(481) Hol, W. G.; Halie, L. M.; Sander, C. Dipoles of the Alpha-Helix and Beta-Sheet: Their Role in Protein Folding. *Nature* **1981**, *294*, 532–536.

(482) Vasanthi, G.; Krishnaswamy, S. Dipole Moment in TIM Alpha/Beta Fold Proteins. *Indian J. Biochem. Biophys.* **2003**, *40*, 194–202.

(483) Tiwari, S. P.; Reuter, N. Similarity in Shape Dictates Signature Intrinsic Dynamics Despite No Functional Conservation in TIM Barrel Enzymes. *PLoS Comput. Biol.* **2016**, *12*, No. e1004834.

(484) Cantarel, B. L.; Coutinho, P. M.; Rancurel, C.; Bernard, T.; Lombard, V.; Henrissat, B. The Carbohydrate-Active EnZymes Database (CAZy): An Expert Resource for Glycogenomics. *Nucleic Acids Res.* **2009**, *37*, D233–238.

(485) MacGregor, E. A.; Janecek, S.; Svensson, B. Relationship of Sequence and Structure to Specificity in the Alpha-Amylase Family of Enzymes. *Biochim. Biophys. Acta* **2001**, *1546*, 1–20.

(486) Janeček, Š.; Mareček, F.; MacGregor, E. A.; Svensson, B. Starch-Binding Domains as CBM Families-History, Occurrence, Structure, Function and Evolution. *Biotechnol. Adv.* **2019**, *37*, No. 107451.

(487) Kari, J.; Olsen, J. P.; Jensen, K.; Badino, S. F.; Krogh, K. B. R. M.; Borch, K.; Westh, P. Sabatier Principle for Interfacial (Heterogeneous) Enzyme Catalysis. *ACS Catal.* **2018**, *8*, 11966–11972.

(488) Kari, J.; Schaller, K.; Molina, G. A.; Borch, K.; Westh, P. The Sabatier Principle as a Tool for Discovery and Engineering of Industrial Enzymes. *Curr. Opin. Biotechnol.* **2022**, *78*, No. 102843.

(489) Møller, M. S.; Henriksen, A.; Svensson, B. Structure and Function of α-Glucan Debranching Enzymes. *Cell. Mol. Life Sci.* **2016**, *73*, 2619–2641.

(490) Abad, M. C.; Binderup, K.; Rios-Steiner, J.; Arni, R. K.; Preiss, J.; Geiger, J. H. The X-Ray Crystallographic Structure of *Escherichia coli* Branching Enzyme. *J. Biol. Chem.* **2002**, *277*, 42164–42170.

(491) Schumacher, M. A.; Wörmann, M. E.; Henderson, M.; Salinas, R.; Latoscha, A.; Al-Bassam, M. M.; Singh, K. S.; Barclay, E.; Gunka, K.; Tschowri, N. Allosteric Regulation of Glycogen Breakdown by the Second Messenger Cyclic Di-GMP. *Nat. Commun.* **2022**, *13*, S834.

(492) Leemhuis, H.; Dijkstra, B. W.; Dijkhuizen, L. Mutations Converting Cyclodextrin Glycosyltransferase from a Transglycosylase into a Starch Hydrolase. *FEBS Lett.* **2002**, *514*, 189–192.

(493) Janecek, S.; Svensson, B.; MacGregor, E. A. Relation between Domain Evolution, Specificity, and Taxonomy of the Alpha-Amylase Family Members Containing a C-Terminal Starch-Binding Domain. *Eur. J. Biochem.* **2003**, *270*, 635–645.

(494) Thanvi, R.; Jayasinghe, T. D.; Kapil, S.; Obadawo, B. S.; Ronning, D. R.; Sucheck, S. L. Synthesis of C7/C8-Cyclitols and C7N-Aminocyclitols from Maltose and X-Ray Crystal Structure of Streptomyces Coelicolor GlgEI V279S in a Complex with an Amylostatin GXG-like Derivative. *Front. Chem.* **2022**, *10*, No. 950433.

(495) Mirza, O.; Skov, L. K.; Remaud-Simeon, M.; Potocki de Montalk, G.; Albenne, C.; Monsan, P.; Gajhede, M. Crystal Structures of Amylosucrase from *Neisseria polysaccharea* in Complex with D-Glucose and the Active Site Mutant Glu328Gln in Complex with the Natural Substrate Sucrose. *Biochemistry* **2001**, *40*, 9032–9039.

(496) Champion, E.; Guérin, F.; Moulis, C.; Barbe, S.; Tran, T. H.; Morel, S.; Descroix, K.; Monsan, P.; Mourey, L.; Mulard, L. A.; et al. Applying Pairwise Combinations of Amino Acid Mutations for Sorting out Highly Efficient Glucosylation Tools for Chemo-Enzymatic Synthesis of Bacterial Oligosaccharides. *J. Am. Chem. Soc.* **2012**, *134*, 18677–18688.

(497) Skov, L. K.; Pizzut-Serin, S.; Remaud-Simeon, M.; Ernst, H. A.; Gajhede, M.; Mirza, O. The Structure of Amylosucrase from *Deinococcus radiodurans* Has an Unusual Open Active-Site Topology. *Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun.* **2013**, *69*, 973–978.

(498) Mirza, O.; Skov, L. K.; Sprogóe, D.; van den Broek, L. A. M.; Beldman, G.; Kastrup, J. S.; Gajhede, M. Structural Rearrangements of Sucrose Phosphorylase from *Bifidobacterium adolescentis* during Sucrose Conversion. *J. Biol. Chem.* **2006**, *281*, 35576–35584.

(499) Kraus, M.; Grimm, C.; Seibel, J. Redesign of the Active Site of Sucrose Phosphorylase through a Clash-Induced Cascade of Loop Shifts. *Chembiochem Eur. J. Chem. Biol.* **2016**, *17*, 33–36.

(500) Kraus, M.; Grimm, C.; Seibel, J. Switching Enzyme Specificity from Phosphate to Resveratrol Glucosylation. *Chem. Commun. Camb. Engl.* **2017**, *53*, 12181–12184.

(501) Franceus, J.; Capra, N.; Desmet, T.; Thunnissen, A.-M. W. H. Structural Comparison of a Promiscuous and a Highly Specific Sucrose 6F-Phosphate Phosphorylase. *Int. J. Mol. Sci.* **2019**, *20*, 3906.

(502) Machius, M.; Declerck, N.; Huber, R.; Wiegand, G. Activation of Bacillus Licheniformis Alpha-Amylase through a Disorder→order Transition of the Substrate-Binding Site Mediated by a Calcium-Sodium-Calcium Metal Triad. *Struct. Lond. Engl. 1993* **1998**, *6*, 281–292.

(503) Machius, M.; Wiegand, G.; Huber, R. Crystal Structure of Calcium-Depleted *Bacillus licheniformis* Alpha-Amylase at 2.2 Å Resolution. *J. Mol. Biol.* **1995**, *246*, 545–559.

(504) Machius, M.; Declerck, N.; Huber, R.; Wiegand, G. Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase through Introduction of Hydrophobic Residues at the Surface. *J. Biol. Chem.* **2003**, *278*, 11546–11553.

