduL (Pfam domain PF06130), was shown to catalyze the conversion of propionyl-CoA to propionyl-phosphate and is associated with a BMC involved in propanediol utilization, the PDU BMC.	INTRO
5	9	pduL	gene	Both pduL and pta genes can be found in genetic loci of functionally distinct BMCs, although the PduL type is much more prevalent, being found in all but one type of metabolosome locus: EUT1 (Table 1).	INTRO
14	17	pta	gene	Both pduL and pta genes can be found in genetic loci of functionally distinct BMCs, although the PduL type is much more prevalent, being found in all but one type of metabolosome locus: EUT1 (Table 1).	INTRO
78	82	BMCs	complex_assembly	Both pduL and pta genes can be found in genetic loci of functionally distinct BMCs, although the PduL type is much more prevalent, being found in all but one type of metabolosome locus: EUT1 (Table 1).	INTRO
97	101	PduL	protein_type	Both pduL and pta genes can be found in genetic loci of functionally distinct BMCs, although the PduL type is much more prevalent, being found in all but one type of metabolosome locus: EUT1 (Table 1).	INTRO
166	184	metabolosome locus	gene	Both pduL and pta genes can be found in genetic loci of functionally distinct BMCs, although the PduL type is much more prevalent, being found in all but one type of metabolosome locus: EUT1 (Table 1).	INTRO
186	190	EUT1	gene	Both pduL and pta genes can be found in genetic loci of functionally distinct BMCs, although the PduL type is much more prevalent, being found in all but one type of metabolosome locus: EUT1 (Table 1).	INTRO
86	93	PF06130	structure_element	Furthermore, in the Integrated Microbial Genomes Database, 91% of genomes that encode PF06130 also encode genes for shell proteins.	INTRO
70	88	aldehyde-oxidizing	protein_state	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
89	102	metabolosomes	complex_assembly	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
104	108	PduL	protein_type	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
197	200	Pta	protein_type	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
246	256	acetyl-CoA	chemical	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
258	262	PduL	protein_type	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
272	279	PDU BMC	complex_assembly	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
283	302	Salmonella enterica	species	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
310	323	propionyl-CoA	chemical	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
329	339	acetyl-CoA	chemical	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
363	367	PduL	protein_type	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
402	406	BMCs	complex_assembly	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
450	453	CoA	chemical	As a member of the core biochemical machinery of functionally diverse aldehyde-oxidizing metabolosomes, PduL must have a certain level of substrate plasticity (see Table 1) that is not required of Pta, which has generally been observed to prefer acetyl-CoA. PduL from the PDU BMC of Salmonella enterica favors propionyl-CoA over acetyl-CoA, and it is likely that PduL orthologs in functionally diverse BMCs would have substrate preferences for other CoA derivatives.	INTRO
31	45	BMC-associated	protein_state	Another distinctive feature of BMC-associated PduL homologs is an N-terminal encapsulation peptide (EP) that is thought to “target” proteins for encapsulation by the BMC shell.	INTRO
46	50	PduL	protein_type	Another distinctive feature of BMC-associated PduL homologs is an N-terminal encapsulation peptide (EP) that is thought to “target” proteins for encapsulation by the BMC shell.	INTRO
77	98	encapsulation peptide	structure_element	Another distinctive feature of BMC-associated PduL homologs is an N-terminal encapsulation peptide (EP) that is thought to “target” proteins for encapsulation by the BMC shell.	INTRO
100	102	EP	structure_element	Another distinctive feature of BMC-associated PduL homologs is an N-terminal encapsulation peptide (EP) that is thought to “target” proteins for encapsulation by the BMC shell.	INTRO
166	169	BMC	complex_assembly	Another distinctive feature of BMC-associated PduL homologs is an N-terminal encapsulation peptide (EP) that is thought to “target” proteins for encapsulation by the BMC shell.	INTRO
170	175	shell	structure_element	Another distinctive feature of BMC-associated PduL homologs is an N-terminal encapsulation peptide (EP) that is thought to “target” proteins for encapsulation by the BMC shell.	INTRO
0	3	EPs	structure_element	EPs are frequently found on BMC-associated proteins and have been shown to interact with shell proteins.	INTRO
28	51	BMC-associated proteins	protein_type	EPs are frequently found on BMC-associated proteins and have been shown to interact with shell proteins.	INTRO
0	3	EPs	structure_element	EPs have also been observed to cause proteins to aggregate, and this has recently been suggested to be functionally relevant as an initial step in metabolosome assembly, in which a multifunctional protein core is formed, around which the shell assembles.	INTRO
147	159	metabolosome	complex_assembly	EPs have also been observed to cause proteins to aggregate, and this has recently been suggested to be functionally relevant as an initial step in metabolosome assembly, in which a multifunctional protein core is formed, around which the shell assembles.	INTRO
238	243	shell	structure_element	EPs have also been observed to cause proteins to aggregate, and this has recently been suggested to be functionally relevant as an initial step in metabolosome assembly, in which a multifunctional protein core is formed, around which the shell assembles.	INTRO
20	32	metabolosome	complex_assembly	Of the three common metabolosome core enzymes, crystal structures are available for both the alcohol and aldehyde dehydrogenases.	INTRO
47	65	crystal structures	evidence	Of the three common metabolosome core enzymes, crystal structures are available for both the alcohol and aldehyde dehydrogenases.	INTRO
93	128	alcohol and aldehyde dehydrogenases	protein_type	Of the three common metabolosome core enzymes, crystal structures are available for both the alcohol and aldehyde dehydrogenases.	INTRO
17	26	structure	evidence	In contrast, the structure of PduL, the PTAC found in the vast majority of catabolic BMCs, has not been determined.	INTRO
30	34	PduL	protein_type	In contrast, the structure of PduL, the PTAC found in the vast majority of catabolic BMCs, has not been determined.	INTRO
40	44	PTAC	protein_type	In contrast, the structure of PduL, the PTAC found in the vast majority of catabolic BMCs, has not been determined.	INTRO
75	84	catabolic	protein_state	In contrast, the structure of PduL, the PTAC found in the vast majority of catabolic BMCs, has not been determined.	INTRO
85	89	BMCs	complex_assembly	In contrast, the structure of PduL, the PTAC found in the vast majority of catabolic BMCs, has not been determined.	INTRO
44	56	metabolosome	complex_assembly	This is a major gap in our understanding of metabolosome-encapsulated biochemistry and cofactor recycling.	INTRO
66	69	BMC	complex_assembly	Moreover, it will be useful for guiding efforts to engineer novel BMC cores for biotechnological applications.	INTRO
25	29	PduL	protein_type	The primary structure of PduL homologs is subdivided into two PF06130 domains, each roughly 80 residues in length.	INTRO
62	69	PF06130	structure_element	The primary structure of PduL homologs is subdivided into two PF06130 domains, each roughly 80 residues in length.	INTRO
92	113	80 residues in length	residue_range	The primary structure of PduL homologs is subdivided into two PF06130 domains, each roughly 80 residues in length.	INTRO
44	51	PF06130	structure_element	No available protein structures contain the PF06130 domain, and homology searches using the primary structure of PduL do not return any significant results that would allow prediction of the structure.	INTRO
64	81	homology searches	experimental_method	No available protein structures contain the PF06130 domain, and homology searches using the primary structure of PduL do not return any significant results that would allow prediction of the structure.	INTRO
113	117	PduL	protein_type	No available protein structures contain the PF06130 domain, and homology searches using the primary structure of PduL do not return any significant results that would allow prediction of the structure.	INTRO
191	200	structure	evidence	No available protein structures contain the PF06130 domain, and homology searches using the primary structure of PduL do not return any significant results that would allow prediction of the structure.	INTRO
33	37	PduL	protein_type	Moreover, the evident novelty of PduL makes its structure interesting in the context of convergent evolution of PTAC function; to-date, only the Pta active site and catalytic mechanism is known.	INTRO
48	57	structure	evidence	Moreover, the evident novelty of PduL makes its structure interesting in the context of convergent evolution of PTAC function; to-date, only the Pta active site and catalytic mechanism is known.	INTRO
112	116	PTAC	protein_type	Moreover, the evident novelty of PduL makes its structure interesting in the context of convergent evolution of PTAC function; to-date, only the Pta active site and catalytic mechanism is known.	INTRO
145	148	Pta	protein_type	Moreover, the evident novelty of PduL makes its structure interesting in the context of convergent evolution of PTAC function; to-date, only the Pta active site and catalytic mechanism is known.	INTRO
149	160	active site	site	Moreover, the evident novelty of PduL makes its structure interesting in the context of convergent evolution of PTAC function; to-date, only the Pta active site and catalytic mechanism is known.	INTRO
31	49	crystal structures	evidence	Here we report high-resolution crystal structures of a PduL-type PTAC in both CoA- and phosphate-bound forms, completing our understanding of the structural basis of catalysis by the metabolosome common core enzymes.	INTRO
55	69	PduL-type PTAC	protein_type	Here we report high-resolution crystal structures of a PduL-type PTAC in both CoA- and phosphate-bound forms, completing our understanding of the structural basis of catalysis by the metabolosome common core enzymes.	INTRO
78	82	CoA-	protein_state	Here we report high-resolution crystal structures of a PduL-type PTAC in both CoA- and phosphate-bound forms, completing our understanding of the structural basis of catalysis by the metabolosome common core enzymes.	INTRO
87	102	phosphate-bound	protein_state	Here we report high-resolution crystal structures of a PduL-type PTAC in both CoA- and phosphate-bound forms, completing our understanding of the structural basis of catalysis by the metabolosome common core enzymes.	INTRO
183	195	metabolosome	complex_assembly	Here we report high-resolution crystal structures of a PduL-type PTAC in both CoA- and phosphate-bound forms, completing our understanding of the structural basis of catalysis by the metabolosome common core enzymes.	INTRO
80	83	Pta	protein_type	We propose a catalytic mechanism analogous but yet distinct from the ubiquitous Pta enzyme, highlighting the functional convergence of two enzymes with completely different structures and metal requirements.	INTRO
65	69	PduL	protein_type	We also investigate the quaternary structures of three different PduL homologs and situate our findings in the context of organelle biogenesis in functionally diverse BMCs.	INTRO
167	171	BMCs	complex_assembly	We also investigate the quaternary structures of three different PduL homologs and situate our findings in the context of organelle biogenesis in functionally diverse BMCs.	INTRO
0	23	Structure Determination	experimental_method	Structure Determination of PduL	RESULTS
27	31	PduL	protein_type	Structure Determination of PduL	RESULTS
3	34	cloned, expressed, and purified	experimental_method	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
51	55	PduL	protein_type	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
92	96	BMCs	complex_assembly	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
130	139	pdu locus	gene	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
143	170	S. enterica Typhimurium LT2	species	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
172	177	sPduL	protein	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
212	221	pvm locus	gene	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
225	249	Planctomyces limnophilus	species	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
251	256	pPduL	protein	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
272	282	grm3 locus	gene	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
286	319	Rhodopseudomonas palustris BisB18	species	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
321	326	rPduL	protein	We cloned, expressed, and purified three different PduL homologs from functionally distinct BMCs (Table 1): from the well-studied pdu locus in S. enterica Typhimurium LT2 (sPduL), from the recently characterized pvm locus in Planctomyces limnophilus (pPduL), and from the grm3 locus in Rhodopseudomonas palustris BisB18 (rPduL).	RESULTS
16	27	full-length	protein_state	While purifying full-length sPduL, we observed a tendency to aggregation as described previously, with a large fraction of the expressed protein found in the insoluble fraction in a white, cake-like pellet.	RESULTS
28	33	sPduL	protein	While purifying full-length sPduL, we observed a tendency to aggregation as described previously, with a large fraction of the expressed protein found in the insoluble fraction in a white, cake-like pellet.	RESULTS
18	26	removing	experimental_method	Remarkably, after removing the N-terminal putative EP (27 amino acids), most of the sPduLΔEP protein was in the soluble fraction upon cell lysis.	RESULTS
51	53	EP	structure_element	Remarkably, after removing the N-terminal putative EP (27 amino acids), most of the sPduLΔEP protein was in the soluble fraction upon cell lysis.	RESULTS
55	69	27 amino acids	residue_range	Remarkably, after removing the N-terminal putative EP (27 amino acids), most of the sPduLΔEP protein was in the soluble fraction upon cell lysis.	RESULTS
84	92	sPduLΔEP	mutant	Remarkably, after removing the N-terminal putative EP (27 amino acids), most of the sPduLΔEP protein was in the soluble fraction upon cell lysis.	RESULTS
52	57	pPduL	protein	Similar differences in solubility were observed for pPduL and rPduL when comparing EP-truncated forms to the full-length protein, but none were quite as dramatic as for sPduL. We confirmed that all homologs were active (S1a and S1b Fig).	RESULTS
62	67	rPduL	protein	Similar differences in solubility were observed for pPduL and rPduL when comparing EP-truncated forms to the full-length protein, but none were quite as dramatic as for sPduL. We confirmed that all homologs were active (S1a and S1b Fig).	RESULTS
83	95	EP-truncated	protein_state	Similar differences in solubility were observed for pPduL and rPduL when comparing EP-truncated forms to the full-length protein, but none were quite as dramatic as for sPduL. We confirmed that all homologs were active (S1a and S1b Fig).	RESULTS
109	120	full-length	protein_state	Similar differences in solubility were observed for pPduL and rPduL when comparing EP-truncated forms to the full-length protein, but none were quite as dramatic as for sPduL. We confirmed that all homologs were active (S1a and S1b Fig).	RESULTS
169	174	sPduL	protein	Similar differences in solubility were observed for pPduL and rPduL when comparing EP-truncated forms to the full-length protein, but none were quite as dramatic as for sPduL. We confirmed that all homologs were active (S1a and S1b Fig).	RESULTS
212	218	active	protein_state	Similar differences in solubility were observed for pPduL and rPduL when comparing EP-truncated forms to the full-length protein, but none were quite as dramatic as for sPduL. We confirmed that all homologs were active (S1a and S1b Fig).	RESULTS
41	69	diffraction-quality crystals	evidence	Among these, we were only able to obtain diffraction-quality crystals of rPduL after removing the N-terminal putative EP (33 amino acids, also see Fig 2a) (rPduLΔEP).	RESULTS