(505) Linden, A.; Mayans, O.; Meyer-Klaucke, W.; Antranikian, G.; Wilmanns, M. Differential Regulation of a Hyperthermophilic Alpha-Amylase with a Novel (Ca,Zn) Two-Metal Center by Zinc. *J. Biol. Chem.* **2003**, *278*, 9875–9884.

(506) Kobayashi, M.; Kubota, M.; Matsuura, Y. Refined Structure and Functional Implications of Trehalose Synthase from *Sulfolobus acidocaldarius*. *J. Appl. Glycosci.* **2003**, *50*, 1–8.

(507) Matsuura, Y.; Kusunoki, M.; Harada, W.; Kakudo, M. Structure and Possible Catalytic Residues of Taka-Amylase A. *J. Biochem. (Tokyo)* **1984**, *95*, 697–702.

(508) Janecek, S.; Svensson, B.; Henrissat, B. Domain Evolution in the Alpha-Amylase Family. *J. Mol. Evol.* **1997**, *45*, 322–331.

(509) Vujicic-Zagar, A.; Pijning, T.; Kralj, S.; López, C. A.; Eeuwema, W.; Dijkhuizen, L.; Dijkstra, B. W. Crystal Structure of a 117 kDa Glucansucrase Fragment Provides Insight into Evolution and Product Specificity of GH70 Enzymes. *Proc. Natl. Acad. Sci. U. S. A.* **2010**, *107*, 21406–21411.

(510) Ito, K.; Ito, S.; Shimamura, T.; Weyand, S.; Kawarasaki, Y.; Misaka, T.; Abe, K.; Kobayashi, T.; Cameron, A. D.; Iwata, S. Crystal Structure of Glucansucrase from the Dental Caries Pathogen *Streptococcus mutans*. *J. Mol. Biol.* **2011**, *408*, 177–186.

(511) Claverie, M.; Cioci, G.; Vuillemin, M.; Monties, N.; Roblin, P.; Lippens, G.; Remaud-Simeon, M.; Moulis, C. Investigations on the Determinants Responsible for Low Molar Mass Dextran Formation by DSR-M Dextransucrase. *ACS Catal.* **2017**, *7*, 7106–7119.

(512) Claverie, M.; Cioci, G.; Guionnet, M.; Schörghuber, J.; Michtenecker, R.; Moulis, C.; Remaud-Simeon, M.; Lippens, G. Futile Encounter Engineering of the DSR-M Dextransucrase Modifies the Resulting Polymer Length. *Biochemistry* **2019**, *58*, 2853–2859.

(513) Molina, M.; Moulis, C.; Monties, N.; Guieysse, D.; Morel, S.; Cioci, G.; Remaud-Siméon, M. A Specific Oligosaccharide-Binding Site in the Alternansucrase Catalytic Domain Mediates Alternan Elongation. *J. Biol. Chem.* **2020**, *295*, 9474–9489.

(514) Pijning, T.; Vujčić-Zagar, A.; Kralj, S.; Dijkhuizen, L.; Dijkstra, B. W. Structure of the α-1,6/α-1,4-Specific Glucansucrase GTFA from *Lactobacillus reuteri* 121. *Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun.* **2012**, *68*, 1448–1454.

(515) Przylas, I.; Tomoo, K.; Terada, Y.; Takaha, T.; Fujii, K.; Saenger, W.; Sträter, N. Crystal Structure of Amylomaltase from *Thermus aquaticus*, a Glycosyltransferase Catalysing the Production of Large Cyclic Glucans. *J. Mol. Biol.* **2000**, *296*, 873–886.

(516) Roth, C.; Weizenmann, N.; Bexten, N.; Saenger, W.; Zimmermann, W.; Maier, T.; Sträter, N. Amylose Recognition and Ring-Size Determination of Amylomaltase. *Sci. Adv.* **2017**, *3*, No. e1601386.

(517) Tumhom, S.; Nimpiboon, P.; Wangkanont, K.; Pongsawasdi, P. *Streptococcus Agalactiae* Amylomaltase Offers Insight into the
Transglycosylation Mechanism and the Molecular Basis of Thermo-
stability among Amylomaltases. *Sci. Rep.* **2021**, *11*, 6740.

(518) Janeček, Š.; Gabriško, M. Remarkable Evolutionary Relatedness among the Enzymes and Proteins from the α-Amylase Family. *Cell. Mol. Life Sci.* **2016**, *73*, 2707–2725.

(519) Mareček, F.; Møller, M. S.; Svensson, B.; Janeček, Š. A Putative Novel Starch-Binding Domain Revealed by in Silico Analysis of the N-Terminal Domain in Bacterial Amylomaltases from the Family GH77. *3 Biotech* **2021**, *11*, 229.

(520) Godány, A.; Vidová, B.; Janecek, S. The Unique Glycoside Hydrolase Family 77 Amylomaltase from Borrelia Burgdorferi with Only Catalytic Triad Conserved. *FEMS Microbiol. Lett.* **2008**, *284*, 84–91.

(521) Janeček, Š.; Svensson, B. Amylolytic Glycoside Hydrolases. *Cell. Mol. Life Sci. CMLS* **2016**, *73*, 2601–2602.

(522) Imamura, H.; Fushinobu, S.; Yamamoto, M.; Kumasaka, T.; Jeon, B.-S.; Wakagi, T.; Matsuzawa, H. Crystal Structures of 4-Alpha-Glucanotransferase from *Thermococcus litoralis* and Its Complex with an Inhibitor. *J. Biol. Chem.* **2003**, *278*, 19378–19386.

(523) Miao, M.; Jiang, B.; Jin, Z.; BeMiller, J. N. Microbial Starch-Converting Enzymes: Recent Insights and Perspectives. *Compr. Rev. Food Sci. Food Saf.* **2018**, *17*, 1238–1260.

(524) Miller, S. L.; Urey, H. C. Organic Compound Synthesis on the Primitive Earth. *Science* **1959**, *130*, 245–251.

(525) Ferris, J. P.; Hill, A. R.; Liu, R.; Orgel, L. E. Synthesis of Long Prebiotic Oligomers on Mineral Surfaces. *Nature* **1996**, *381*, 59–61.

(526) Orgel, L. E. Polymerization on the Rocks: Theoretical Introduction. *Orig. Life Evol. Biosphere J. Int. Soc. Study Orig. Life* **1998**, *28*, 227–234.

(527) Stern, R.; Jedrzejas, M. J. Carbohydrate Polymers at the Center of Life's Origins: The Importance of Molecular Processivity. *Chem. Rev.* **2008**, *108*, 5061–5085.

(528) Tolstoguzov, V. Why Were Polysaccharides Necessary? *Orig. Life Evol. Biosphere* **2004** **346 2004**, 34 (6), 571–597.

(529) Brown, M. R. W.; Kornberg, A. Inorganic Polyphosphate in the Origin and Survival of Species. *Proc. Natl. Acad. Sci. U. S. A.* **2004**, *101*, 16085–16087.

(530) Long, M. S.; Jones, C. D.; Helfrich, M. R.; Mangeney-Slavin, L. K.; Keating, C. D. Dynamic Microcompartmentation in Synthetic Cells. *Proc. Natl. Acad. Sci. U. S. A.* **2005**, *102*, 5920–5925.