73	78	rPduL	protein	Among these, we were only able to obtain diffraction-quality crystals of rPduL after removing the N-terminal putative EP (33 amino acids, also see Fig 2a) (rPduLΔEP).	RESULTS
85	93	removing	experimental_method	Among these, we were only able to obtain diffraction-quality crystals of rPduL after removing the N-terminal putative EP (33 amino acids, also see Fig 2a) (rPduLΔEP).	RESULTS
118	120	EP	structure_element	Among these, we were only able to obtain diffraction-quality crystals of rPduL after removing the N-terminal putative EP (33 amino acids, also see Fig 2a) (rPduLΔEP).	RESULTS
122	136	33 amino acids	residue_range	Among these, we were only able to obtain diffraction-quality crystals of rPduL after removing the N-terminal putative EP (33 amino acids, also see Fig 2a) (rPduLΔEP).	RESULTS
156	164	rPduLΔEP	mutant	Among these, we were only able to obtain diffraction-quality crystals of rPduL after removing the N-terminal putative EP (33 amino acids, also see Fig 2a) (rPduLΔEP).	RESULTS
0	9	Truncated	protein_state	Truncated rPduLΔEP had comparable enzymatic activity to the full-length enzyme (S1a Fig).	RESULTS
10	18	rPduLΔEP	mutant	Truncated rPduLΔEP had comparable enzymatic activity to the full-length enzyme (S1a Fig).	RESULTS
60	71	full-length	protein_state	Truncated rPduLΔEP had comparable enzymatic activity to the full-length enzyme (S1a Fig).	RESULTS
23	35	R. palustris	species	Structural overview of R. palustris PduL from the grm3 locus.	FIG
36	40	PduL	protein_type	Structural overview of R. palustris PduL from the grm3 locus.	FIG
50	60	grm3 locus	gene	Structural overview of R. palustris PduL from the grm3 locus.	FIG
39	44	rPduL	protein	(a) Primary and secondary structure of rPduL (tubes represent α-helices, arrows β-sheets and dashed line residues disordered in the structure.	FIG
62	71	α-helices	structure_element	(a) Primary and secondary structure of rPduL (tubes represent α-helices, arrows β-sheets and dashed line residues disordered in the structure.	FIG
80	88	β-sheets	structure_element	(a) Primary and secondary structure of rPduL (tubes represent α-helices, arrows β-sheets and dashed line residues disordered in the structure.	FIG
132	141	structure	evidence	(a) Primary and secondary structure of rPduL (tubes represent α-helices, arrows β-sheets and dashed line residues disordered in the structure.	FIG
4	24	first 33 amino acids	residue_range	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
95	97	EP	structure_element	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
98	109	alpha helix	structure_element	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
111	113	α0	structure_element	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
120	129	truncated	protein_state	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
130	138	rPduLΔEP	mutant	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
148	160	crystallized	experimental_method	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
173	174	M	residue_name	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
175	176	G	residue_name	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
177	178	V	residue_name	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
225	233	domain 1	structure_element	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
234	241	D36-N46	residue_range	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
242	251	Q155-C224	residue_range	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
259	273	loop insertion	structure_element	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
274	281	G61-E81	residue_range	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
289	297	domain 2	structure_element	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
298	305	R47-F60	residue_range	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
306	314	E82-A154	residue_range	The first 33 amino acids are present only in the wildtype construct and contains the predicted EP alpha helix, α0); the truncated rPduLΔEP that was crystallized begins with M-G-V. Coloring is according to structural domains (domain 1 D36-N46/Q155-C224, blue; loop insertion G61-E81, grey; domain 2 R47-F60/E82-A154, red).	FIG
0	27	Metal coordination residues	site	Metal coordination residues are highlighted in light blue and CoA contacting residues in magenta, residues contacting the CoA of the other chain are also outlined.	FIG
62	85	CoA contacting residues	site	Metal coordination residues are highlighted in light blue and CoA contacting residues in magenta, residues contacting the CoA of the other chain are also outlined.	FIG
122	125	CoA	chemical	Metal coordination residues are highlighted in light blue and CoA contacting residues in magenta, residues contacting the CoA of the other chain are also outlined.	FIG
34	43	structure	evidence	(b) Cartoon representation of the structure colored by domains and including secondary structure numbering.	FIG
87	96	structure	evidence	(b) Cartoon representation of the structure colored by domains and including secondary structure numbering.	FIG
0	10	Coenzyme A	chemical	Coenzyme A is shown in magenta sticks and Zinc (grey) as spheres.	FIG
42	46	Zinc	chemical	Coenzyme A is shown in magenta sticks and Zinc (grey) as spheres.	FIG
3	29	collected a native dataset	experimental_method	We collected a native dataset from rPduLΔEP crystals diffracting to a resolution of 1.54 Å (Table 2).	RESULTS
35	43	rPduLΔEP	mutant	We collected a native dataset from rPduLΔEP crystals diffracting to a resolution of 1.54 Å (Table 2).	RESULTS
44	52	crystals	evidence	We collected a native dataset from rPduLΔEP crystals diffracting to a resolution of 1.54 Å (Table 2).	RESULTS
8	34	mercury-derivative crystal	experimental_method	Using a mercury-derivative crystal form diffracting to 1.99 Å (Table 2), we obtained high quality electron density for model building and used the initial model to refine against the native data to Rwork/Rfree values of 18.9/22.1%.	RESULTS
98	114	electron density	evidence	Using a mercury-derivative crystal form diffracting to 1.99 Å (Table 2), we obtained high quality electron density for model building and used the initial model to refine against the native data to Rwork/Rfree values of 18.9/22.1%.	RESULTS
198	203	Rwork	evidence	Using a mercury-derivative crystal form diffracting to 1.99 Å (Table 2), we obtained high quality electron density for model building and used the initial model to refine against the native data to Rwork/Rfree values of 18.9/22.1%.	RESULTS
204	209	Rfree	evidence	Using a mercury-derivative crystal form diffracting to 1.99 Å (Table 2), we obtained high quality electron density for model building and used the initial model to refine against the native data to Rwork/Rfree values of 18.9/22.1%.	RESULTS
14	18	PduL	protein_type	There are two PduL molecules in the asymmetric unit of the P212121 unit cell.	RESULTS
52	59	PduLΔEP	mutant	We were able to fit all of the primary structure of PduLΔEP into the electron density with the exception of three amino acids at the N-terminus and two amino acids at the C-terminus (Fig 2a); the model is of excellent quality (Table 2).	RESULTS
69	85	electron density	evidence	We were able to fit all of the primary structure of PduLΔEP into the electron density with the exception of three amino acids at the N-terminus and two amino acids at the C-terminus (Fig 2a); the model is of excellent quality (Table 2).	RESULTS
2	5	CoA	chemical	A CoA cofactor as well as two metal ions are clearly resolved in the density (for omit maps of CoA see S2 Fig).	RESULTS
69	76	density	evidence	A CoA cofactor as well as two metal ions are clearly resolved in the density (for omit maps of CoA see S2 Fig).	RESULTS
82	91	omit maps	evidence	A CoA cofactor as well as two metal ions are clearly resolved in the density (for omit maps of CoA see S2 Fig).	RESULTS
95	98	CoA	chemical	A CoA cofactor as well as two metal ions are clearly resolved in the density (for omit maps of CoA see S2 Fig).	RESULTS
14	18	PduL	protein_type	Structurally, PduL consists of two domains (Fig 2, blue/red), each a beta-barrel that is capped on both ends by short α-helices.	RESULTS
35	42	domains	structure_element	Structurally, PduL consists of two domains (Fig 2, blue/red), each a beta-barrel that is capped on both ends by short α-helices.	RESULTS
69	80	beta-barrel	structure_element	Structurally, PduL consists of two domains (Fig 2, blue/red), each a beta-barrel that is capped on both ends by short α-helices.	RESULTS
118	127	α-helices	structure_element	Structurally, PduL consists of two domains (Fig 2, blue/red), each a beta-barrel that is capped on both ends by short α-helices.	RESULTS
0	10	β-Barrel 1	structure_element	β-Barrel 1 consists of the N-terminal β strand and β strands from the C-terminal half of the polypeptide chain (β1, β10-β14; residues 37–46 and 155–224).	RESULTS
38	46	β strand	structure_element	β-Barrel 1 consists of the N-terminal β strand and β strands from the C-terminal half of the polypeptide chain (β1, β10-β14; residues 37–46 and 155–224).	RESULTS
51	60	β strands	structure_element	β-Barrel 1 consists of the N-terminal β strand and β strands from the C-terminal half of the polypeptide chain (β1, β10-β14; residues 37–46 and 155–224).	RESULTS
70	85	C-terminal half	structure_element	β-Barrel 1 consists of the N-terminal β strand and β strands from the C-terminal half of the polypeptide chain (β1, β10-β14; residues 37–46 and 155–224).	RESULTS
112	114	β1	structure_element	β-Barrel 1 consists of the N-terminal β strand and β strands from the C-terminal half of the polypeptide chain (β1, β10-β14; residues 37–46 and 155–224).	RESULTS
116	123	β10-β14	structure_element	β-Barrel 1 consists of the N-terminal β strand and β strands from the C-terminal half of the polypeptide chain (β1, β10-β14; residues 37–46 and 155–224).	RESULTS
134	139	37–46	residue_range	β-Barrel 1 consists of the N-terminal β strand and β strands from the C-terminal half of the polypeptide chain (β1, β10-β14; residues 37–46 and 155–224).	RESULTS
144	151	155–224	residue_range	β-Barrel 1 consists of the N-terminal β strand and β strands from the C-terminal half of the polypeptide chain (β1, β10-β14; residues 37–46 and 155–224).	RESULTS
0	10	β-Barrel 2	structure_element	β-Barrel 2 consists mainly of the central segment of primary structure (β2, β5–β9; residues 47–60 and 82–154) (Fig 2, red), but is interrupted by a short two-strand beta sheet (β3-β4, residues 61–81).	RESULTS
72	74	β2	structure_element	β-Barrel 2 consists mainly of the central segment of primary structure (β2, β5–β9; residues 47–60 and 82–154) (Fig 2, red), but is interrupted by a short two-strand beta sheet (β3-β4, residues 61–81).	RESULTS
76	81	β5–β9	structure_element	β-Barrel 2 consists mainly of the central segment of primary structure (β2, β5–β9; residues 47–60 and 82–154) (Fig 2, red), but is interrupted by a short two-strand beta sheet (β3-β4, residues 61–81).	RESULTS
92	97	47–60	residue_range	β-Barrel 2 consists mainly of the central segment of primary structure (β2, β5–β9; residues 47–60 and 82–154) (Fig 2, red), but is interrupted by a short two-strand beta sheet (β3-β4, residues 61–81).	RESULTS
102	108	82–154	residue_range	β-Barrel 2 consists mainly of the central segment of primary structure (β2, β5–β9; residues 47–60 and 82–154) (Fig 2, red), but is interrupted by a short two-strand beta sheet (β3-β4, residues 61–81).	RESULTS
148	175	short two-strand beta sheet	structure_element	β-Barrel 2 consists mainly of the central segment of primary structure (β2, β5–β9; residues 47–60 and 82–154) (Fig 2, red), but is interrupted by a short two-strand beta sheet (β3-β4, residues 61–81).	RESULTS
177	182	β3-β4	structure_element	β-Barrel 2 consists mainly of the central segment of primary structure (β2, β5–β9; residues 47–60 and 82–154) (Fig 2, red), but is interrupted by a short two-strand beta sheet (β3-β4, residues 61–81).	RESULTS
193	198	61–81	residue_range	β-Barrel 2 consists mainly of the central segment of primary structure (β2, β5–β9; residues 47–60 and 82–154) (Fig 2, red), but is interrupted by a short two-strand beta sheet (β3-β4, residues 61–81).	RESULTS
5	12	β-sheet	structure_element	This β-sheet is involved in contacts between the two domains and forms a lid over the active site.	RESULTS
86	97	active site	site	This β-sheet is involved in contacts between the two domains and forms a lid over the active site.	RESULTS
25	30	Gln42	residue_name_number	Residues in this region (Gln42, Pro43, Gly44), covering the active site, are strongly conserved (Fig 3).	RESULTS
32	37	Pro43	residue_name_number	Residues in this region (Gln42, Pro43, Gly44), covering the active site, are strongly conserved (Fig 3).	RESULTS
39	44	Gly44	residue_name_number	Residues in this region (Gln42, Pro43, Gly44), covering the active site, are strongly conserved (Fig 3).	RESULTS
60	71	active site	site	Residues in this region (Gln42, Pro43, Gly44), covering the active site, are strongly conserved (Fig 3).	RESULTS
77	95	strongly conserved	protein_state	Residues in this region (Gln42, Pro43, Gly44), covering the active site, are strongly conserved (Fig 3).	RESULTS
82	85	Pta	protein_type	This structural arrangement is completely different from the functionally related Pta, which is composed of two domains, each consisting of a central flat beta sheet with alpha-helices on the top and bottom.	RESULTS
112	119	domains	structure_element	This structural arrangement is completely different from the functionally related Pta, which is composed of two domains, each consisting of a central flat beta sheet with alpha-helices on the top and bottom.	RESULTS
155	165	beta sheet	structure_element	This structural arrangement is completely different from the functionally related Pta, which is composed of two domains, each consisting of a central flat beta sheet with alpha-helices on the top and bottom.	RESULTS
171	184	alpha-helices	structure_element	This structural arrangement is completely different from the functionally related Pta, which is composed of two domains, each consisting of a central flat beta sheet with alpha-helices on the top and bottom.	RESULTS
38	42	PduL	protein_type	Primary structure conservation of the PduL protein family.	FIG
34	61	multiple sequence alignment	experimental_method	Sequence logo calculated from the multiple sequence alignment of PduL homologs (see Materials and Methods), but not including putative EP sequences.	FIG
65	69	PduL	protein_type	Sequence logo calculated from the multiple sequence alignment of PduL homologs (see Materials and Methods), but not including putative EP sequences.	FIG
112	125	not including	protein_state	Sequence logo calculated from the multiple sequence alignment of PduL homologs (see Materials and Methods), but not including putative EP sequences.	FIG
135	137	EP	structure_element	Sequence logo calculated from the multiple sequence alignment of PduL homologs (see Materials and Methods), but not including putative EP sequences.	FIG
35	39	PduL	protein_type	Residues 100% conserved across all PduL homologs in our dataset are noted with an asterisk, and residues conserved in over 90% of sequences are noted with a colon.	FIG
30	37	PF06130	structure_element	The sequences aligning to the PF06130 domain (determined by BLAST) are highlighted in red and blue.	FIG
66	71	rPduL	protein	The position numbers shown correspond to the residue numbering of rPduL; note that some positions in the logo represent gaps in the rPduL sequence.	FIG
132	137	rPduL	protein	The position numbers shown correspond to the residue numbering of rPduL; note that some positions in the logo represent gaps in the rPduL sequence.	FIG
14	18	PduL	protein_type	There are two PduL molecules in the asymmetric unit forming a butterfly-shaped dimer (Fig 4c).	RESULTS
62	78	butterfly-shaped	protein_state	There are two PduL molecules in the asymmetric unit forming a butterfly-shaped dimer (Fig 4c).	RESULTS
79	84	dimer	oligomeric_state	There are two PduL molecules in the asymmetric unit forming a butterfly-shaped dimer (Fig 4c).	RESULTS
35	64	size exclusion chromatography	experimental_method	Consistent with this, results from size exclusion chromatography of rPduLΔEP suggest that it is a dimer in solution (Fig 5e).	RESULTS
68	76	rPduLΔEP	mutant	Consistent with this, results from size exclusion chromatography of rPduLΔEP suggest that it is a dimer in solution (Fig 5e).	RESULTS
98	103	dimer	oligomeric_state	Consistent with this, results from size exclusion chromatography of rPduLΔEP suggest that it is a dimer in solution (Fig 5e).	RESULTS
4	13	interface	site	The interface between the two chains buries 882 Å2 per monomer and is mainly formed by α-helices 2 and 4 and parts of β-sheets 12 and 14, as well as a π–π stacking of the adenine moiety of CoA with Phe116 of the adjacent chain (Fig 4c).	RESULTS
55	62	monomer	oligomeric_state	The interface between the two chains buries 882 Å2 per monomer and is mainly formed by α-helices 2 and 4 and parts of β-sheets 12 and 14, as well as a π–π stacking of the adenine moiety of CoA with Phe116 of the adjacent chain (Fig 4c).	RESULTS
87	104	α-helices 2 and 4	structure_element	The interface between the two chains buries 882 Å2 per monomer and is mainly formed by α-helices 2 and 4 and parts of β-sheets 12 and 14, as well as a π–π stacking of the adenine moiety of CoA with Phe116 of the adjacent chain (Fig 4c).	RESULTS
118	136	β-sheets 12 and 14	structure_element	The interface between the two chains buries 882 Å2 per monomer and is mainly formed by α-helices 2 and 4 and parts of β-sheets 12 and 14, as well as a π–π stacking of the adenine moiety of CoA with Phe116 of the adjacent chain (Fig 4c).	RESULTS
171	178	adenine	chemical	The interface between the two chains buries 882 Å2 per monomer and is mainly formed by α-helices 2 and 4 and parts of β-sheets 12 and 14, as well as a π–π stacking of the adenine moiety of CoA with Phe116 of the adjacent chain (Fig 4c).	RESULTS
189	192	CoA	chemical	The interface between the two chains buries 882 Å2 per monomer and is mainly formed by α-helices 2 and 4 and parts of β-sheets 12 and 14, as well as a π–π stacking of the adenine moiety of CoA with Phe116 of the adjacent chain (Fig 4c).	RESULTS
198	204	Phe116	residue_name_number	The interface between the two chains buries 882 Å2 per monomer and is mainly formed by α-helices 2 and 4 and parts of β-sheets 12 and 14, as well as a π–π stacking of the adenine moiety of CoA with Phe116 of the adjacent chain (Fig 4c).	RESULTS
69	82	superimposing	experimental_method	The folds of the two chains in the asymmetric unit are very similar, superimposing with a rmsd of 0.16 Å over 2,306 aligned atom pairs.	RESULTS
90	94	rmsd	evidence	The folds of the two chains in the asymmetric unit are very similar, superimposing with a rmsd of 0.16 Å over 2,306 aligned atom pairs.	RESULTS
15	22	helices	structure_element	The peripheral helices and the short antiparallel β3–4 sheet mediate most of the crystal contacts.	RESULTS
31	60	short antiparallel β3–4 sheet	structure_element	The peripheral helices and the short antiparallel β3–4 sheet mediate most of the crystal contacts.	RESULTS
11	22	active site	site	Details of active site, dimeric assembly, and sequence conservation of PduL.	FIG
24	31	dimeric	oligomeric_state	Details of active site, dimeric assembly, and sequence conservation of PduL.	FIG
71	75	PduL	protein_type	Details of active site, dimeric assembly, and sequence conservation of PduL.	FIG
15	26	active site	site	(a,b) Proposed active site of PduL with relevant residues shown as sticks in atom coloring (nitrogen blue, oxygen red, sulfur yellow), zinc as grey colored spheres and coordinating ordered water molecules in red.	FIG
30	34	PduL	protein_type	(a,b) Proposed active site of PduL with relevant residues shown as sticks in atom coloring (nitrogen blue, oxygen red, sulfur yellow), zinc as grey colored spheres and coordinating ordered water molecules in red.	FIG
92	100	nitrogen	chemical	(a,b) Proposed active site of PduL with relevant residues shown as sticks in atom coloring (nitrogen blue, oxygen red, sulfur yellow), zinc as grey colored spheres and coordinating ordered water molecules in red.	FIG
107	113	oxygen	chemical	(a,b) Proposed active site of PduL with relevant residues shown as sticks in atom coloring (nitrogen blue, oxygen red, sulfur yellow), zinc as grey colored spheres and coordinating ordered water molecules in red.	FIG
119	125	sulfur	chemical	(a,b) Proposed active site of PduL with relevant residues shown as sticks in atom coloring (nitrogen blue, oxygen red, sulfur yellow), zinc as grey colored spheres and coordinating ordered water molecules in red.	FIG
135	139	zinc	chemical	(a,b) Proposed active site of PduL with relevant residues shown as sticks in atom coloring (nitrogen blue, oxygen red, sulfur yellow), zinc as grey colored spheres and coordinating ordered water molecules in red.	FIG
189	194	water	chemical	(a,b) Proposed active site of PduL with relevant residues shown as sticks in atom coloring (nitrogen blue, oxygen red, sulfur yellow), zinc as grey colored spheres and coordinating ordered water molecules in red.	FIG
55	65	Coenzyme A	chemical	Distances between atom centers are indicated in Å. (a) Coenzyme A containing, (b) phosphate-bound structure.	FIG
82	97	phosphate-bound	protein_state	Distances between atom centers are indicated in Å. (a) Coenzyme A containing, (b) phosphate-bound structure.	FIG
98	107	structure	evidence	Distances between atom centers are indicated in Å. (a) Coenzyme A containing, (b) phosphate-bound structure.	FIG
16	21	dimer	oligomeric_state	(c) View of the dimer in the asymmetric unit from the side, domains 1 and 2 colored as in Fig 2 and the two chains differentiated by blue/red versus slate/firebrick.	FIG
60	75	domains 1 and 2	structure_element	(c) View of the dimer in the asymmetric unit from the side, domains 1 and 2 colored as in Fig 2 and the two chains differentiated by blue/red versus slate/firebrick.	FIG
80	84	F116	residue_name_number	The asterisk and double arrow marks the location of the π–π interaction between F116 and the CoA base of the other dimer chain.	FIG
93	96	CoA	chemical	The asterisk and double arrow marks the location of the π–π interaction between F116 and the CoA base of the other dimer chain.	FIG
115	120	dimer	oligomeric_state	The asterisk and double arrow marks the location of the π–π interaction between F116 and the CoA base of the other dimer chain.	FIG
34	43	structure	evidence	(d) Surface representation of the structure with indicated conservation (red: high, white: intermediate, yellow: low).	FIG
0	29	Size exclusion chromatography	experimental_method	Size exclusion chromatography of PduL homologs.	FIG
33	37	PduL	protein_type	Size exclusion chromatography of PduL homologs.	FIG
9	22	Chromatograms	evidence	(a)–(c): Chromatograms of sPduL (a), rPduL (b), and pPduL (c) with (orange) or without (blue) the predicted EP, post-nickel affinity purification, applied over a preparative size exclusion column (see Materials and Methods).	FIG
26	31	sPduL	protein	(a)–(c): Chromatograms of sPduL (a), rPduL (b), and pPduL (c) with (orange) or without (blue) the predicted EP, post-nickel affinity purification, applied over a preparative size exclusion column (see Materials and Methods).	FIG
37	42	rPduL	protein	(a)–(c): Chromatograms of sPduL (a), rPduL (b), and pPduL (c) with (orange) or without (blue) the predicted EP, post-nickel affinity purification, applied over a preparative size exclusion column (see Materials and Methods).	FIG
52	57	pPduL	protein	(a)–(c): Chromatograms of sPduL (a), rPduL (b), and pPduL (c) with (orange) or without (blue) the predicted EP, post-nickel affinity purification, applied over a preparative size exclusion column (see Materials and Methods).	FIG
108	110	EP	structure_element	(a)–(c): Chromatograms of sPduL (a), rPduL (b), and pPduL (c) with (orange) or without (blue) the predicted EP, post-nickel affinity purification, applied over a preparative size exclusion column (see Materials and Methods).	FIG
117	145	nickel affinity purification	experimental_method	(a)–(c): Chromatograms of sPduL (a), rPduL (b), and pPduL (c) with (orange) or without (blue) the predicted EP, post-nickel affinity purification, applied over a preparative size exclusion column (see Materials and Methods).	FIG
9	22	Chromatograms	evidence	(d)–(f): Chromatograms of sPduL (d), rPduL (e), and pPduL (f) post-preparative size exclusion chromatography with different size fractions separated, applied over an analytical size exclusion column (see Materials and Methods).	FIG
26	31	sPduL	protein	(d)–(f): Chromatograms of sPduL (d), rPduL (e), and pPduL (f) post-preparative size exclusion chromatography with different size fractions separated, applied over an analytical size exclusion column (see Materials and Methods).	FIG
37	42	rPduL	protein	(d)–(f): Chromatograms of sPduL (d), rPduL (e), and pPduL (f) post-preparative size exclusion chromatography with different size fractions separated, applied over an analytical size exclusion column (see Materials and Methods).	FIG
52	57	pPduL	protein	(d)–(f): Chromatograms of sPduL (d), rPduL (e), and pPduL (f) post-preparative size exclusion chromatography with different size fractions separated, applied over an analytical size exclusion column (see Materials and Methods).	FIG
79	108	size exclusion chromatography	experimental_method	(d)–(f): Chromatograms of sPduL (d), rPduL (e), and pPduL (f) post-preparative size exclusion chromatography with different size fractions separated, applied over an analytical size exclusion column (see Materials and Methods).	FIG
4	17	chromatograms	evidence	All chromatograms are cropped to show only the linear range of separation based on standard runs, shown in black squares with a dashed linear trend line.	FIG
0	11	Active Site	site	Active Site Properties	RESULTS
0	3	CoA	chemical	CoA and the metal ions bind between the two domains, presumably in the active site (Figs 2b and 4a).	RESULTS
71	82	active site	site	CoA and the metal ions bind between the two domains, presumably in the active site (Figs 2b and 4a).	RESULTS
46	69	X-ray fluorescence scan	experimental_method	To identify the bound metals, we performed an X-ray fluorescence scan on the crystals at various wavelengths (corresponding to the K-edges of Mn, Fe, Co, Ni, Cu, and Zn).	RESULTS
77	85	crystals	evidence	To identify the bound metals, we performed an X-ray fluorescence scan on the crystals at various wavelengths (corresponding to the K-edges of Mn, Fe, Co, Ni, Cu, and Zn).	RESULTS
142	144	Mn	chemical	To identify the bound metals, we performed an X-ray fluorescence scan on the crystals at various wavelengths (corresponding to the K-edges of Mn, Fe, Co, Ni, Cu, and Zn).	RESULTS
146	148	Fe	chemical	To identify the bound metals, we performed an X-ray fluorescence scan on the crystals at various wavelengths (corresponding to the K-edges of Mn, Fe, Co, Ni, Cu, and Zn).	RESULTS
150	152	Co	chemical	To identify the bound metals, we performed an X-ray fluorescence scan on the crystals at various wavelengths (corresponding to the K-edges of Mn, Fe, Co, Ni, Cu, and Zn).	RESULTS
154	156	Ni	chemical	To identify the bound metals, we performed an X-ray fluorescence scan on the crystals at various wavelengths (corresponding to the K-edges of Mn, Fe, Co, Ni, Cu, and Zn).	RESULTS
158	160	Cu	chemical	To identify the bound metals, we performed an X-ray fluorescence scan on the crystals at various wavelengths (corresponding to the K-edges of Mn, Fe, Co, Ni, Cu, and Zn).	RESULTS
166	168	Zn	chemical	To identify the bound metals, we performed an X-ray fluorescence scan on the crystals at various wavelengths (corresponding to the K-edges of Mn, Fe, Co, Ni, Cu, and Zn).	RESULTS
77	81	zinc	chemical	There was a large signal at the zinc edge, and we tested for the presence of zinc by collecting full data sets before and after the Zn K-edge (1.2861 and 1.2822 Å, respectively).	RESULTS
85	162	collecting full data sets before and after the Zn K-edge (1.2861 and 1.2822 Å	experimental_method	There was a large signal at the zinc edge, and we tested for the presence of zinc by collecting full data sets before and after the Zn K-edge (1.2861 and 1.2822 Å, respectively).	RESULTS
76	80	zinc	chemical	The large differences between the anomalous signals confirm the presence of zinc at both metal sites (S3 Fig).	RESULTS
10	14	zinc	chemical	The first zinc ion (Zn1) is in a tetrahedral coordination state with His48, His50, Glu109, and the CoA sulfur (Fig 4a).	RESULTS
20	23	Zn1	chemical	The first zinc ion (Zn1) is in a tetrahedral coordination state with His48, His50, Glu109, and the CoA sulfur (Fig 4a).	RESULTS
69	74	His48	residue_name_number	The first zinc ion (Zn1) is in a tetrahedral coordination state with His48, His50, Glu109, and the CoA sulfur (Fig 4a).	RESULTS
76	81	His50	residue_name_number	The first zinc ion (Zn1) is in a tetrahedral coordination state with His48, His50, Glu109, and the CoA sulfur (Fig 4a).	RESULTS
83	89	Glu109	residue_name_number	The first zinc ion (Zn1) is in a tetrahedral coordination state with His48, His50, Glu109, and the CoA sulfur (Fig 4a).	RESULTS
99	102	CoA	chemical	The first zinc ion (Zn1) is in a tetrahedral coordination state with His48, His50, Glu109, and the CoA sulfur (Fig 4a).	RESULTS
103	109	sulfur	chemical	The first zinc ion (Zn1) is in a tetrahedral coordination state with His48, His50, Glu109, and the CoA sulfur (Fig 4a).	RESULTS
12	15	Zn2	chemical	The second (Zn2) is in octahedral coordination by three conserved histidine residues (His157, His159 and His204) as well as three water molecules (Fig 4a).	RESULTS
56	65	conserved	protein_state	The second (Zn2) is in octahedral coordination by three conserved histidine residues (His157, His159 and His204) as well as three water molecules (Fig 4a).	RESULTS
66	75	histidine	residue_name	The second (Zn2) is in octahedral coordination by three conserved histidine residues (His157, His159 and His204) as well as three water molecules (Fig 4a).	RESULTS
86	92	His157	residue_name_number	The second (Zn2) is in octahedral coordination by three conserved histidine residues (His157, His159 and His204) as well as three water molecules (Fig 4a).	RESULTS
94	100	His159	residue_name_number	The second (Zn2) is in octahedral coordination by three conserved histidine residues (His157, His159 and His204) as well as three water molecules (Fig 4a).	RESULTS
105	111	His204	residue_name_number	The second (Zn2) is in octahedral coordination by three conserved histidine residues (His157, His159 and His204) as well as three water molecules (Fig 4a).	RESULTS
130	135	water	chemical	The second (Zn2) is in octahedral coordination by three conserved histidine residues (His157, His159 and His204) as well as three water molecules (Fig 4a).	RESULTS
35	39	zinc	chemical	The nitrogen atom coordinating the zinc is the Nε in each histidine residue, as is typical for this interaction.	RESULTS
58	67	histidine	residue_name	The nitrogen atom coordinating the zinc is the Nε in each histidine residue, as is typical for this interaction.	RESULTS
9	29	crystals were soaked	experimental_method	When the crystals were soaked in a sodium phosphate solution for 2 d prior to data collection, the CoA dissociates, and density for a phosphate molecule is visible at the active site (Table 2, Fig 4b).	RESULTS
35	51	sodium phosphate	chemical	When the crystals were soaked in a sodium phosphate solution for 2 d prior to data collection, the CoA dissociates, and density for a phosphate molecule is visible at the active site (Table 2, Fig 4b).	RESULTS
99	102	CoA	chemical	When the crystals were soaked in a sodium phosphate solution for 2 d prior to data collection, the CoA dissociates, and density for a phosphate molecule is visible at the active site (Table 2, Fig 4b).	RESULTS
120	127	density	evidence	When the crystals were soaked in a sodium phosphate solution for 2 d prior to data collection, the CoA dissociates, and density for a phosphate molecule is visible at the active site (Table 2, Fig 4b).	RESULTS
134	143	phosphate	chemical	When the crystals were soaked in a sodium phosphate solution for 2 d prior to data collection, the CoA dissociates, and density for a phosphate molecule is visible at the active site (Table 2, Fig 4b).	RESULTS
171	182	active site	site	When the crystals were soaked in a sodium phosphate solution for 2 d prior to data collection, the CoA dissociates, and density for a phosphate molecule is visible at the active site (Table 2, Fig 4b).	RESULTS
4	19	phosphate-bound	protein_state	The phosphate-bound structure aligns well with the CoA-bound structure (0.43 Å rmsd over 2,361 atoms for the monomer, 0.83 Å over 5,259 aligned atoms for the dimer).	RESULTS