(531) Damager, I.; Engelsen, S. B.; Blennow, A.; Lindberg Møller, B.; Motawia, M. S. First Principles Insight into the α-Glucan Structures of Starch: Their Synthesis, Conformation, and Hydration. *Chem. Rev.* **2010**, *110*, 2049–2080.

(532) Zhu, Y.; Delbianco, M.; Seeberger, P. H. Automated Assembly of Starch and Glycogen Polysaccharides. *J. Am. Chem. Soc.* **2021**, *143*, 9758–9768.

(533) Degani, C.; Halmann, M. D-Glucose 1-Phosphate Formation by Cyanogen-Induced Phosphorylation of D-Glucose. Synthesis, Mechanism, and Application to Other Reducing Sugars. *J. Chem. Soc. C Org.* **1971**, 1459–1465.

(534) Nam, I.; Lee, J. K.; Nam, H. G.; Zare, R. N. Abiotic Production of Sugar Phosphates and Uridine Ribonucleoside in Aqueous Microdroplets. *Proc. Natl. Acad. Sci. U. S. A.* **2017**, *114*, 12396–12400.

(535) Römling, U. Is Biofilm Formation Intrinsic to the Origin of Life? *Environ. Microbiol.* **2023**, *25*, 26.

(536) Penesyan, A.; Paulsen, I. T.; Kjelleberg, S.; Gillings, M. R. Three Faces of Biofilms: A Microbial Lifestyle, a Nascent Multicellular Organism, and an Incubator for Diversity. *NPJ Biofilms Microbiomes* **2021**, *7*, 80.

(537) Stoodley, P.; Sauer, K.; Davies, D. G.; Costerton, J. W. Biofilms as Complex Differentiated Communities. *Annu. Rev. Microbiol.* **2002**, *56*, 187–209.

(538) Flemming, H.-C.; Wingender, J.; Szewzyk, U.; Steinberg, P.; Rice, S. A.; Kjelleberg, S. Biofilms: An Emergent Form of Bacterial Life. *Nat. Rev. Microbiol.* **2016**, *14*, 563–575.

(539) Hall-Stoodley, L.; Costerton, J. W.; Stoodley, P. Bacterial Biofilms: From the Natural Environment to Infectious Diseases. *Nat. Rev. Microbiol.* **2004**, *2*, 95–108.

(540) Betts, H. C.; Puttick, M. N.; Clark, J. W.; Williams, T. A.; Donoghue, P. C. J.; Pisani, D. Integrated Genomic and Fossil Evidence Illuminates Life's Early Evolution and Eukaryote Origin. *Nat. Ecol. Evol.* **2018**, *2*, 1556–1562.

(541) Brown, R. M.; Willison, J. H.; Richardson, C. L. Cellulose Biosynthesis in Acetobacter Xylinum: Visualization of the Site of Synthesis and Direct Measurement of the in Vivo Process. *Proc. Natl. Acad. Sci. U. S. A.* **1976**, *73*, 4565–4569.

(542) Serra, D. O.; Richter, A. M.; Hengge, R. Cellulose as an Architectural Element in Spatially Structured *Escherichia coli* Biofilms. *J. Bacteriol.* **2013**, *195*, 5540–5554.

(543) McIntosh, M.; Stone, B. A.; Stanisich, V. A. Curdlan and Other Bacterial (1→3)-Beta-D-Glucans. *Appl. Microbiol. Biotechnol.* **2005**, *68*, 163–173.

(544) Bonafonte, M. A.; Solano, C.; Sesma, B.; Alvarez, M.; Montuenga, L.; Garcia-Ros, D.; Gamazo, C. The Relationship between Glycogen Synthesis, Biofilm Formation and Virulence in *Salmonella enteritidis*. *FEMS Microbiol Lett* **2000**, *191*, 31–36.

(545) Jackson, D. W.; Suzuki, K.; Oakford, L.; Simecka, J. W.; Hart, M. E.; Romeo, T. Biofilm Formation and Dispersal under the Influence of the Global Regulator CsrA of *Escherichia coli*. *J. Bacteriol.* **2002**, *184*, 290–301.

(546) Bai, Y.; Gangoiti, J.; Dijkstra, B. W.; Dijkhuizen, L.; Pijning, T. Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria. *Struct. Lond. Engl.* **1993** **2017**, 25, 231–242.

(547) Petruzzi, B.; Briggs, R. E.; Swords, W. E.; de Castro, C.; Molinaro, A.; Inzana, T. J. Capsular Polysaccharide Interferes with Biofilm Formation by *Pasteurella multocida* Serogroup A. *mBio* **2017**, *8*, No. e01843-17.

(548) Champion, A. E.; Catanzaro, K. C. F.; Bandara, A. B.; Inzana, T. J. Formation of the Francisella Tularensis Biofilm Is Affected by Cell Surface Glycosylation, Growth Medium, and a Glucan Exopolysaccharide. *Sci. Rep.* **2019**, *9*, 12252.

(549) Kambourova, M.; Mandeva, R.; Dimova, D.; Poli, A.; Nicolaus, B.; Tommonaro, G. Production and Characterization of a Microbial Glucan, Synthesized by *Geobacillus Tepidamans* V264 Isolated from Bulgarian Hot Spring. *Carbohydr. Polym.* **2009**, *77*, 338–343.

(550) Te Poele, E. M.; Van Der Hoek, S. E.; Chatzioiannou, A. C.; Gerwig, G. J.; Duisterwinkel, W. J.; Oudhuis, L. A. A. C. M.; Gangoiti, J.; Dijkhuizen, L.; Leemhuis, H. GtfC Enzyme of *Geobacillus* Sp. 12AMOR1 Represents a Novel Thermostable Type of GH70 4,6-α-Glucanotransferase That Synthesizes a Linear Alternating (A1 → 6)/(A1 → 4) α-Glucan and Delays Bread Staling. *J. Agric. Food Chem.* **2021**, *69*, 9859–9868.

(551) Probst, A. J.; Weinmaier, T.; Raymann, K.; Perras, A.; Emerson, J. B.; Rattei, T.; Wanner, G.; Klingl, A.; Berg, I. A.; Yoshinaga, M.; et al. Biology of a Widespread Uncultivated Archaeon That Contributes to Carbon Fixation in the Subsurface. *Nat. Commun.* **2014**, *5*, 5497.

(552) Koonin, E. V. Comparative Genomics, Minimal Gene-Sets and the Last Universal Common Ancestor. *Nat. Rev. Microbiol.* **2003**, *1*, 127–136.

(553) McMeechan, A.; Lovell, M. A.; Cogan, T. A.; Marston, K. L.; Humphrey, T. J.; Barrow, P. A. Glycogen Production by Different *Salmonella enterica* Serotypes: Contribution of Functional glgC to Virulence, Intestinal Colonization and Environmental Survival. *Microbiol. Read. Engl.* **2005**, *151*, 3969–3977.