20	29	structure	evidence	The phosphate-bound structure aligns well with the CoA-bound structure (0.43 Å rmsd over 2,361 atoms for the monomer, 0.83 Å over 5,259 aligned atoms for the dimer).	RESULTS
30	36	aligns	experimental_method	The phosphate-bound structure aligns well with the CoA-bound structure (0.43 Å rmsd over 2,361 atoms for the monomer, 0.83 Å over 5,259 aligned atoms for the dimer).	RESULTS
51	60	CoA-bound	protein_state	The phosphate-bound structure aligns well with the CoA-bound structure (0.43 Å rmsd over 2,361 atoms for the monomer, 0.83 Å over 5,259 aligned atoms for the dimer).	RESULTS
61	70	structure	evidence	The phosphate-bound structure aligns well with the CoA-bound structure (0.43 Å rmsd over 2,361 atoms for the monomer, 0.83 Å over 5,259 aligned atoms for the dimer).	RESULTS
79	83	rmsd	evidence	The phosphate-bound structure aligns well with the CoA-bound structure (0.43 Å rmsd over 2,361 atoms for the monomer, 0.83 Å over 5,259 aligned atoms for the dimer).	RESULTS
109	116	monomer	oligomeric_state	The phosphate-bound structure aligns well with the CoA-bound structure (0.43 Å rmsd over 2,361 atoms for the monomer, 0.83 Å over 5,259 aligned atoms for the dimer).	RESULTS
158	163	dimer	oligomeric_state	The phosphate-bound structure aligns well with the CoA-bound structure (0.43 Å rmsd over 2,361 atoms for the monomer, 0.83 Å over 5,259 aligned atoms for the dimer).	RESULTS
4	13	phosphate	chemical	The phosphate contacts both zinc atoms (Fig 4b) and replaces the coordination by CoA at Zn1; the coordination for Zn2 changes from octahedral with three bound waters to tetrahedral with a phosphate ion as one of the ligands (Fig 4b).	RESULTS
28	32	zinc	chemical	The phosphate contacts both zinc atoms (Fig 4b) and replaces the coordination by CoA at Zn1; the coordination for Zn2 changes from octahedral with three bound waters to tetrahedral with a phosphate ion as one of the ligands (Fig 4b).	RESULTS
81	84	CoA	chemical	The phosphate contacts both zinc atoms (Fig 4b) and replaces the coordination by CoA at Zn1; the coordination for Zn2 changes from octahedral with three bound waters to tetrahedral with a phosphate ion as one of the ligands (Fig 4b).	RESULTS
88	91	Zn1	chemical	The phosphate contacts both zinc atoms (Fig 4b) and replaces the coordination by CoA at Zn1; the coordination for Zn2 changes from octahedral with three bound waters to tetrahedral with a phosphate ion as one of the ligands (Fig 4b).	RESULTS
114	117	Zn2	chemical	The phosphate contacts both zinc atoms (Fig 4b) and replaces the coordination by CoA at Zn1; the coordination for Zn2 changes from octahedral with three bound waters to tetrahedral with a phosphate ion as one of the ligands (Fig 4b).	RESULTS
159	165	waters	chemical	The phosphate contacts both zinc atoms (Fig 4b) and replaces the coordination by CoA at Zn1; the coordination for Zn2 changes from octahedral with three bound waters to tetrahedral with a phosphate ion as one of the ligands (Fig 4b).	RESULTS
188	197	phosphate	chemical	The phosphate contacts both zinc atoms (Fig 4b) and replaces the coordination by CoA at Zn1; the coordination for Zn2 changes from octahedral with three bound waters to tetrahedral with a phosphate ion as one of the ligands (Fig 4b).	RESULTS
0	9	Conserved	protein_state	Conserved Arg103 seems to be involved in maintaining the phosphate in that position.	RESULTS
10	16	Arg103	residue_name_number	Conserved Arg103 seems to be involved in maintaining the phosphate in that position.	RESULTS
57	66	phosphate	chemical	Conserved Arg103 seems to be involved in maintaining the phosphate in that position.	RESULTS
8	12	zinc	chemical	The two zinc atoms are slightly closer together in the phosphate-bound form (5.8 Å vs 6.3 Å), possibly due to the bridging effect of the phosphate.	RESULTS
55	70	phosphate-bound	protein_state	The two zinc atoms are slightly closer together in the phosphate-bound form (5.8 Å vs 6.3 Å), possibly due to the bridging effect of the phosphate.	RESULTS
137	146	phosphate	chemical	The two zinc atoms are slightly closer together in the phosphate-bound form (5.8 Å vs 6.3 Å), possibly due to the bridging effect of the phosphate.	RESULTS
14	23	phosphate	chemical	An additional phosphate molecule is bound at a crystal contact interface, perhaps accounting for the 14 Å shorter c-axis in the phosphate-bound crystal form (Table 2).	RESULTS
128	143	phosphate-bound	protein_state	An additional phosphate molecule is bound at a crystal contact interface, perhaps accounting for the 14 Å shorter c-axis in the phosphate-bound crystal form (Table 2).	RESULTS
21	25	PduL	protein_type	Oligomeric States of PduL Orthologs Are Influenced by the EP	RESULTS
58	60	EP	structure_element	Oligomeric States of PduL Orthologs Are Influenced by the EP	RESULTS
66	71	rPduL	protein	Interestingly, some of the residues important for dimerization of rPduL, particularly Phe116, are poorly conserved across PduL homologs associated with functionally diverse BMCs (Figs 4c and 3), suggesting that they may have alternative oligomeric states.	RESULTS
86	92	Phe116	residue_name_number	Interestingly, some of the residues important for dimerization of rPduL, particularly Phe116, are poorly conserved across PduL homologs associated with functionally diverse BMCs (Figs 4c and 3), suggesting that they may have alternative oligomeric states.	RESULTS
98	114	poorly conserved	protein_state	Interestingly, some of the residues important for dimerization of rPduL, particularly Phe116, are poorly conserved across PduL homologs associated with functionally diverse BMCs (Figs 4c and 3), suggesting that they may have alternative oligomeric states.	RESULTS
122	126	PduL	protein_type	Interestingly, some of the residues important for dimerization of rPduL, particularly Phe116, are poorly conserved across PduL homologs associated with functionally diverse BMCs (Figs 4c and 3), suggesting that they may have alternative oligomeric states.	RESULTS
173	177	BMCs	complex_assembly	Interestingly, some of the residues important for dimerization of rPduL, particularly Phe116, are poorly conserved across PduL homologs associated with functionally diverse BMCs (Figs 4c and 3), suggesting that they may have alternative oligomeric states.	RESULTS
40	69	size exclusion chromatography	experimental_method	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
78	89	full-length	protein_state	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
114	121	lacking	protein_state	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
126	128	EP	structure_element	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
130	133	ΔEP	mutant	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
138	143	sPduL	protein	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
145	150	rPduL	protein	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
156	161	pPduL	protein	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
219	223	BMCs	complex_assembly	We tested this hypothesis by performing size exclusion chromatography on both full-length and truncated variants (lacking the EP, ΔEP) of sPduL, rPduL, and pPduL. These three homologs are found in functionally distinct BMCs (Table 1).	RESULTS
30	39	catabolic	protein_state	It has been proposed that the catabolic BMCs may assemble in a core-first manner, with the luminal enzymes (signature enzyme, aldehyde, and alcohol dehydrogenases and the BMC PTAC) forming an initial bolus, or prometabolosome, around which a shell assembles.	RESULTS
40	44	BMCs	complex_assembly	It has been proposed that the catabolic BMCs may assemble in a core-first manner, with the luminal enzymes (signature enzyme, aldehyde, and alcohol dehydrogenases and the BMC PTAC) forming an initial bolus, or prometabolosome, around which a shell assembles.	RESULTS
126	162	aldehyde, and alcohol dehydrogenases	protein_type	It has been proposed that the catabolic BMCs may assemble in a core-first manner, with the luminal enzymes (signature enzyme, aldehyde, and alcohol dehydrogenases and the BMC PTAC) forming an initial bolus, or prometabolosome, around which a shell assembles.	RESULTS
171	174	BMC	complex_assembly	It has been proposed that the catabolic BMCs may assemble in a core-first manner, with the luminal enzymes (signature enzyme, aldehyde, and alcohol dehydrogenases and the BMC PTAC) forming an initial bolus, or prometabolosome, around which a shell assembles.	RESULTS
175	179	PTAC	protein_type	It has been proposed that the catabolic BMCs may assemble in a core-first manner, with the luminal enzymes (signature enzyme, aldehyde, and alcohol dehydrogenases and the BMC PTAC) forming an initial bolus, or prometabolosome, around which a shell assembles.	RESULTS
242	247	shell	structure_element	It has been proposed that the catabolic BMCs may assemble in a core-first manner, with the luminal enzymes (signature enzyme, aldehyde, and alcohol dehydrogenases and the BMC PTAC) forming an initial bolus, or prometabolosome, around which a shell assembles.	RESULTS
73	77	PduL	protein_type	Given the diversity of signature enzymes (Table 1), it is plausible that PduL orthologs may adopt different oligomeric states that reflect the differences in the proteins being packaged with them in the organelle lumen.	RESULTS
170	172	EP	structure_element	We found that not only did the different orthologs appear to assemble into different oligomeric states, but that quaternary structure was dependent on whether or not the EP was present.	RESULTS
0	11	Full-length	protein_state	Full-length sPduL was unstable in solution—precipitating over time—and eluted throughout the entire volume of a size exclusion column, indicating it was nonspecifically aggregating.	RESULTS
12	17	sPduL	protein	Full-length sPduL was unstable in solution—precipitating over time—and eluted throughout the entire volume of a size exclusion column, indicating it was nonspecifically aggregating.	RESULTS
27	29	EP	structure_element	However, when the putative EP (residues 1–27) was removed (sPduL ΔEP), the truncated protein was stable and eluted as a single peak (Fig 5a) consistent with the size of a monomer (Fig 5d, blue curve).	RESULTS
40	44	1–27	residue_range	However, when the putative EP (residues 1–27) was removed (sPduL ΔEP), the truncated protein was stable and eluted as a single peak (Fig 5a) consistent with the size of a monomer (Fig 5d, blue curve).	RESULTS
50	57	removed	experimental_method	However, when the putative EP (residues 1–27) was removed (sPduL ΔEP), the truncated protein was stable and eluted as a single peak (Fig 5a) consistent with the size of a monomer (Fig 5d, blue curve).	RESULTS
59	68	sPduL ΔEP	mutant	However, when the putative EP (residues 1–27) was removed (sPduL ΔEP), the truncated protein was stable and eluted as a single peak (Fig 5a) consistent with the size of a monomer (Fig 5d, blue curve).	RESULTS
75	84	truncated	protein_state	However, when the putative EP (residues 1–27) was removed (sPduL ΔEP), the truncated protein was stable and eluted as a single peak (Fig 5a) consistent with the size of a monomer (Fig 5d, blue curve).	RESULTS
171	178	monomer	oligomeric_state	However, when the putative EP (residues 1–27) was removed (sPduL ΔEP), the truncated protein was stable and eluted as a single peak (Fig 5a) consistent with the size of a monomer (Fig 5d, blue curve).	RESULTS
18	29	full-length	protein_state	In contrast, both full-length rPduL and pPduL appeared to exist in two distinct oligomeric states (Fig 5b and 5c respectively, orange curves), one form of the approximate size of a dimer and the second, a higher molecular weight oligomer (~150 kDa).	RESULTS
30	35	rPduL	protein	In contrast, both full-length rPduL and pPduL appeared to exist in two distinct oligomeric states (Fig 5b and 5c respectively, orange curves), one form of the approximate size of a dimer and the second, a higher molecular weight oligomer (~150 kDa).	RESULTS
40	45	pPduL	protein	In contrast, both full-length rPduL and pPduL appeared to exist in two distinct oligomeric states (Fig 5b and 5c respectively, orange curves), one form of the approximate size of a dimer and the second, a higher molecular weight oligomer (~150 kDa).	RESULTS
181	186	dimer	oligomeric_state	In contrast, both full-length rPduL and pPduL appeared to exist in two distinct oligomeric states (Fig 5b and 5c respectively, orange curves), one form of the approximate size of a dimer and the second, a higher molecular weight oligomer (~150 kDa).	RESULTS
229	237	oligomer	oligomeric_state	In contrast, both full-length rPduL and pPduL appeared to exist in two distinct oligomeric states (Fig 5b and 5c respectively, orange curves), one form of the approximate size of a dimer and the second, a higher molecular weight oligomer (~150 kDa).	RESULTS
5	13	deletion	experimental_method	Upon deletion of the putative EP (residues 1–47 for rPduL, and 1–20 for pPduL), there was a distinct change in the elution profiles (Fig 5b and 5c respectively, blue curves).	RESULTS
30	32	EP	structure_element	Upon deletion of the putative EP (residues 1–47 for rPduL, and 1–20 for pPduL), there was a distinct change in the elution profiles (Fig 5b and 5c respectively, blue curves).	RESULTS
43	47	1–47	residue_range	Upon deletion of the putative EP (residues 1–47 for rPduL, and 1–20 for pPduL), there was a distinct change in the elution profiles (Fig 5b and 5c respectively, blue curves).	RESULTS
52	57	rPduL	protein	Upon deletion of the putative EP (residues 1–47 for rPduL, and 1–20 for pPduL), there was a distinct change in the elution profiles (Fig 5b and 5c respectively, blue curves).	RESULTS
63	67	1–20	residue_range	Upon deletion of the putative EP (residues 1–47 for rPduL, and 1–20 for pPduL), there was a distinct change in the elution profiles (Fig 5b and 5c respectively, blue curves).	RESULTS
72	77	pPduL	protein	Upon deletion of the putative EP (residues 1–47 for rPduL, and 1–20 for pPduL), there was a distinct change in the elution profiles (Fig 5b and 5c respectively, blue curves).	RESULTS
0	8	pPduLΔEP	mutant	pPduLΔEP eluted as two smaller forms, possibly corresponding to a trimer and a monomer.	RESULTS
66	72	trimer	oligomeric_state	pPduLΔEP eluted as two smaller forms, possibly corresponding to a trimer and a monomer.	RESULTS
79	86	monomer	oligomeric_state	pPduLΔEP eluted as two smaller forms, possibly corresponding to a trimer and a monomer.	RESULTS
13	21	rPduLΔEP	mutant	In contrast, rPduLΔEP eluted as one smaller oligomer, possibly a dimer.	RESULTS
65	70	dimer	oligomeric_state	In contrast, rPduLΔEP eluted as one smaller oligomer, possibly a dimer.	RESULTS
26	31	rPduL	protein	We also analyzed purified rPduL and rPduLΔEP by size exclusion chromatography coupled with multiangle light scattering (SEC-MALS) for a complementary approach to assessing oligomeric state.	RESULTS
36	44	rPduLΔEP	mutant	We also analyzed purified rPduL and rPduLΔEP by size exclusion chromatography coupled with multiangle light scattering (SEC-MALS) for a complementary approach to assessing oligomeric state.	RESULTS
48	77	size exclusion chromatography	experimental_method	We also analyzed purified rPduL and rPduLΔEP by size exclusion chromatography coupled with multiangle light scattering (SEC-MALS) for a complementary approach to assessing oligomeric state.	RESULTS
91	118	multiangle light scattering	experimental_method	We also analyzed purified rPduL and rPduLΔEP by size exclusion chromatography coupled with multiangle light scattering (SEC-MALS) for a complementary approach to assessing oligomeric state.	RESULTS
120	128	SEC-MALS	experimental_method	We also analyzed purified rPduL and rPduLΔEP by size exclusion chromatography coupled with multiangle light scattering (SEC-MALS) for a complementary approach to assessing oligomeric state.	RESULTS
0	8	SEC-MALS	experimental_method	SEC-MALS analysis of rPdulΔEP is consistent with a dimer (as observed in the crystal structure) with a weighted average (Mw) and number average (Mn) of the molar mass of 58.4 kDa +/− 11.2% and 58.8 kDa +/− 10.9%, respectively (S4a Fig).	RESULTS
21	29	rPdulΔEP	mutant	SEC-MALS analysis of rPdulΔEP is consistent with a dimer (as observed in the crystal structure) with a weighted average (Mw) and number average (Mn) of the molar mass of 58.4 kDa +/− 11.2% and 58.8 kDa +/− 10.9%, respectively (S4a Fig).	RESULTS
51	56	dimer	oligomeric_state	SEC-MALS analysis of rPdulΔEP is consistent with a dimer (as observed in the crystal structure) with a weighted average (Mw) and number average (Mn) of the molar mass of 58.4 kDa +/− 11.2% and 58.8 kDa +/− 10.9%, respectively (S4a Fig).	RESULTS
77	94	crystal structure	evidence	SEC-MALS analysis of rPdulΔEP is consistent with a dimer (as observed in the crystal structure) with a weighted average (Mw) and number average (Mn) of the molar mass of 58.4 kDa +/− 11.2% and 58.8 kDa +/− 10.9%, respectively (S4a Fig).	RESULTS
103	166	weighted average (Mw) and number average (Mn) of the molar mass	evidence	SEC-MALS analysis of rPdulΔEP is consistent with a dimer (as observed in the crystal structure) with a weighted average (Mw) and number average (Mn) of the molar mass of 58.4 kDa +/− 11.2% and 58.8 kDa +/− 10.9%, respectively (S4a Fig).	RESULTS
0	5	rPduL	protein	rPduL full length runs as Mw = 140.3 kDa +/− 1.2% and Mn = 140.5 kDa +/− 1.2%.	RESULTS
6	17	full length	protein_state	rPduL full length runs as Mw = 140.3 kDa +/− 1.2% and Mn = 140.5 kDa +/− 1.2%.	RESULTS
26	28	Mw	evidence	rPduL full length runs as Mw = 140.3 kDa +/− 1.2% and Mn = 140.5 kDa +/− 1.2%.	RESULTS
54	56	Mn	evidence	rPduL full length runs as Mw = 140.3 kDa +/− 1.2% and Mn = 140.5 kDa +/− 1.2%.	RESULTS
43	55	six subunits	oligomeric_state	This corresponds to an oligomeric state of six subunits (calculated molecular weight of 144 kDa).	RESULTS
68	84	molecular weight	evidence	This corresponds to an oligomeric state of six subunits (calculated molecular weight of 144 kDa).	RESULTS
62	64	EP	structure_element	Collectively, these data strongly suggest that the N-terminal EP of PduL plays a role in defining the quaternary structure of the protein.	RESULTS
68	72	PduL	protein_type	Collectively, these data strongly suggest that the N-terminal EP of PduL plays a role in defining the quaternary structure of the protein.	RESULTS
4	7	BMC	complex_assembly	The BMC shell not only sequesters specific enzymes but also their cofactors, thereby establishing a private cofactor pool dedicated to the encapsulated reactions.	DISCUSS
8	13	shell	structure_element	The BMC shell not only sequesters specific enzymes but also their cofactors, thereby establishing a private cofactor pool dedicated to the encapsulated reactions.	DISCUSS
3	12	catabolic	protein_state	In catabolic BMCs, CoA and NAD+ must be continually recycled within the organelle (Fig 1).	DISCUSS
13	17	BMCs	complex_assembly	In catabolic BMCs, CoA and NAD+ must be continually recycled within the organelle (Fig 1).	DISCUSS
19	22	CoA	chemical	In catabolic BMCs, CoA and NAD+ must be continually recycled within the organelle (Fig 1).	DISCUSS
27	31	NAD+	chemical	In catabolic BMCs, CoA and NAD+ must be continually recycled within the organelle (Fig 1).	DISCUSS
47	69	aldehyde dehydrogenase	protein_type	Homologs of the predominant cofactor utilizer (aldehyde dehydrogenase) and NAD+ regenerator (alcohol dehydrogenase) have been structurally characterized, but until now structural information was lacking for PduL, which recycles CoA in the organelle lumen.	DISCUSS
75	79	NAD+	chemical	Homologs of the predominant cofactor utilizer (aldehyde dehydrogenase) and NAD+ regenerator (alcohol dehydrogenase) have been structurally characterized, but until now structural information was lacking for PduL, which recycles CoA in the organelle lumen.	DISCUSS
93	114	alcohol dehydrogenase	protein_type	Homologs of the predominant cofactor utilizer (aldehyde dehydrogenase) and NAD+ regenerator (alcohol dehydrogenase) have been structurally characterized, but until now structural information was lacking for PduL, which recycles CoA in the organelle lumen.	DISCUSS
207	211	PduL	protein_type	Homologs of the predominant cofactor utilizer (aldehyde dehydrogenase) and NAD+ regenerator (alcohol dehydrogenase) have been structurally characterized, but until now structural information was lacking for PduL, which recycles CoA in the organelle lumen.	DISCUSS
228	231	CoA	chemical	Homologs of the predominant cofactor utilizer (aldehyde dehydrogenase) and NAD+ regenerator (alcohol dehydrogenase) have been structurally characterized, but until now structural information was lacking for PduL, which recycles CoA in the organelle lumen.	DISCUSS
21	33	housekeeping	protein_state	Curiously, while the housekeeping Pta could provide this function, and indeed does so in the case of one type of ethanolamine-utilizing (EUT) BMC, the evolutionarily unrelated PduL fulfills this function for the majority of metabolosomes using a novel structure and active site for convergent evolution of function.	DISCUSS
34	37	Pta	protein_type	Curiously, while the housekeeping Pta could provide this function, and indeed does so in the case of one type of ethanolamine-utilizing (EUT) BMC, the evolutionarily unrelated PduL fulfills this function for the majority of metabolosomes using a novel structure and active site for convergent evolution of function.	DISCUSS
113	145	ethanolamine-utilizing (EUT) BMC	complex_assembly	Curiously, while the housekeeping Pta could provide this function, and indeed does so in the case of one type of ethanolamine-utilizing (EUT) BMC, the evolutionarily unrelated PduL fulfills this function for the majority of metabolosomes using a novel structure and active site for convergent evolution of function.	DISCUSS
176	180	PduL	protein_type	Curiously, while the housekeeping Pta could provide this function, and indeed does so in the case of one type of ethanolamine-utilizing (EUT) BMC, the evolutionarily unrelated PduL fulfills this function for the majority of metabolosomes using a novel structure and active site for convergent evolution of function.	DISCUSS
224	237	metabolosomes	complex_assembly	Curiously, while the housekeeping Pta could provide this function, and indeed does so in the case of one type of ethanolamine-utilizing (EUT) BMC, the evolutionarily unrelated PduL fulfills this function for the majority of metabolosomes using a novel structure and active site for convergent evolution of function.	DISCUSS
252	261	structure	evidence	Curiously, while the housekeeping Pta could provide this function, and indeed does so in the case of one type of ethanolamine-utilizing (EUT) BMC, the evolutionarily unrelated PduL fulfills this function for the majority of metabolosomes using a novel structure and active site for convergent evolution of function.	DISCUSS
266	277	active site	site	Curiously, while the housekeeping Pta could provide this function, and indeed does so in the case of one type of ethanolamine-utilizing (EUT) BMC, the evolutionarily unrelated PduL fulfills this function for the majority of metabolosomes using a novel structure and active site for convergent evolution of function.	DISCUSS
26	30	PduL	protein_type	The Tertiary Structure of PduL Is Formed by Discontinuous Segments of Primary Structure	DISCUSS
4	13	structure	evidence	The structure of PduL consists of two β-barrel domains capped by short alpha helical segments (Fig 2b).	DISCUSS
17	21	PduL	protein_type	The structure of PduL consists of two β-barrel domains capped by short alpha helical segments (Fig 2b).	DISCUSS
34	54	two β-barrel domains	structure_element	The structure of PduL consists of two β-barrel domains capped by short alpha helical segments (Fig 2b).	DISCUSS
65	93	short alpha helical segments	structure_element	The structure of PduL consists of two β-barrel domains capped by short alpha helical segments (Fig 2b).	DISCUSS
47	60	superimposing	experimental_method	The two domains are structurally very similar (superimposing with a rmsd of 1.34 Å (over 123 out of 320/348 aligned backbone atoms, S5a Fig).	DISCUSS
68	72	rmsd	evidence	The two domains are structurally very similar (superimposing with a rmsd of 1.34 Å (over 123 out of 320/348 aligned backbone atoms, S5a Fig).	DISCUSS
88	98	RHxH motif	structure_element	However, the amino acid sequences of the two domains are only 16% identical (mainly the RHxH motif, β2 and β10), and 34% similar.	DISCUSS
100	102	β2	structure_element	However, the amino acid sequences of the two domains are only 16% identical (mainly the RHxH motif, β2 and β10), and 34% similar.	DISCUSS
107	110	β10	structure_element	However, the amino acid sequences of the two domains are only 16% identical (mainly the RHxH motif, β2 and β10), and 34% similar.	DISCUSS
4	13	structure	evidence	Our structure reveals that the two assigned PF06130 domains (Fig 3) do not form structurally discrete units; this reduces the apparent sequence conservation at the level of primary structure.	DISCUSS
44	51	PF06130	structure_element	Our structure reveals that the two assigned PF06130 domains (Fig 3) do not form structurally discrete units; this reduces the apparent sequence conservation at the level of primary structure.	DISCUSS
4	10	strand	structure_element	One strand of the domain 1 beta barrel (shown in blue in Fig 2) is contributed by the N-terminus, while the rest of the domain is formed by the residues from the C-terminal half of the protein.	DISCUSS
18	26	domain 1	structure_element	One strand of the domain 1 beta barrel (shown in blue in Fig 2) is contributed by the N-terminus, while the rest of the domain is formed by the residues from the C-terminal half of the protein.	DISCUSS
27	38	beta barrel	structure_element	One strand of the domain 1 beta barrel (shown in blue in Fig 2) is contributed by the N-terminus, while the rest of the domain is formed by the residues from the C-terminal half of the protein.	DISCUSS
162	177	C-terminal half	structure_element	One strand of the domain 1 beta barrel (shown in blue in Fig 2) is contributed by the N-terminus, while the rest of the domain is formed by the residues from the C-terminal half of the protein.	DISCUSS
185	192	protein	protein_type	One strand of the domain 1 beta barrel (shown in blue in Fig 2) is contributed by the N-terminus, while the rest of the domain is formed by the residues from the C-terminal half of the protein.	DISCUSS
5	12	aligned	experimental_method	When aligned by structure, the β1 strand of the first domain (Fig 2a and 2b, blue) corresponds to the final strand of the second domain (β9), effectively making the domains continuous if the first strand was transplanted to the C-terminus.	DISCUSS
16	25	structure	evidence	When aligned by structure, the β1 strand of the first domain (Fig 2a and 2b, blue) corresponds to the final strand of the second domain (β9), effectively making the domains continuous if the first strand was transplanted to the C-terminus.	DISCUSS
31	40	β1 strand	structure_element	When aligned by structure, the β1 strand of the first domain (Fig 2a and 2b, blue) corresponds to the final strand of the second domain (β9), effectively making the domains continuous if the first strand was transplanted to the C-terminus.	DISCUSS
48	60	first domain	structure_element	When aligned by structure, the β1 strand of the first domain (Fig 2a and 2b, blue) corresponds to the final strand of the second domain (β9), effectively making the domains continuous if the first strand was transplanted to the C-terminus.	DISCUSS
102	114	final strand	structure_element	When aligned by structure, the β1 strand of the first domain (Fig 2a and 2b, blue) corresponds to the final strand of the second domain (β9), effectively making the domains continuous if the first strand was transplanted to the C-terminus.	DISCUSS
122	135	second domain	structure_element	When aligned by structure, the β1 strand of the first domain (Fig 2a and 2b, blue) corresponds to the final strand of the second domain (β9), effectively making the domains continuous if the first strand was transplanted to the C-terminus.	DISCUSS
137	139	β9	structure_element	When aligned by structure, the β1 strand of the first domain (Fig 2a and 2b, blue) corresponds to the final strand of the second domain (β9), effectively making the domains continuous if the first strand was transplanted to the C-terminus.	DISCUSS
39	48	structure	evidence	Refined domain assignment based on our structure should be able to predict domains of PF06130 homologs much more accurately.	DISCUSS
86	93	PF06130	structure_element	Refined domain assignment based on our structure should be able to predict domains of PF06130 homologs much more accurately.	DISCUSS
38	42	PduL	protein_type	The closest structural homolog of the PduL barrel domain is a subdomain of a multienzyme complex, the alpha subunit of ethylbenzene dehydrogenase (S5b Fig, rmsd of 2.26 Å over 226 aligned atoms consisting of one beta barrel and one capping helix).	DISCUSS
43	56	barrel domain	structure_element	The closest structural homolog of the PduL barrel domain is a subdomain of a multienzyme complex, the alpha subunit of ethylbenzene dehydrogenase (S5b Fig, rmsd of 2.26 Å over 226 aligned atoms consisting of one beta barrel and one capping helix).	DISCUSS
102	115	alpha subunit	structure_element	The closest structural homolog of the PduL barrel domain is a subdomain of a multienzyme complex, the alpha subunit of ethylbenzene dehydrogenase (S5b Fig, rmsd of 2.26 Å over 226 aligned atoms consisting of one beta barrel and one capping helix).	DISCUSS
119	145	ethylbenzene dehydrogenase	protein_type	The closest structural homolog of the PduL barrel domain is a subdomain of a multienzyme complex, the alpha subunit of ethylbenzene dehydrogenase (S5b Fig, rmsd of 2.26 Å over 226 aligned atoms consisting of one beta barrel and one capping helix).	DISCUSS
156	160	rmsd	evidence	The closest structural homolog of the PduL barrel domain is a subdomain of a multienzyme complex, the alpha subunit of ethylbenzene dehydrogenase (S5b Fig, rmsd of 2.26 Å over 226 aligned atoms consisting of one beta barrel and one capping helix).	DISCUSS
212	223	beta barrel	structure_element	The closest structural homolog of the PduL barrel domain is a subdomain of a multienzyme complex, the alpha subunit of ethylbenzene dehydrogenase (S5b Fig, rmsd of 2.26 Å over 226 aligned atoms consisting of one beta barrel and one capping helix).	DISCUSS
232	245	capping helix	structure_element	The closest structural homolog of the PduL barrel domain is a subdomain of a multienzyme complex, the alpha subunit of ethylbenzene dehydrogenase (S5b Fig, rmsd of 2.26 Å over 226 aligned atoms consisting of one beta barrel and one capping helix).	DISCUSS
15	19	PduL	protein_type	In contrast to PduL, there is only one barrel present in ethylbenzene dehydrogenase, and there is no comparable active site arrangement.	DISCUSS
39	45	barrel	structure_element	In contrast to PduL, there is only one barrel present in ethylbenzene dehydrogenase, and there is no comparable active site arrangement.	DISCUSS
57	83	ethylbenzene dehydrogenase	protein_type	In contrast to PduL, there is only one barrel present in ethylbenzene dehydrogenase, and there is no comparable active site arrangement.	DISCUSS
112	123	active site	site	In contrast to PduL, there is only one barrel present in ethylbenzene dehydrogenase, and there is no comparable active site arrangement.	DISCUSS
4	8	PduL	protein_type	The PduL signature primary structure, two PF06130 domains, occurs in some multidomain proteins, most of them annotated as Acks, suggesting that PduL may also replace Pta in variants of the phosphotransacetylase-Ack pathway.	DISCUSS
42	49	PF06130	structure_element	The PduL signature primary structure, two PF06130 domains, occurs in some multidomain proteins, most of them annotated as Acks, suggesting that PduL may also replace Pta in variants of the phosphotransacetylase-Ack pathway.	DISCUSS
122	126	Acks	protein_type	The PduL signature primary structure, two PF06130 domains, occurs in some multidomain proteins, most of them annotated as Acks, suggesting that PduL may also replace Pta in variants of the phosphotransacetylase-Ack pathway.	DISCUSS
144	148	PduL	protein_type	The PduL signature primary structure, two PF06130 domains, occurs in some multidomain proteins, most of them annotated as Acks, suggesting that PduL may also replace Pta in variants of the phosphotransacetylase-Ack pathway.	DISCUSS
166	169	Pta	protein_type	The PduL signature primary structure, two PF06130 domains, occurs in some multidomain proteins, most of them annotated as Acks, suggesting that PduL may also replace Pta in variants of the phosphotransacetylase-Ack pathway.	DISCUSS