(554) Klotz, A.; Georg, J.; Bučinská, L.; Watanabe, S.; Reimann, V.; Januszewski, W.; Sobotka, R.; Jendrossek, D.; Hess, W. R.; Forchhammer, K. Awakening of a Dormant Cyanobacterium from Nitrogen Chlorosis Reveals a Genetically Determined Program. *Curr. Biol.* **2016**, *26*, 2862–2872.

(555) Mushegian, A. The Minimal Genome Concept. *Curr. Opin. Genet. Dev.* **1999**, *9*, 709–714.
(556) Acevedo-Rocha, C. G.; Fang, G.; Schmidt, M.; Ussery, D. W.; Danchin, A. From Essential to Persistent Genes: A Functional Approach to Constructing Synthetic Life. *Trends Genet.* **2013**, *29*, 273–279.

(557) Henrissat, B.; Deleury, E.; Coutinho, P. M. Glycogen Metabolism Loss: A Common Marker of Parasitic Behaviour in Bacteria? *Trends Genet.* **2002**, *18*, 437–440.

(558) Seibold, G.; Dempf, S.; Schreiner, J.; Eikmanns, B. J. Glycogen Formation in *Corynebacterium glutamicum* and Role of ADP-Glucose Pyrophosphorylase. *Microbiol. Read. Engl.* **2007**, *153*, 1275–1285.

(559) Zmasek, C. M.; Godzik, A. Phylogenomic Analysis of Glycogen Branching and Debranching Enzymatic Duo. *BMC Evol. Biol.* **2014**, *14*, 183–183.

(560) Ouzounis, C. A.; Kunin, V.; Darzentas, N.; Goldovsky, L. A. Minimal Estimate for the Gene Content of the Last Universal Common Ancestor—Exobiology from a Terrestrial Perspective. *Res. Microbiol.* **2006**, *157*, S7–68.

(561) Goldman, A. D.; Baross, J. A.; Samudrala, R. The Enzymatic and Metabolic Capabilities of Early Life. *PloS ONE* **2012**, *7*, No. e39912.

(562) Sousa, F. L.; Thiergart, T.; Landan, G.; Nelson-Sathi, S.; Pereira, I. A. C.; Allen, J. F.; Lane, N.; Martin, W. F. Early Bioenergetic Evolution. *Philos. Trans. R. Soc. Lond. B. Biol. Sci.* **2013**, *368*, 20130088.

(563) Weiss, M. C.; Sousa, F. L.; Mrnjavac, N.; Neukirchen, S.; Roettger, M.; Nelson-Sathi, S.; Martin, W. F. The Physiology and Habitat of the Last Universal Common Ancestor. *Nat. Microbiol.* **2016**, *1*, 1–8.

(564) Weiss, M. C.; Preiner, M.; Xavier, J. C.; Zimorski, V.; Martin, W. F. The Last Universal Common Ancestor between Ancient Earth Chemistry and the Onset of Genetics. *PLoS Genet.* **2018**, *14*, No. e1007518.

(565) Linton, J. D.; Cripps, R. E. The Occurrence and Identification of Intracellular Polyglucose Storage Granules in *Methylococcus* NCIB 11083 Grown in Chemostat Culture on Methane. *Arch. Microbiol.* **1978** *1171* **1978**, *117*, 41–48.

(566) Rozova, O. N.; Ekimova, G. A.; Molochkov, N. V.; Reshetnikov, A. S.; Khmelenina, V. N.; Mustakhimov, I. I. Enzymes of an Alternative Pathway of Glucose Metabolism in Obligate Methanotrophs. *Sci. Rep.* **2021**, *11*, 8795.

(567) Bhuiyan, S. H.; Rus'd, A. A.; Kitaoka, M.; Hayashi, K. Characterization of a Hyperthermostable Glycogen Phosphorylase from Aquifex Aeolicus Expressed in *Escherichia coli*. *J. Mol. Catal. B Enzym.* **2003**, *22*, 173–180.

(568) Zhang, X.; Leemhuis, H.; Janeček, Š.; Martinovičová, M.; Pijning, T.; van der Maarel, M. J. E. C. Identification of *Thermotoga maritima* MSB8 GH57 α-Amylase AmyC as a Glycogen-Branching Enzyme with High Hydrolytic Activity. *Appl. Microbiol. Biotechnol.* **2019**, *103*, 6141–6141.

(569) Ciccarelli, F. D.; Doerks, T.; Von Mering, C.; Creevey, C. J.; Snel, B.; Bork, P. Toward Automatic Reconstruction of a Highly Resolved Tree of Life. *Science* **2006**, *311*, 1283–1287.

(570) Martin, W.; Baross, J.; Kelley, D.; Russell, M. J. Hydrothermal Vents and the Origin of Life. *Nat. Rev. Microbiol.* **2008**, *6*, 805–814.

(571) Bocchetta, M.; Gribaldo, S.; Sanangelantoni, A.; Cammarano, P. Phylogenetic Depth of the Bacterial Genera Aquifex and Thermotoga Inferred from Analysis of Ribosomal Protein, Elongation Factor, and RNA Polymerase Subunit Sequences. *J. Mol. Evol.* **2000**, *50*, 366–380.

(572) Bult, C. J.; White, O.; Olsen, G. J.; Zhou, L.; Fleischmann, R. D.; Sutton, G. G.; Blake, J. A.; FitzGerald, L. M.; Clayton, R. A.; Gocayne, J. D.; et al. Complete Genome Sequence of the Methanogenic Archaeon, *Methanococcus jannaschii*. *Science* **1996**, *273*, 1058–1073.

(573) Sorgo, A.; Gaill, F.; Lechaire, J. P.; Arndt, C.; Bright, M. Glycogen Storage in the Riftia Pachyptila Trophosome: Contribution of Host and Symbionts. *Mar. Ecol. Prog. Ser.* **2002**, *231*, 115–120.

(574) Muchowska, K. B.; Varma, S. J.; Moran, J. Nonenzymatic Metabolic Reactions and Life's Origins. *Chem. Rev.* **2020**, *120*, 7708–7744.

(575) Horowitz, N. H. On the Evolution of Biochemical Syntheses. *Proc. Natl. Acad. Sci. U.S.A.* **1945**, *31*, 153–157.

(576) Peregrin-Alvarez, J. M.; Tsoka, S.; Ouzounis, C. A. The Phylogenetic Extent of Metabolic Enzymes and Pathways. *Genome Res.* **2003**, *13*, 422–427.

(577) Hulsmann, A.; Lurz, R.; Scheffel, F.; Schneider, E. Maltose and Maltodextrin Transport in the Thermoacidophilic Gram-Positive Bacterium Alicyclobacillus Acidocaldarius Is Mediated by a High-Affinity Transport System That Includes a Maltose Binding Protein Tolerant to Low pH. *J. Bacteriol.* **2000**, *182*, 6292–6292.

(578) Nakai, H.; Baumann, M. J.; Petersen, B. O.; Westphal, Y.; Schols, H.; Dilokpimol, A.; Hachem, M. A.; Lahtinen, S. J.; Duus, J. O.; Svensson, B. The Maltodextrin Transport System and Metabolism in *Lactobacillus acidophilus* NCFM and Production of Novel α-Glucosides through Reverse Phosphorolysis by Maltose Phosphorylase. *FEBS J.* **2009**, *276*, 7353–7365.