189	210	phosphotransacetylase	protein_type	The PduL signature primary structure, two PF06130 domains, occurs in some multidomain proteins, most of them annotated as Acks, suggesting that PduL may also replace Pta in variants of the phosphotransacetylase-Ack pathway.	DISCUSS
211	214	Ack	protein_type	The PduL signature primary structure, two PF06130 domains, occurs in some multidomain proteins, most of them annotated as Acks, suggesting that PduL may also replace Pta in variants of the phosphotransacetylase-Ack pathway.	DISCUSS
6	10	PduL	protein_type	These PduL homologs lack EPs, and their fusion to Ack may have evolved as a way to facilitate substrate channeling between the two enzymes.	DISCUSS
20	24	lack	protein_state	These PduL homologs lack EPs, and their fusion to Ack may have evolved as a way to facilitate substrate channeling between the two enzymes.	DISCUSS
25	28	EPs	structure_element	These PduL homologs lack EPs, and their fusion to Ack may have evolved as a way to facilitate substrate channeling between the two enzymes.	DISCUSS
34	39	their	protein_type	These PduL homologs lack EPs, and their fusion to Ack may have evolved as a way to facilitate substrate channeling between the two enzymes.	DISCUSS
50	53	Ack	protein_type	These PduL homologs lack EPs, and their fusion to Ack may have evolved as a way to facilitate substrate channeling between the two enzymes.	DISCUSS
17	29	Metabolosome	complex_assembly	Implications for Metabolosome Core Assembly	DISCUSS
4	7	BMC	complex_assembly	For BMC-encapsulated proteins to properly function together, they must be targeted to the lumen and assemble into an organization that facilitates substrate/product channeling among the different catalytic sites of the signature and core enzymes.	DISCUSS
196	211	catalytic sites	site	For BMC-encapsulated proteins to properly function together, they must be targeted to the lumen and assemble into an organization that facilitates substrate/product channeling among the different catalytic sites of the signature and core enzymes.	DISCUSS
4	24	N-terminal extension	structure_element	The N-terminal extension on PduL homologs may serve both of these functions.	DISCUSS
28	32	PduL	protein_type	The N-terminal extension on PduL homologs may serve both of these functions.	DISCUSS
0	13	The extension	structure_element	The extension shares many features with previously characterized EPs: it is present only in homologs associated with BMC loci, and it is predicted to form an amphipathic α-helix.	DISCUSS
65	68	EPs	structure_element	The extension shares many features with previously characterized EPs: it is present only in homologs associated with BMC loci, and it is predicted to form an amphipathic α-helix.	DISCUSS
117	125	BMC loci	gene	The extension shares many features with previously characterized EPs: it is present only in homologs associated with BMC loci, and it is predicted to form an amphipathic α-helix.	DISCUSS
158	169	amphipathic	protein_state	The extension shares many features with previously characterized EPs: it is present only in homologs associated with BMC loci, and it is predicted to form an amphipathic α-helix.	DISCUSS
170	177	α-helix	structure_element	The extension shares many features with previously characterized EPs: it is present only in homologs associated with BMC loci, and it is predicted to form an amphipathic α-helix.	DISCUSS
14	21	removal	experimental_method	Moreover, its removal affects the oligomeric state of the protein.	DISCUSS
0	2	EP	structure_element	EP-mediated oligomerization has been observed for the signature and core BMC enzymes; for example, full-length propanediol dehydratase and ethanolamine ammonia-lyase (signature enzymes for PDU and EUT BMCs) subunits are also insoluble, but become soluble upon removal of the predicted EP.	DISCUSS
73	76	BMC	complex_assembly	EP-mediated oligomerization has been observed for the signature and core BMC enzymes; for example, full-length propanediol dehydratase and ethanolamine ammonia-lyase (signature enzymes for PDU and EUT BMCs) subunits are also insoluble, but become soluble upon removal of the predicted EP.	DISCUSS
99	110	full-length	protein_state	EP-mediated oligomerization has been observed for the signature and core BMC enzymes; for example, full-length propanediol dehydratase and ethanolamine ammonia-lyase (signature enzymes for PDU and EUT BMCs) subunits are also insoluble, but become soluble upon removal of the predicted EP.	DISCUSS
111	134	propanediol dehydratase	protein_type	EP-mediated oligomerization has been observed for the signature and core BMC enzymes; for example, full-length propanediol dehydratase and ethanolamine ammonia-lyase (signature enzymes for PDU and EUT BMCs) subunits are also insoluble, but become soluble upon removal of the predicted EP.	DISCUSS
139	165	ethanolamine ammonia-lyase	protein_type	EP-mediated oligomerization has been observed for the signature and core BMC enzymes; for example, full-length propanediol dehydratase and ethanolamine ammonia-lyase (signature enzymes for PDU and EUT BMCs) subunits are also insoluble, but become soluble upon removal of the predicted EP.	DISCUSS
189	192	PDU	complex_assembly	EP-mediated oligomerization has been observed for the signature and core BMC enzymes; for example, full-length propanediol dehydratase and ethanolamine ammonia-lyase (signature enzymes for PDU and EUT BMCs) subunits are also insoluble, but become soluble upon removal of the predicted EP.	DISCUSS
197	205	EUT BMCs	complex_assembly	EP-mediated oligomerization has been observed for the signature and core BMC enzymes; for example, full-length propanediol dehydratase and ethanolamine ammonia-lyase (signature enzymes for PDU and EUT BMCs) subunits are also insoluble, but become soluble upon removal of the predicted EP.	DISCUSS
285	287	EP	structure_element	EP-mediated oligomerization has been observed for the signature and core BMC enzymes; for example, full-length propanediol dehydratase and ethanolamine ammonia-lyase (signature enzymes for PDU and EUT BMCs) subunits are also insoluble, but become soluble upon removal of the predicted EP.	DISCUSS
0	5	sPduL	protein	sPduL has also previously been reported to localize to inclusion bodies when overexpressed; we show here that this is dependent on the presence of the EP.	DISCUSS
77	90	overexpressed	experimental_method	sPduL has also previously been reported to localize to inclusion bodies when overexpressed; we show here that this is dependent on the presence of the EP.	DISCUSS
151	153	EP	structure_element	sPduL has also previously been reported to localize to inclusion bodies when overexpressed; we show here that this is dependent on the presence of the EP.	DISCUSS
23	25	EP	structure_element	This propensity of the EP to cause proteins to form complexes (Fig 5) might not be a coincidence, but could be a necessary step in the assembly of BMCs.	DISCUSS
147	151	BMCs	complex_assembly	This propensity of the EP to cause proteins to form complexes (Fig 5) might not be a coincidence, but could be a necessary step in the assembly of BMCs.	DISCUSS
87	99	metabolosome	complex_assembly	Structured aggregation of the core enzymes has been proposed to be the initial step in metabolosome assembly and is known to be the first step of β-carboxysome biogenesis, where the core enzyme Ribulose Bisphosphate Carboxylase/Oxygenase (RuBisCO) is aggregated by the CcmM protein.	DISCUSS
194	237	Ribulose Bisphosphate Carboxylase/Oxygenase	protein_type	Structured aggregation of the core enzymes has been proposed to be the initial step in metabolosome assembly and is known to be the first step of β-carboxysome biogenesis, where the core enzyme Ribulose Bisphosphate Carboxylase/Oxygenase (RuBisCO) is aggregated by the CcmM protein.	DISCUSS
239	246	RuBisCO	protein_type	Structured aggregation of the core enzymes has been proposed to be the initial step in metabolosome assembly and is known to be the first step of β-carboxysome biogenesis, where the core enzyme Ribulose Bisphosphate Carboxylase/Oxygenase (RuBisCO) is aggregated by the CcmM protein.	DISCUSS
269	273	CcmM	protein_type	Structured aggregation of the core enzymes has been proposed to be the initial step in metabolosome assembly and is known to be the first step of β-carboxysome biogenesis, where the core enzyme Ribulose Bisphosphate Carboxylase/Oxygenase (RuBisCO) is aggregated by the CcmM protein.	DISCUSS
10	15	CsoS2	protein_type	Likewise, CsoS2, a protein in the α-carboxysome core, also aggregates when purified and is proposed to facilitate the nucleation and encapsulation of RuBisCO molecules in the lumen of the organelle.	DISCUSS
34	47	α-carboxysome	complex_assembly	Likewise, CsoS2, a protein in the α-carboxysome core, also aggregates when purified and is proposed to facilitate the nucleation and encapsulation of RuBisCO molecules in the lumen of the organelle.	DISCUSS
150	157	RuBisCO	protein_type	Likewise, CsoS2, a protein in the α-carboxysome core, also aggregates when purified and is proposed to facilitate the nucleation and encapsulation of RuBisCO molecules in the lumen of the organelle.	DISCUSS
14	17	EPs	structure_element	This role for EPs in BMC assembly is in addition to their interaction with shell proteins.	DISCUSS
21	24	BMC	complex_assembly	This role for EPs in BMC assembly is in addition to their interaction with shell proteins.	DISCUSS
14	18	PduL	protein_type	Moreover, the PduL crystal structures offer a clue as to how required cofactors enter the BMC lumen during assembly.	DISCUSS
19	37	crystal structures	evidence	Moreover, the PduL crystal structures offer a clue as to how required cofactors enter the BMC lumen during assembly.	DISCUSS
90	93	BMC	complex_assembly	Moreover, the PduL crystal structures offer a clue as to how required cofactors enter the BMC lumen during assembly.	DISCUSS
5	8	CoA	chemical	Free CoA and NAD+/H could potentially be bound to the enzymes as the core assembles and is encapsulated.	DISCUSS
13	17	NAD+	chemical	Free CoA and NAD+/H could potentially be bound to the enzymes as the core assembles and is encapsulated.	DISCUSS
18	19	H	chemical	Free CoA and NAD+/H could potentially be bound to the enzymes as the core assembles and is encapsulated.	DISCUSS
4	8	PduL	protein_type	Our PduL crystals contained CoA that was captured from the Escherichia coli cytosol, indicating that the “ground state” of PduL is in the CoA-bound form; this could provide an elegantly simple means of guaranteeing a 1:1 ratio of CoA:PduL within the metabolosome lumen.	DISCUSS
9	17	crystals	evidence	Our PduL crystals contained CoA that was captured from the Escherichia coli cytosol, indicating that the “ground state” of PduL is in the CoA-bound form; this could provide an elegantly simple means of guaranteeing a 1:1 ratio of CoA:PduL within the metabolosome lumen.	DISCUSS
28	31	CoA	chemical	Our PduL crystals contained CoA that was captured from the Escherichia coli cytosol, indicating that the “ground state” of PduL is in the CoA-bound form; this could provide an elegantly simple means of guaranteeing a 1:1 ratio of CoA:PduL within the metabolosome lumen.	DISCUSS
59	75	Escherichia coli	species	Our PduL crystals contained CoA that was captured from the Escherichia coli cytosol, indicating that the “ground state” of PduL is in the CoA-bound form; this could provide an elegantly simple means of guaranteeing a 1:1 ratio of CoA:PduL within the metabolosome lumen.	DISCUSS
123	127	PduL	protein_type	Our PduL crystals contained CoA that was captured from the Escherichia coli cytosol, indicating that the “ground state” of PduL is in the CoA-bound form; this could provide an elegantly simple means of guaranteeing a 1:1 ratio of CoA:PduL within the metabolosome lumen.	DISCUSS
138	147	CoA-bound	protein_state	Our PduL crystals contained CoA that was captured from the Escherichia coli cytosol, indicating that the “ground state” of PduL is in the CoA-bound form; this could provide an elegantly simple means of guaranteeing a 1:1 ratio of CoA:PduL within the metabolosome lumen.	DISCUSS
230	238	CoA:PduL	complex_assembly	Our PduL crystals contained CoA that was captured from the Escherichia coli cytosol, indicating that the “ground state” of PduL is in the CoA-bound form; this could provide an elegantly simple means of guaranteeing a 1:1 ratio of CoA:PduL within the metabolosome lumen.	DISCUSS
250	262	metabolosome	complex_assembly	Our PduL crystals contained CoA that was captured from the Escherichia coli cytosol, indicating that the “ground state” of PduL is in the CoA-bound form; this could provide an elegantly simple means of guaranteeing a 1:1 ratio of CoA:PduL within the metabolosome lumen.	DISCUSS
0	11	Active Site	site	Active Site Identification and Structural Insights into Catalysis	DISCUSS
4	15	active site	site	The active site of PduL is formed at the interface of the two structural domains (Fig 2b).	DISCUSS
19	23	PduL	protein_type	The active site of PduL is formed at the interface of the two structural domains (Fig 2b).	DISCUSS
41	50	interface	site	The active site of PduL is formed at the interface of the two structural domains (Fig 2b).	DISCUSS
73	80	domains	structure_element	The active site of PduL is formed at the interface of the two structural domains (Fig 2b).	DISCUSS
95	106	active site	site	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
117	133	highly conserved	protein_state	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
164	167	CoA	chemical	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
201	206	Ser45	residue_name_number	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
208	213	Lys70	residue_name_number	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
215	220	Arg97	residue_name_number	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
222	227	Leu99	residue_name_number	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
229	235	His204	residue_name_number	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
237	243	Asn211	residue_name_number	As expected, the amino acid sequence conservation is highest in the region around the proposed active site (Fig 4d); highly conserved residues are also involved in CoA binding (Figs 2a and 3, residues Ser45, Lys70, Arg97, Leu99, His204, Asn211).	DISCUSS
11	38	metal-coordinating residues	site	All of the metal-coordinating residues (Fig 2a) are absolutely conserved, implicating them in catalysis or the correct spatial orientation of the substrates.	DISCUSS
52	72	absolutely conserved	protein_state	All of the metal-coordinating residues (Fig 2a) are absolutely conserved, implicating them in catalysis or the correct spatial orientation of the substrates.	DISCUSS
0	6	Arg103	residue_name_number	Arg103, which contacts the phosphate (Fig 4b), is present in all PduL homologs.	DISCUSS
27	36	phosphate	chemical	Arg103, which contacts the phosphate (Fig 4b), is present in all PduL homologs.	DISCUSS
65	69	PduL	protein_type	Arg103, which contacts the phosphate (Fig 4b), is present in all PduL homologs.	DISCUSS
53	56	CoA	chemical	The close resemblance between the structures binding CoA and phosphate likely indicates that no large changes in protein conformation are involved in catalysis, and that our crystal structures are representative of the active form.	DISCUSS
61	70	phosphate	chemical	The close resemblance between the structures binding CoA and phosphate likely indicates that no large changes in protein conformation are involved in catalysis, and that our crystal structures are representative of the active form.	DISCUSS
174	192	crystal structures	evidence	The close resemblance between the structures binding CoA and phosphate likely indicates that no large changes in protein conformation are involved in catalysis, and that our crystal structures are representative of the active form.	DISCUSS
219	225	active	protein_state	The close resemblance between the structures binding CoA and phosphate likely indicates that no large changes in protein conformation are involved in catalysis, and that our crystal structures are representative of the active form.	DISCUSS
49	54	rPduL	protein	The native substrate for the forward reaction of rPduL and pPduL, propionyl-CoA, most likely binds to the enzyme in the same way at the observed nucleotide and pantothenic acid moiety, but the propionyl group in the CoA-thioester might point in a different direction.	DISCUSS
59	64	pPduL	protein	The native substrate for the forward reaction of rPduL and pPduL, propionyl-CoA, most likely binds to the enzyme in the same way at the observed nucleotide and pantothenic acid moiety, but the propionyl group in the CoA-thioester might point in a different direction.	DISCUSS
66	79	propionyl-CoA	chemical	The native substrate for the forward reaction of rPduL and pPduL, propionyl-CoA, most likely binds to the enzyme in the same way at the observed nucleotide and pantothenic acid moiety, but the propionyl group in the CoA-thioester might point in a different direction.	DISCUSS
145	155	nucleotide	chemical	The native substrate for the forward reaction of rPduL and pPduL, propionyl-CoA, most likely binds to the enzyme in the same way at the observed nucleotide and pantothenic acid moiety, but the propionyl group in the CoA-thioester might point in a different direction.	DISCUSS
160	176	pantothenic acid	chemical	The native substrate for the forward reaction of rPduL and pPduL, propionyl-CoA, most likely binds to the enzyme in the same way at the observed nucleotide and pantothenic acid moiety, but the propionyl group in the CoA-thioester might point in a different direction.	DISCUSS
216	229	CoA-thioester	chemical	The native substrate for the forward reaction of rPduL and pPduL, propionyl-CoA, most likely binds to the enzyme in the same way at the observed nucleotide and pantothenic acid moiety, but the propionyl group in the CoA-thioester might point in a different direction.	DISCUSS
11	17	pocket	site	There is a pocket nearby the active site between the well-conserved residues Ser45 and Ala154, which could accommodate the propionyl group (S6 Fig).	DISCUSS
29	40	active site	site	There is a pocket nearby the active site between the well-conserved residues Ser45 and Ala154, which could accommodate the propionyl group (S6 Fig).	DISCUSS
53	67	well-conserved	protein_state	There is a pocket nearby the active site between the well-conserved residues Ser45 and Ala154, which could accommodate the propionyl group (S6 Fig).	DISCUSS
77	82	Ser45	residue_name_number	There is a pocket nearby the active site between the well-conserved residues Ser45 and Ala154, which could accommodate the propionyl group (S6 Fig).	DISCUSS
87	93	Ala154	residue_name_number	There is a pocket nearby the active site between the well-conserved residues Ser45 and Ala154, which could accommodate the propionyl group (S6 Fig).	DISCUSS
2	16	homology model	experimental_method	A homology model of sPduL indicates that the residues making up this pocket and the surrounding active site region are identical to that of rPduL, which is not surprising, because these two homologs presumably have the same propionyl-CoA substrate.	DISCUSS
20	25	sPduL	protein	A homology model of sPduL indicates that the residues making up this pocket and the surrounding active site region are identical to that of rPduL, which is not surprising, because these two homologs presumably have the same propionyl-CoA substrate.	DISCUSS
69	75	pocket	site	A homology model of sPduL indicates that the residues making up this pocket and the surrounding active site region are identical to that of rPduL, which is not surprising, because these two homologs presumably have the same propionyl-CoA substrate.	DISCUSS
96	107	active site	site	A homology model of sPduL indicates that the residues making up this pocket and the surrounding active site region are identical to that of rPduL, which is not surprising, because these two homologs presumably have the same propionyl-CoA substrate.	DISCUSS
140	145	rPduL	protein	A homology model of sPduL indicates that the residues making up this pocket and the surrounding active site region are identical to that of rPduL, which is not surprising, because these two homologs presumably have the same propionyl-CoA substrate.	DISCUSS
224	237	propionyl-CoA	chemical	A homology model of sPduL indicates that the residues making up this pocket and the surrounding active site region are identical to that of rPduL, which is not surprising, because these two homologs presumably have the same propionyl-CoA substrate.	DISCUSS
4	18	homology model	experimental_method	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
22	27	pPduL	protein	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
70	76	pocket	site	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
127	138	active site	site	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
140	145	Gln77	residue_name_number	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
149	154	rPduL	protein	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
172	180	tyrosine	residue_name	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
182	187	Tyr77	residue_name_number	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
192	197	pPduL	protein	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
230	235	pPduL	protein	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
263	273	lactyl-CoA	chemical	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
331	344	propionyl-CoA	chemical	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
365	373	aromatic	protein_state	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
374	381	residue	structure_element	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
444	448	PduL	protein_type	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
465	474	pvm locus	gene	The homology model of pPduL also has identical residues making up the pocket, but with a key difference in the vicinity of the active site: Gln77 of rPduL is replaced by a tyrosine (Tyr77) in pPduL. The physiological substrate of pPduL (Table 1) is thought to be lactyl-CoA, which contains an additional hydroxyl group relative to propionyl-CoA. The presence of an aromatic residue at this position may underlie the substrate preference of the PduL enzyme from the pvm locus.	DISCUSS
27	32	PduLs	protein_type	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
44	52	pvm loci	gene	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
54	59	Gln77	residue_name_number	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
87	90	Tyr	residue_name	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
94	97	Phe	residue_name	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
125	128	Gln	residue_name	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
132	135	Glu	residue_name	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
139	144	PduLs	protein_type	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
158	161	BMC	complex_assembly	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
181	188	acetyl-	chemical	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
192	205	propionyl-CoA	chemical	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
209	219	comparison	experimental_method	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
227	231	PduL	protein_type	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
232	243	active site	site	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
282	285	Pta	protein_type	Indeed, in the majority of PduLs encoded in pvm loci, Gln77 is substituted by either a Tyr or Phe, whereas it is typically a Gln or Glu in PduLs in all other BMC types that degrade acetyl- or propionyl-CoA. A comparison of the PduL active site to that of the functionally identical Pta suggests that the two enzymes have distinctly different mechanisms.	DISCUSS
27	30	Pta	protein_type	The catalytic mechanism of Pta involves the abstraction of a thiol hydrogen by an aspartate residue, resulting in the nucleophilic attack of thiolate upon the carbonyl carbon of acetyl-phosphate, oriented by an arginine and stabilized by a serine —there are no metals involved.	DISCUSS
82	91	aspartate	residue_name	The catalytic mechanism of Pta involves the abstraction of a thiol hydrogen by an aspartate residue, resulting in the nucleophilic attack of thiolate upon the carbonyl carbon of acetyl-phosphate, oriented by an arginine and stabilized by a serine —there are no metals involved.	DISCUSS
178	194	acetyl-phosphate	chemical	The catalytic mechanism of Pta involves the abstraction of a thiol hydrogen by an aspartate residue, resulting in the nucleophilic attack of thiolate upon the carbonyl carbon of acetyl-phosphate, oriented by an arginine and stabilized by a serine —there are no metals involved.	DISCUSS
211	219	arginine	residue_name	The catalytic mechanism of Pta involves the abstraction of a thiol hydrogen by an aspartate residue, resulting in the nucleophilic attack of thiolate upon the carbonyl carbon of acetyl-phosphate, oriented by an arginine and stabilized by a serine —there are no metals involved.	DISCUSS
240	246	serine	residue_name	The catalytic mechanism of Pta involves the abstraction of a thiol hydrogen by an aspartate residue, resulting in the nucleophilic attack of thiolate upon the carbonyl carbon of acetyl-phosphate, oriented by an arginine and stabilized by a serine —there are no metals involved.	DISCUSS
20	25	rPduL	protein	In contrast, in the rPduL structure, there are no conserved aspartate residues in or around the active site, and the only well-conserved glutamate residue in the active site is involved in coordinating one of the metal ions.	DISCUSS
26	35	structure	evidence	In contrast, in the rPduL structure, there are no conserved aspartate residues in or around the active site, and the only well-conserved glutamate residue in the active site is involved in coordinating one of the metal ions.	DISCUSS
60	69	aspartate	residue_name	In contrast, in the rPduL structure, there are no conserved aspartate residues in or around the active site, and the only well-conserved glutamate residue in the active site is involved in coordinating one of the metal ions.	DISCUSS
96	107	active site	site	In contrast, in the rPduL structure, there are no conserved aspartate residues in or around the active site, and the only well-conserved glutamate residue in the active site is involved in coordinating one of the metal ions.	DISCUSS
122	136	well-conserved	protein_state	In contrast, in the rPduL structure, there are no conserved aspartate residues in or around the active site, and the only well-conserved glutamate residue in the active site is involved in coordinating one of the metal ions.	DISCUSS
137	146	glutamate	residue_name	In contrast, in the rPduL structure, there are no conserved aspartate residues in or around the active site, and the only well-conserved glutamate residue in the active site is involved in coordinating one of the metal ions.	DISCUSS
162	173	active site	site	In contrast, in the rPduL structure, there are no conserved aspartate residues in or around the active site, and the only well-conserved glutamate residue in the active site is involved in coordinating one of the metal ions.	DISCUSS
44	50	acidic	protein_state	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
51	58	residue	structure_element	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
100	104	PduL	protein_type	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
119	138	dimetal active site	site	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
142	146	PduL	protein_type	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
212	221	phosphate	chemical	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
280	288	acyl-CoA	chemical	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
412	426	acyl-phosphate	chemical	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
471	483	phosphatases	protein_type	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
564	583	dimetal active site	site	These observations strongly suggest that an acidic residue is not directly involved in catalysis by PduL. Instead, the dimetal active site of PduL may create a nucleophile from one of the hydroxyl groups on free phosphate to attack the carbonyl carbon of the thioester bond of an acyl-CoA. In the reverse direction, the metal ion(s) could stabilize the thiolate anion that would attack the carbonyl carbon of an acyl-phosphate; a similar mechanism has been described for phosphatases where hydroxyl groups or hydroxide ions can act as a base when coordinated by a dimetal active site.	DISCUSS
4	14	structures	evidence	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
105	109	PduL	protein_type	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
111	120	Conserved	protein_state	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
137	148	active site	site	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
236	242	Ser127	residue_name_number	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
244	250	Arg103	residue_name_number	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
252	258	Arg194	residue_name_number	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
260	266	Gln107	residue_name_number	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
268	273	Gln74	residue_name_number	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
279	282	Gln	residue_name_number	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
283	288	Glu77	residue_name_number	Our structures provide the foundation for studies to elucidate the details of the catalytic mechanism of PduL. Conserved residues in the active site that may contribute to substrate binding and/or transition state stabilization include Ser127, Arg103, Arg194, Gln107, Gln74, and Gln/Glu77.	DISCUSS
7	22	phosphate-bound	protein_state	In the phosphate-bound crystal structure, Ser127 and Arg103 appear to position the phosphate (Fig 4b).	DISCUSS
23	40	crystal structure	evidence	In the phosphate-bound crystal structure, Ser127 and Arg103 appear to position the phosphate (Fig 4b).	DISCUSS
42	48	Ser127	residue_name_number	In the phosphate-bound crystal structure, Ser127 and Arg103 appear to position the phosphate (Fig 4b).	DISCUSS
53	59	Arg103	residue_name_number	In the phosphate-bound crystal structure, Ser127 and Arg103 appear to position the phosphate (Fig 4b).	DISCUSS
83	92	phosphate	chemical	In the phosphate-bound crystal structure, Ser127 and Arg103 appear to position the phosphate (Fig 4b).	DISCUSS
15	21	Arg103	residue_name_number	Alternatively, Arg103 might act as a base to render the phosphate more nucleophilic.	DISCUSS
56	65	phosphate	chemical	Alternatively, Arg103 might act as a base to render the phosphate more nucleophilic.	DISCUSS
25	30	Gln74	residue_name_number	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
32	35	Gln	residue_name_number	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
36	41	Glu77	residue_name_number	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
47	53	Arg194	residue_name_number	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
81	92	active site	site	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
101	104	CoA	protein_state	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
109	124	phosphate-bound	protein_state	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
125	143	crystal structures	evidence	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
272	286	acyl-phosphate	chemical	The functional groups of Gln74, Gln/Glu77, and Arg194 are directed away from the active site in both CoA and phosphate-bound crystal structures and do not appear to be involved in hydrogen bonding with these substrates, although they could be important for positioning an acyl-phosphate.	DISCUSS
9	18	CoA-bound	protein_state	The free CoA-bound form is presumably poised for attack upon an acyl-phosphate, indicating that the enzyme initially binds CoA as opposed to acyl-phosphate.	DISCUSS
64	78	acyl-phosphate	chemical	The free CoA-bound form is presumably poised for attack upon an acyl-phosphate, indicating that the enzyme initially binds CoA as opposed to acyl-phosphate.	DISCUSS
123	126	CoA	chemical	The free CoA-bound form is presumably poised for attack upon an acyl-phosphate, indicating that the enzyme initially binds CoA as opposed to acyl-phosphate.	DISCUSS
141	155	acyl-phosphate	chemical	The free CoA-bound form is presumably poised for attack upon an acyl-phosphate, indicating that the enzyme initially binds CoA as opposed to acyl-phosphate.	DISCUSS
53	62	CoA-bound	protein_state	This hypothesis is strengthened by the fact that the CoA-bound crystals were obtained without added CoA, indicating that the protein bound CoA from the E. coli expression strain and retained it throughout purification and crystallization.	DISCUSS