(579) Joyet, P.; Mokhtari, A.; Riboulet-Bisson, E.; Blancato, V. S.; Espariz, M.; Magni, C.; Hartke, A.; Deutscher, J.; Sauvageot, N. Enzymes Required for Maltodextrin Catabolism in *Enterococcus faecalis* Exhibit Novel Activities. *Appl. Environ. Microbiol.* **2017**, *83*, 38–55.

(580) Cori, G. T.; Cori, C. F. The Kinetics of the Enzymatic Synthesis of Glycogen from Glucose-1-Phosphate. *J. Biol. Chem.* **1940**, *135*, 733–756.

(581) Granick, S. Speculations on the Origins and Evolution of Photosynthesis. *Ann. N. Y. Acad. Sci.* **1957**, *69*, 292–308.

(582) Yčas, M. On Earlier States of the Biochemical System. *J. Theor. Biol.* **1974**, *44*, 145–160.

(583) Jensen, R. A. Enzyme Recruitment in Evolution of New Function. *Annu. Rev. Microbiol.* **1976**, *30*, 409–425.

(584) Rueffler, C.; Hermisson, J.; Wagner, G. P. Evolution of Functional Specialization and Division of Labor. *Proc. Natl. Acad. Sci. U. S. A.* **2012**, *109*, E326–E335.

(585) Khersonsky, O.; Tawfik, D. S. Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective. *Annu. Rev. Biochem.* **2010**, *79*, 471–505.

(586) Cereijo, A. E.; Asencion Diez, M. D.; Dávila Costa, J. S.; Alvarez, H. M.; Iglesias, A. A. On the Kinetic and Allosteric Regulatory Properties of the ADP-Glucose Pyrophosphorylase from *Rhodococcus jostii*: An Approach to Evaluate Glycogen Metabolism in Oleaginous Bacteria. *Front. Microbiol.* **2016**, *7*, 830–830.

(587) Goldman, A. D.; Beatty, J. T.; Landweber, L. F. The TIM Barrel Architecture Facilitated the Early Evolution of Protein-Mediated Metabolism. *J. Mol. Evol.* **2016**, *82* (1), 17–26.

(588) Johnson, J. L.; Bastian, N. R.; Rajagopalan, K. V. Molybdopterin Guanine Dinucleotide: A Modified Form of Molybdopterin Identified in the Molybdenum Cofactor of Dimethyl Sulfoxide Reductase from Rhodobacter Sphaeroides Forma Specialis Denitrificans. *Proc. Natl. Acad. Sci. U. S. A.* **1990**, *87*, 3190–3194.

(589) Stevenson, C. E. M.; Sargent, F.; Buchanan, G.; Palmer, T.; Lawson, D. M. Crystal Structure of the Molybdenum Cofactor Biosynthesis Protein MobA from *Escherichia coli* at Near-Atomic Resolution. *Struct. Lond. Engl.* **1993** **2000**, *8*, 1115–1125.

(590) Gabrielsen, M.; Bond, C. S.; Hallyburton, I.; Hecht, S.; Bacher, A.; Eisenreich, W.; Rohdich, F.; Hunter, W. N. Hexameric Assembly of the Bifunctional Methylerythritol 2,4-Cyclodiphosphate Synthase and Protein-Protein Associations in the Deoxy-Xylulose-Dependent Pathway of Isoprenoid Precursor Biosynthesis. *J. Biol. Chem.* **2004**, *279*, 52753–52761.

(591) Renner-Schneck, M.; Hinderberger, I.; Gisin, J.; Exner, T.; Mayer, C.; Stehle, T. Crystal Structure of the N-Acetylmuramic Acid α-1-Phosphate (MurNAc-A1-P) Uridylyltransferase MurU, a Minimal Sugar Nucleotidyltransferase and Potential Drug Target Enzyme in Gram-Negative Pathogens. *J. Biol. Chem.* **2015**, *290*, 10804–10813.
(592) Jelakovic, S.; Schulz, G. E. The Structure of CMP:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase and of Its Complexes with Substrates and Substrate Analogs. *J. Mol. Biol.* **2001**, *312*, 143–155.

(593) Zyryanova, A. F.; Weis, F.; Faille, A.; Alard, A. A.; Crespillo-Casado, A.; Sekine, Y.; Harding, H. P.; Allen, F.; Parts, L.; Fromont, C.; et al. Binding of ISRIB Reveals a Regulatory Site in the Nucleotide Exchange Factor eIF2B. *Science* **2018**, *359*, 1533–1536.

(594) Shirakihara, Y.; Evans, P. R. Crystal Structure of the Complex of Phosphofructokinase from Escherichia Coli with Its Reaction Products. *J. Mol. Biol.* **1988**, *204*, 973–994.

(595) Jedrzejas, M. J.; Chander, M.; Setlow, P.; Krishnasamy, G. Structure and Mechanism of Action of a Novel Phosphoglycerate Mutase from *Bacillus stearothermophilus*. *EMBO J.* **2000**, *19*, 1419–1431.

(596) Auerbach, G.; Huber, R.; Grättinger, M.; Zaiss, K.; Schurig, H.; Jaenicke, R.; Jacob, U. Closed Structure of Phosphoglycerate Kinase from *Thermotoga maritima* Reveals the Catalytic Mechanism and Determinants of Thermal Stability. *Structure* **1997**, *5*, 1475–1483.

(597) Chen, Y.-Y.; Ko, T.-P.; Lin, C.-H.; Chen, W.-H.; Wang, A. H.-J. Conformational Change upon Product Binding to *Klebsiella pneumoniae* UDP-Glucose Dehydrogenase: A Possible Inhibition Mechanism for the Key Enzyme in Polymyxin Resistance. *J. Struct. Biol.* **2011**, *175*, 300–310.

(598) Schuller, D. J.; Grant, G. A.; Banaszak, L. J. The Allosteric Ligand Site in the Vmax-Type Cooperative Enzyme Phosphoglycerate Dehydrogenase. *Nat. Struct. Biol.* **1995**, *2*, 69–76.

(599) Nagano, N.; Orengo, C. A.; Thornton, J. M. One Fold with Many Functions: The Evolutionary Relationships between TIM Barrel Families Based on Their Sequences, Structures and Functions. *J. Mol. Biol.* **2002**, *321*, 741–765.

(600) Alvarez, M.; Zeelen, J. P.; Mainfroid, V.; Rentier-Delrue, F.; Martial, J. A.; Wyns, L.; Wierenga, R. K.; Maes, D. Triose-Phosphate Isomerase (TIM) of the Psychrophilic Bacterium Vibrio Marinus. Kinetic and Structural Properties. *J. Biol. Chem.* **1998**, *273*, 2199–2206.

(601) Mattevi, A.; Valentini, G.; Rizzi, M.; Speranza, M. L.; Bolognesi, M.; Coda, A. Crystal Structure of Escherichia Coli Pyruvate Kinase Type I: Molecular Basis of the Allosteric Transition. *Structure* **1995**, *3*, 729–741.

(602) Allard, J.; Grochulski, P.; Sygusch, J. Covalent Intermediate Trapped in 2-Keto-3-Deoxy-6-Phosphogluconate (KDPG) Aldolase Structure at 1.95-A Resolution. *Proc. Natl. Acad. Sci. U. S. A.* **2001**, *98*, 3679–3684.

(603) Rhee, S.; Parris, K. D.; Ahmed, S. A.; Miles, E. W.; Davies, D. R. Exchange of K+ or Cs+ for Na+ Induces Local and Long-Range Changes in the Three-Dimensional Structure of the Tryptophan Synthase Alpha2beta2 Complex. *Biochemistry* **1996**, *35*, 4211–4221.

(604) Barber, M. J.; Neame, P. J.; Lim, L. W.; White, S.; Matthews, F. S. Correlation of X-Ray Deduced and Experimental Amino Acid Sequences of Trimethylamine Dehydrogenase. *J. Biol. Chem.* **1992**, *267*, 6611–6619.

(605) Wang, L.; Yang, J.; Huang, Y.; Liu, Q.; Xu, Y.; Piao, X.; Wise, M. J. Systematic Analysis of Metabolic Pathway Distributions of Bacterial Energy Reserves. *G3 Bethesda Md* **2019**, *9*, 2489–2496.

(606) Goldford, J. E.; Hartman, H.; Smith, T. F.; Segrè, D. Remnants of an Ancient Metabolism without Phosphate. *Cell* **2017**, *168*, 1126–1134.

(607) Daffe, M.; Etienne, G. The Capsule of *Mycobacterium tuberculosis* and Its Implications for Pathogenicity. *Tuber. Lung Dis.* **1999**, *79*, 153–169.

(608) Cywes, C.; Hoppe, H. C.; Daffe, M.; Ehlers, M. R. Nonopsonic Binding of *Mycobacterium tuberculosis* to Complement Receptor Type 3 Is Mediated by Capsular Polysaccharides and Is Strain Dependent. *Infect. Immun.* **1997**, *65*, 4258–4266.

(609) Gagliardi, M. C.; Lemassu, A.; Teloni, R.; Mariotti, S.; Sargentini, V.; Pardini, M.; Daffe, M.; Nisini, R. Cell Wall-Associated Alpha-Glucan Is Instrumental for *Mycobacterium tuberculosis* to Block CD1 Molecule Expression and Disable the Function of Dendritic Cell

Derived from Infected Monocyte. *Cell. Microbiol.* **2007**, *9*, 2081–2092.

(610) Geurtsen, J.; Chedammi, S.; Mesters, J.; Cot, M.; Driessen, N. N.; Sambou, T.; Kakutani, R.; Ummels, R.; Maaskant, J.; Takata, H.; et al. Identification of Mycobacterial Alpha-Glucan as a Novel Ligand for DC-SIGN: Involvement of Mycobacterial Capsular Polysaccharides in Host Immune Modulation. *J. Immunol.* **2009**, *183*, 5221–5231.

(611) Kalscheuer, R.; Palacios, A.; Anso, I.; Cifuente, J.; Anguita, J.; Jacobs, W. R., Jr.; Guerin, M. E.; Prados-Rosales, R. The *Mycobacterium tuberculosis* Capsule: A Cell Structure with Key Implications in Pathogenesis. *Biochem. J.* **2019**, *476*, 1995–2016.

(612) Bayramova, F.; Jacquier, N.; Greub, G. Insight in the Biology of Chlamydia-Related Bacteria. *Microbes Infect.* **2018**, *20*, 432–440.

(613) Cosse, M. M.; Hayward, R. D.; Subtil, A. One Face of *Chlamydia trachomatis*: The Infectious Elementary Body. *Curr. Top. Microbiol. Immunol.* **2016**, *412*, 35–58.

(614) Abdelrahman, Y. M.; Belland, R. J. The Chlamydiaal Developmental Cycle. *FEMS Microbiol. Rev.* **2005**, *29*, 949–959.

(615) Everett, K. D.; Bush, R. M.; Andersen, A. A. Emended Description of the Order Chlamydiales, Proposal of Parachlamydiaeae Fam. Nov. and Simkaniaceae Fam. Nov., Each Containing One Monotypic Genus, Revised Taxonomy of the Family Chlamydiaceae, Including a New Genus and Five New Species, and Standards for the Identification of Organisms. *Int. J. Syst. Bacteriol.* **1999**, *49*, 415–440.

(616) Elwell, C.; Mirrashidi, K.; Engel, J. Chlamydia Cell Biology and Pathogenesis. *Nat. Rev. Microbiol.* **2016**, *14*, 385–400.

(617) Chiappino, M. L.; Dawson, C.; Schachter, J.; Nichols, B. A. Cytochemical Localization of Glycogen in *Chlamydia trachomatis* Inclusions. *J. Bacteriol* **1995**, *177*, 5358–5363.

(618) Gordon, F. B.; Quan, A. L. Occurence of Glycogen in Inclusions of the Psittacosis-Lymphogranuloma Venereum-Trachoma Agents. *J. Infect. Dis.* **1965**, *115*, 186–196.

(619) Gehre, L.; Gorgette, O.; Perrinet, S.; Prevost, M.-C.; Ducatez, M.; Giebel, A. M.; Nelson, D. E.; Ball, S. G.; Subtil, A. Sequestration of Host Metabolism by an Intracellular Pathogen. *eLife* **2016**, *5*, No. e12552.

(620) Lu, C.; Lei, L.; Peng, B.; Tang, L.; Ding, H.; Gong, S.; Li, Z.; Wu, Y.; Zhong, G. *Chlamydia trachomatis* GlgA Is Secreted into Host Cell Cytoplasm. *PLoS ONE* **2013**, *8* (7), No. e68764.

(621) Nguyen, B. D.; Valdivia, R. H. Virulence Determinants in the Obligate Intracellular Pathogen Chlamydia Trachomatis Revealed by Forward Genetic Approaches. *Proc Natl Acad Sci U. S. A.* **2012**, *109*, 1263–1268.

(622) Lei, L.; Yang, C.; Patton, M. J.; Smelkinson, M.; Dorward, D.; Ma, L.; Karanovic, U.; Firdous, S.; McClarty, G.; Caldwell, H. D. A Chlamydial Plasmid-Dependent Secretion System for the Delivery of Virulence Factors to the Host Cytosol. *mBio* **2021**, *12*, No. e0117921.

(623) Hu, C.; Wu, H.; Sun, Y.; Kong, J.; Shao, L.; Chen, X.; Liu, Q.; Liu, Y. GlgA Plays an Important Role in the Induction of Hydrosalpinx by *Chlamydia muridarum*. *Pathog. Dis.* **2020**, *78*, No. ftaa027.

(624) Sun, Z.; Li, Y.; Chen, H.; Xie, L.; Xiao, J.; Luan, X.; Peng, B.; Li, Z.; Chen, L.; Wang, C.; Lu, C. *Chlamydia trachomatis* Glycogen Synthase Promotes MAPK-Mediated Proinflammatory Cytokine Production via TLR2/TLR4 in THP-1 Cells. *Life Sci.* **2021**, *271*, No. 119181.