63	71	crystals	evidence	This hypothesis is strengthened by the fact that the CoA-bound crystals were obtained without added CoA, indicating that the protein bound CoA from the E. coli expression strain and retained it throughout purification and crystallization.	DISCUSS
100	103	CoA	chemical	This hypothesis is strengthened by the fact that the CoA-bound crystals were obtained without added CoA, indicating that the protein bound CoA from the E. coli expression strain and retained it throughout purification and crystallization.	DISCUSS
133	138	bound	protein_state	This hypothesis is strengthened by the fact that the CoA-bound crystals were obtained without added CoA, indicating that the protein bound CoA from the E. coli expression strain and retained it throughout purification and crystallization.	DISCUSS
139	142	CoA	chemical	This hypothesis is strengthened by the fact that the CoA-bound crystals were obtained without added CoA, indicating that the protein bound CoA from the E. coli expression strain and retained it throughout purification and crystallization.	DISCUSS
152	159	E. coli	species	This hypothesis is strengthened by the fact that the CoA-bound crystals were obtained without added CoA, indicating that the protein bound CoA from the E. coli expression strain and retained it throughout purification and crystallization.	DISCUSS
4	19	phosphate-bound	protein_state	The phosphate-bound structure indicates that in the opposite reaction direction phosphate is bound first, and then an acyl-CoA enters.	DISCUSS
20	29	structure	evidence	The phosphate-bound structure indicates that in the opposite reaction direction phosphate is bound first, and then an acyl-CoA enters.	DISCUSS
80	89	phosphate	chemical	The phosphate-bound structure indicates that in the opposite reaction direction phosphate is bound first, and then an acyl-CoA enters.	DISCUSS
118	126	acyl-CoA	chemical	The phosphate-bound structure indicates that in the opposite reaction direction phosphate is bound first, and then an acyl-CoA enters.	DISCUSS
24	42	crystal structures	evidence	The two high-resolution crystal structures presented here will serve as the foundation for mechanistic studies on this noncanonical PTAC enzyme to determine how the dimetal active site functions to catalyze both forward and reverse reactions.	DISCUSS
132	136	PTAC	protein_type	The two high-resolution crystal structures presented here will serve as the foundation for mechanistic studies on this noncanonical PTAC enzyme to determine how the dimetal active site functions to catalyze both forward and reverse reactions.	DISCUSS
165	184	dimetal active site	site	The two high-resolution crystal structures presented here will serve as the foundation for mechanistic studies on this noncanonical PTAC enzyme to determine how the dimetal active site functions to catalyze both forward and reverse reactions.	DISCUSS
47	51	PduL	protein_type	Functional, but Not Structural, Convergence of PduL and Pta	DISCUSS
56	59	Pta	protein_type	Functional, but Not Structural, Convergence of PduL and Pta	DISCUSS
0	4	PduL	protein_type	PduL and Pta are mechanistically and structurally distinct enzymes that catalyze the same reaction, a prime example of evolutionary convergence upon a function.	DISCUSS
9	12	Pta	protein_type	PduL and Pta are mechanistically and structurally distinct enzymes that catalyze the same reaction, a prime example of evolutionary convergence upon a function.	DISCUSS
155	167	active sites	site	There are several examples of such functional convergence of enzymes, although typically the enzymes have independently evolved similar, or even identical active sites; for example, the carbonic anhydrase family.	DISCUSS
186	204	carbonic anhydrase	protein_type	There are several examples of such functional convergence of enzymes, although typically the enzymes have independently evolved similar, or even identical active sites; for example, the carbonic anhydrase family.	DISCUSS
102	114	active sites	site	However, apparently less frequent is functional convergence that is supported by distinctly different active sites and accordingly catalytic mechanism, as revealed by comparison of the structures of Pta and PduL. One well-studied example of this is the β-lactamase family of enzymes, in which the active site of Class A and Class C enzymes involve serine-based catalysis, but Class B enzymes are metalloproteins.	DISCUSS
199	202	Pta	protein_type	However, apparently less frequent is functional convergence that is supported by distinctly different active sites and accordingly catalytic mechanism, as revealed by comparison of the structures of Pta and PduL. One well-studied example of this is the β-lactamase family of enzymes, in which the active site of Class A and Class C enzymes involve serine-based catalysis, but Class B enzymes are metalloproteins.	DISCUSS
207	211	PduL	protein_type	However, apparently less frequent is functional convergence that is supported by distinctly different active sites and accordingly catalytic mechanism, as revealed by comparison of the structures of Pta and PduL. One well-studied example of this is the β-lactamase family of enzymes, in which the active site of Class A and Class C enzymes involve serine-based catalysis, but Class B enzymes are metalloproteins.	DISCUSS
253	264	β-lactamase	protein_type	However, apparently less frequent is functional convergence that is supported by distinctly different active sites and accordingly catalytic mechanism, as revealed by comparison of the structures of Pta and PduL. One well-studied example of this is the β-lactamase family of enzymes, in which the active site of Class A and Class C enzymes involve serine-based catalysis, but Class B enzymes are metalloproteins.	DISCUSS
297	308	active site	site	However, apparently less frequent is functional convergence that is supported by distinctly different active sites and accordingly catalytic mechanism, as revealed by comparison of the structures of Pta and PduL. One well-studied example of this is the β-lactamase family of enzymes, in which the active site of Class A and Class C enzymes involve serine-based catalysis, but Class B enzymes are metalloproteins.	DISCUSS
396	411	metalloproteins	protein_type	However, apparently less frequent is functional convergence that is supported by distinctly different active sites and accordingly catalytic mechanism, as revealed by comparison of the structures of Pta and PduL. One well-studied example of this is the β-lactamase family of enzymes, in which the active site of Class A and Class C enzymes involve serine-based catalysis, but Class B enzymes are metalloproteins.	DISCUSS
27	39	β-lactamases	protein_type	This is not surprising, as β-lactamases are not so widespread among bacteria and therefore would be expected to have evolved independently several times as a defense mechanism against β-lactam antibiotics.	DISCUSS
68	76	bacteria	taxonomy_domain	This is not surprising, as β-lactamases are not so widespread among bacteria and therefore would be expected to have evolved independently several times as a defense mechanism against β-lactam antibiotics.	DISCUSS
20	28	bacteria	taxonomy_domain	However, nearly all bacteria encode Pta, and it is not immediately clear why the Pta/PduL functional convergence should have evolved: it would seem to be evolutionarily more resourceful for the Pta-encoding gene to be duplicated and repurposed for BMCs, as is apparently the case in one type of BMC—EUT1 (Table 1).	DISCUSS
36	39	Pta	protein_type	However, nearly all bacteria encode Pta, and it is not immediately clear why the Pta/PduL functional convergence should have evolved: it would seem to be evolutionarily more resourceful for the Pta-encoding gene to be duplicated and repurposed for BMCs, as is apparently the case in one type of BMC—EUT1 (Table 1).	DISCUSS
81	84	Pta	protein_type	However, nearly all bacteria encode Pta, and it is not immediately clear why the Pta/PduL functional convergence should have evolved: it would seem to be evolutionarily more resourceful for the Pta-encoding gene to be duplicated and repurposed for BMCs, as is apparently the case in one type of BMC—EUT1 (Table 1).	DISCUSS
85	89	PduL	protein_type	However, nearly all bacteria encode Pta, and it is not immediately clear why the Pta/PduL functional convergence should have evolved: it would seem to be evolutionarily more resourceful for the Pta-encoding gene to be duplicated and repurposed for BMCs, as is apparently the case in one type of BMC—EUT1 (Table 1).	DISCUSS
194	211	Pta-encoding gene	gene	However, nearly all bacteria encode Pta, and it is not immediately clear why the Pta/PduL functional convergence should have evolved: it would seem to be evolutionarily more resourceful for the Pta-encoding gene to be duplicated and repurposed for BMCs, as is apparently the case in one type of BMC—EUT1 (Table 1).	DISCUSS
248	252	BMCs	complex_assembly	However, nearly all bacteria encode Pta, and it is not immediately clear why the Pta/PduL functional convergence should have evolved: it would seem to be evolutionarily more resourceful for the Pta-encoding gene to be duplicated and repurposed for BMCs, as is apparently the case in one type of BMC—EUT1 (Table 1).	DISCUSS
295	303	BMC—EUT1	complex_assembly	However, nearly all bacteria encode Pta, and it is not immediately clear why the Pta/PduL functional convergence should have evolved: it would seem to be evolutionarily more resourceful for the Pta-encoding gene to be duplicated and repurposed for BMCs, as is apparently the case in one type of BMC—EUT1 (Table 1).	DISCUSS
90	94	PduL	protein_type	There could be some intrinsic biochemical difference between the two enzymes that renders PduL a more attractive candidate for encapsulation in a BMC—for example, PduL might be more amenable to tight packaging, or is better suited for the chemical microenvironment formed within the lumen of the BMC, which can be quite different from the cytosol.	DISCUSS
146	149	BMC	complex_assembly	There could be some intrinsic biochemical difference between the two enzymes that renders PduL a more attractive candidate for encapsulation in a BMC—for example, PduL might be more amenable to tight packaging, or is better suited for the chemical microenvironment formed within the lumen of the BMC, which can be quite different from the cytosol.	DISCUSS
163	167	PduL	protein_type	There could be some intrinsic biochemical difference between the two enzymes that renders PduL a more attractive candidate for encapsulation in a BMC—for example, PduL might be more amenable to tight packaging, or is better suited for the chemical microenvironment formed within the lumen of the BMC, which can be quite different from the cytosol.	DISCUSS
296	299	BMC	complex_assembly	There could be some intrinsic biochemical difference between the two enzymes that renders PduL a more attractive candidate for encapsulation in a BMC—for example, PduL might be more amenable to tight packaging, or is better suited for the chemical microenvironment formed within the lumen of the BMC, which can be quite different from the cytosol.	DISCUSS
47	52	PTACs	protein_type	Further biochemical comparison between the two PTACs will likely yield exciting results that could answer this evolutionary question.	DISCUSS
0	4	BMCs	complex_assembly	BMCs are now known to be widespread among the bacteria and are involved in critical segments of both autotrophic and heterotrophic biochemical pathways that confer to the host organism a competitive (metabolic) advantage in select niches.	DISCUSS
46	54	bacteria	taxonomy_domain	BMCs are now known to be widespread among the bacteria and are involved in critical segments of both autotrophic and heterotrophic biochemical pathways that confer to the host organism a competitive (metabolic) advantage in select niches.	DISCUSS
27	39	metabolosome	complex_assembly	As one of the three common metabolosome core enzymes, the structure of PduL provides a key missing piece to our structural picture of the shared core biochemistry (Fig 1) of functionally diverse catabolic BMCs.	DISCUSS
58	67	structure	evidence	As one of the three common metabolosome core enzymes, the structure of PduL provides a key missing piece to our structural picture of the shared core biochemistry (Fig 1) of functionally diverse catabolic BMCs.	DISCUSS
71	75	PduL	protein_type	As one of the three common metabolosome core enzymes, the structure of PduL provides a key missing piece to our structural picture of the shared core biochemistry (Fig 1) of functionally diverse catabolic BMCs.	DISCUSS
195	204	catabolic	protein_state	As one of the three common metabolosome core enzymes, the structure of PduL provides a key missing piece to our structural picture of the shared core biochemistry (Fig 1) of functionally diverse catabolic BMCs.	DISCUSS
205	209	BMCs	complex_assembly	As one of the three common metabolosome core enzymes, the structure of PduL provides a key missing piece to our structural picture of the shared core biochemistry (Fig 1) of functionally diverse catabolic BMCs.	DISCUSS
53	57	PduL	protein_type	We have observed the oligomeric state differences of PduL to correlate with the presence of an EP, providing new insight into the function of this sequence extension in BMC assembly.	DISCUSS
95	97	EP	structure_element	We have observed the oligomeric state differences of PduL to correlate with the presence of an EP, providing new insight into the function of this sequence extension in BMC assembly.	DISCUSS
169	172	BMC	complex_assembly	We have observed the oligomeric state differences of PduL to correlate with the presence of an EP, providing new insight into the function of this sequence extension in BMC assembly.	DISCUSS
42	52	Coenzyme A	chemical	Moreover, our results suggest a means for Coenzyme A incorporation during metabolosome biogenesis.	DISCUSS
74	86	metabolosome	complex_assembly	Moreover, our results suggest a means for Coenzyme A incorporation during metabolosome biogenesis.	DISCUSS
117	121	BMCs	complex_assembly	A detailed understanding of the underlying principles governing the assembly and internal structural organization of BMCs is a requisite for synthetic biologists to design custom nanoreactors that use BMC architectures as a template.	DISCUSS
201	204	BMC	complex_assembly	A detailed understanding of the underlying principles governing the assembly and internal structural organization of BMCs is a requisite for synthetic biologists to design custom nanoreactors that use BMC architectures as a template.	DISCUSS
41	54	metabolosomes	complex_assembly	Furthermore, given the growing number of metabolosomes implicated in pathogenesis, the PduL structure will be useful in the development of therapeutics.	DISCUSS
87	91	PduL	protein_type	Furthermore, given the growing number of metabolosomes implicated in pathogenesis, the PduL structure will be useful in the development of therapeutics.	DISCUSS
92	101	structure	evidence	Furthermore, given the growing number of metabolosomes implicated in pathogenesis, the PduL structure will be useful in the development of therapeutics.	DISCUSS
14	18	PduL	protein_type	The fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt BMC-based metabolism, while not affecting most commensal organisms that require PTAC activity.	DISCUSS
53	66	metabolosomes	complex_assembly	The fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt BMC-based metabolism, while not affecting most commensal organisms that require PTAC activity.	DISCUSS
120	124	PduL	protein_type	The fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt BMC-based metabolism, while not affecting most commensal organisms that require PTAC activity.	DISCUSS
133	136	Pta	protein_type	The fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt BMC-based metabolism, while not affecting most commensal organisms that require PTAC activity.	DISCUSS
169	172	BMC	complex_assembly	The fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt BMC-based metabolism, while not affecting most commensal organisms that require PTAC activity.	DISCUSS
249	253	PTAC	protein_type	The fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt BMC-based metabolism, while not affecting most commensal organisms that require PTAC activity.	DISCUSS