(625) Lamoth, F.; Pillonel, T.; Greub, G. Waddlia: An Emerging Pathogen and a Model Organism to Study the Biology of Chlamydiae. *Microbes Infect.* **2015**, *17*, 732–737.

(626) Baud, D.; Regan, L.; Greub, G. Emerging Role of *Chlamydia* and *Chlamydia*-like Organisms in Adverse Pregnancy Outcomes. *Curr. Opin. Infect. Dis.* **2008**, *21*, 70–76.

(627) Tuon, F. F.; Dantas, L. R.; Suss, P. H.; Ribeiro, V. S. T. Pathogenesis of the *Pseudomonas aeruginosa* Biofilm: A Review. *Pathogens* **2022**, *11*, 300.

(628) Coyne, A. J. K.; Ghali, A. E.; Holger, D.; Rebold, N.; Rybak, M. J. Therapeutic Strategies for Emerging Multidrug-Resistant *Pseudomonas aeruginosa*. *Infect. Ther.* **2022**, *11*, 661–682.
(629) Kim, J. S.; Yoon, S. J.; Park, Y. J.; Kim, S. Y.; Ryu, C. M. Crossing the Kingdom Border: Human Diseases Caused by Plant Pathogens. *Env. Microbiol.* **2020**, *22*, 2485-2495.

(630) Cao, H.; Baldini, R. L.; Rahme, L. G. Common Mechanisms for Pathogens of Plants and Animals. *Annu. Rev. Phytopathol.* **2001**, *39*, 259-284.

(631) Djonovic, S.; Urbach, J. M.; Drenkard, E.; Bush, J.; Feinbaum, R.; Ausubel, J. L.; Traficante, D.; Risech, M.; Kocks, C.; Fischbach, M. A.; et al. Trehalose Biosynthesis Promotes *Pseudomonas aeruginosa* Pathogenicity in Plants. *PLoS Pathog* **2013**, *9*, No. e1003217.

(632) Freeman, B. C.; Chen, C.; Beattie, G. A. Identification of the Trehalose Biosynthetic Loci of Pseudomonas Syringae and Their Contribution to Fitness in the Phyllosphere. *Env. Microbiol.* **2010**, *12*, 1486-1497.

(633) Emilson, C. G.; Nilsson, B.; Bowen, W. H. Carbohydrate Composition of Dental Plaque from Primates with Irradiation Caries. *J. Oral Pathol.* **1984**, *13*, 213-220.

(634) Mayhall, C. W.; Butler, W. T. The Carbohydrate Composition of Experimental Salivary Pellicles. *J. Oral Pathol.* **1976**, *5*, 358-370.

(635) Critchley, P. The Breakdown of the Carbohydrate and Protein Matrix of Dental Plaque. *Caries Res.* **1969**, *3*, 249-265.

(636) Wood, J. M. The State of Hexose Sugar in Human Dental Plaque and Its Metabolism by the Plaque Bacteria. *Arch. Oral Biol.* **1969**, *14*, 161-168.

(637) Gibbons, R. J. Formation and Significance of Bacterial Polysaccharides in Caries Etiology. *Caries Res.* **1968**, *2*, 164-171.

(638) Takahashi, N.; Nyvad, B. The Role of Bacteria in the Caries Process: Ecological Perspectives. *J. Dent. Res.* **2011**, *90*, 294-303.

(639) Valm, A. M.; Welch, J. L. M.; Rieken, C. W.; Hasegawa, Y.; Sogin, M. L.; Oldenbourg, R.; Dewhirst, F. E.; Borisy, G. G. Systems-Level Analysis of Microbial Community Organization through Combinatorial Labeling and Spectral Imaging. *Proc Natl Acad Sci U. S. A.* **2011**, *108*, 4152-4157.

(640) Marsh, P. D.; Moter, A.; Devine, D. A. Dental Plaque Biofilms: Communities, Conflict and Control. *Periodontol 2000* **2000**, *11*, 55-16-35.

(641) Leme, A. F. P.; Koo, H.; Bellato, C. M.; Bedi, G.; Cury, J. A. The Role of Sucrose in Cariogenic Dental Biofilm Formation—New Insight. *J. Dent. Res.* **2006**, *85*, 878-887.

(642) Ribeiro, C. C.; Tabchoury, C. P.; Cury, A. A. D. B.; Tenuta, L. M.; Rosalen, P. L.; Cury, J. A. Effect of Starch on the Cariogenic Potential of Sucrose. *Br. J. Nutr.* **2005**, *94*, 44-50.

(643) Firestone, A. R.; Schmid, R.; Muhlemann, H. R. Cariogenic Effects of Cooked Wheat Starch Alone or with Sucrose and Frequency-Controlled Feedings in Rats. *Arch. Oral Biol.* **1982**, *27*, 759-763.

(644) Ueda, S.; Shiroza, T.; Kuramitsu, H. K. Sequence Analysis of the gtfC Gene from *Streptococcus mutans* GS-5. *Gene* **1988**, *69*, 101-109.

(645) Shiroza, T.; Ueda, S.; Kuramitsu, H. K. Sequence Analysis of the gtfB Gene from *Streptococcus mutans*. *J. Bacteriol* **1987**, *169*, 4263-4270.

(646) Hanada, N.; Kuramitsu, H. K. Isolation and Characterization of the *Streptococcus mutans* gtfD Gene, Coding for Primer-Dependent Soluble Glucan Synthesis. *Infect. Immun.* **1989**, *57* (7), 2079-2085.

(647) Ooshima, T.; Matsumura, M.; Hoshino, T.; Kawabata, S.; Sobue, S.; Fujiwara, T. Contributions of Three Glycosyltransferases to Sucrose-Dependent Adherence of *Streptococcus mutans*. *J. Dent. Res.* **2001**, *80*, 1672-1677.

(648) Klein, M. I.; Hwang, G.; Santos, P. H.; Campanella, O. H.; Koo, H. *Streptococcus mutans*-Derived Extracellular Matrix in Cariogenic Oral Biofilms. *Front. Cell. Infect. Microbiol.* **2015**, *5*, 10.

(649) Yamashita, Y.; Bowen, W. H.; Burne, R. A.; Kuramitsu, H. K. Role of the *Streptococcus mutans* Gtf Genes in Caries Induction in the Specific-Pathogen-Free Rat Model. *Infect. Immun.* **1993**, *61*, 3811-3817.

(650) Johnson, M. C.; Bozzola, J. J.; Shechmeister, I. L.; Shklair, I. L. Biochemical Study of the Relationship of Extracellular Glucan to

Adherence and Cariogenicity in *Streptococcus mutans* and an Extracellular Polysaccharide Mutant. *J. Bacteriol.* **1977**, *129*, 351-357.

(651) Tanzer, J. M.; Freedman, M. L.; Fitzgerald, R. J.; Larson, R. H. Diminished Virulence of Glucan Synthesis-Defective Mutants of *Streptococcus mutans*. *Infect. Immun.* **1974**, *10*, 197-203.

(652) Harris, G. S.; Michalek, S. M.; Curtiss, R. Cloning of a Locus Involved in *Streptococcus mutans* Intracellular Polysaccharide Accumulation and Virulence Testing of an Intracellular Polysaccharide-Deficient Mutant. *Infect. Immun.* **1992**, *60*, 3175-3185.

(653) Spatafora, G.; Rohrer, K.; Barnard, D.; Michalek, S. A. *Streptococcus mutans* Mutant That Synthesizes Elevated Levels of Intracellular Polysaccharide Is Hypercariogenic in Vivo. *Infect. Immun.* **1995**, *63*, 2556-2563.

(654) Janda, J. M.; Abbott, S. L. The Genus Aeromonas: Taxonomy, Pathogenicity, and Infection. *Clin. Microbiol. Rev.* **2010**, *23*, 35-73.

(655) Fabich, A. J.; Jones, S. A.; Chowdhury, F. Z.; Cernosek, A.; Anderson, A.; Smalley, D.; McHargue, J. W.; Hightower, G. A.; Smith, J. T.; Autieri, S. M.; et al. Comparison of Carbon Nutrition for Pathogenic and Commensal *Escherichia coli* Strains in the Mouse Intestine. *Infect. Immun.* **2008**, *76*, 1143-1152.

(656) Chang, D.-E.; Smalley, D. J.; Tucker, D. L.; Leatham, M. P.; Norris, W. E.; Stevenson, S. J.; Anderson, A. B.; Grissom, J. E.; Laux, D. C.; Cohen, P. S.; Conway, T. Carbon Nutrition of *Escherichia coli* in the Mouse Intestine. *Proc. Natl. Acad. Sci. U. S. A.* **2004**, *101*, 7427-7432.

(657) Jones, S. A.; Jorgensen, M.; Chowdhury, F. Z.; Rodgers, R.; Hartline, J.; Leatham, M. P.; Struve, C.; Krogfelt, K. A.; Cohen, P. S.; Conway, T. Glycogen and Maltose Utilization by *Escherichia coli* O157:H7 in the Mouse Intestine. *Infect. Immun.* **2008**, *76*, 2531-2540.

(658) Morán-Zorzano, M. T.; Alonso-Casajús, N.; Muñoz, F. J.; Viale, A. M.; Baroja-Fernández, E.; Eydallin, G.; Pozueta-Romero, J. Occurrence of More than One Important Source of ADPglucose Linked to Glycogen Biosynthesis in *Escherichia coli* and *Salmonella*. *FEBS Lett.* **2007**, *581*, 4423-4429.

(659) Goh, Y. J.; Klaenhammer, T. R. Insights into Glycogen Metabolism in Lactobacillus Acidophilus: Impact on Carbohydrate Metabolism, Stress Tolerance and Gut Retention. *Microb. Cell Factories* **2014**, *13*, 94.

(660) Leviatan, S.; Shoer, S.; Rothschild, D.; Gorodetski, M.; Segal, E. An Expanded Reference Map of the Human Gut Microbiome Reveals Hundreds of Previously Unknown Species. *Nat. Commun.* **2022**, *13*, 1-14.

(661) Warren, F. J.; Fukuma, N. M.; Mikkelsen, D.; Flanagan, B. M.; Williams, B. A.; Lisle, A. T.; Cuív, P. Ó.; Morrison, M.; Gidley, M. J. Food Starch Structure Impacts Gut Microbiome Composition. *mSphere* **2018**, *3*. DOI: 10.1128/mSphere.00086-18

(662) Kaoutari, A. E.; Armougom, F.; Gordon, J. I.; Raoult, D.; Henrissat, B. The Abundance and Variety of Carbohydrate-Active Enzymes in the Human Gut Microbiota. *Nat. Rev. Microbiol.* **2013**, *11*, 497-504.

(663) Hooda, S.; Vester Boler, B. M.; Rossoni Serao, M. C.; Brulc, J. M.; Staeger, M. A.; Boileau, T. W.; Dowd, S. E.; Fahey, G. C.; Swanson, K. S. 454 Pyrosequencing Reveals a Shift in Fecal Microbiota of Healthy Adult Men Consuming Polydextrose or Soluble Corn Fiber. *J. Nutr.* **2012**, *142*, 1259-1265.

(664) Zmora, N.; Zeevi, D.; Korem, T.; Segal, E.; Elinav, E. Taking It Personally: Personalized Utilization of the Human Microbiome in Health and Disease. *Cell Host Microbe* **2016**, *19*, 12-20.

(665) Mora, C.; Tittensor, D. P.; Adl, S.; Simpson, A. G. B.; Worm, B. How Many Species Are There on Earth and in the Ocean? *PLoS Biol.* **2011**, *9*, No. e1001127.

(666) Locey, K. J.; Lennon, J. T. Scaling Laws Predict Global Microbial Diversity. *Proc. Natl. Acad. Sci. U. S. A.* **2016**, *113* (21), 5970-5975.

(667) Lloyd, K. G.; Steen, A. D.; Ladau, J.; Yin, J.; Crosby, L. Phylogenetically Novel Uncultured Microbial Cells Dominate Earth Microbiomes. *mSystems* **2018**, *3*. DOI: 10.1128/mSystems.00055-18
(668) Abendroth, J.; Higgins, T. W.; Dranow, D. M.; Lorimer, D.; Edwards, T. E. Crystal structure of UTP-glucose-1-phosphate uridylyltransferase from *Burkholderia ambifaria* in complex with UTP. https://www.rcsb.org/structure/Sve7.

(669) Kang, L. W. UDP-glucose pyrophosphorylase from *Acinetobacter baumanii*. https://doi.org/10.2210/pdb6IKZ/pdb.

(670) Purvis, A.; Nidetzky, B.; Watson, K. Starch Phosphorylase: Structural Studies Explain Oxyanion-Dependent Kinetic Stability and Regulatory Control. https://doi.org/10.2210/pdb2C4M/pdb.

(671) Mayclin, S.J.; Dranow, D.M.; Lorimer, D.; Edwards, T.E. Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from *Burkholderia xenovorans* in complex with glucose-6-phosphate. https://doi.org/10.2210/pdb5V0T/pdb.

(672) Barford, D.; Johnson, L. N. The Allosteric Transition of Glycogen Phosphorylase. *Nature* **1989**, *340*, 609–616.

(673) Hayashi, M.; Suzuki, R.; Colleoni, C.; Ball, S. G.; Fujita, N.; Suzuki, E. Bound Substrate in the Structure of Cyanobacterial Branching Enzyme Supports a New Mechanistic Model. *J. Biol. Chem.* **2017**, *292*, 5465–5475.

(674) Flint, H. J.; Scott, K. P.; Duncan, S. H.; Louis, P.; Forano, E. Microbial Degradation of Complex Carbohydrates in the Gut. *Gut Microbes.* **2012**, *3*, 289–306.

(675) Jung, D. H.; Park, C. S. Resistant Starch Utilization by *Bifidobacterium*, the Beneficial Human Gut Bacteria. *Food Sci. Biotechnol.* **2023**, *32*, 441–452.

(676) Cerqueira, F. M.; Photenhauer, A. L.; Pollet, R. M.; Brown, H. A.; Koropatkin, N. M. Starch Digestion by Gut Bacteria: Crowdsourcing for Carbs. *Trends Microbiol.* **2020**, *28*, 95–108.