ids
stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A923XN16 | MSFDVVIISNGPGELSTWVKPLAEKINDTLPEARIIICLVPCPYASGAEEEIALSFHGVSVVLSVKETSKFLFSKKLPNNFSFKEKGIIIHLGGDQFFTVMMAWRTKFASVVYTEKLVLWPTIIDKYLLTDQNIYANARLKKVSATKLSVVGNLMADAVSQELNPQEIRAKLGLSTDSSIVSLLPGSKPFKVKYATPFFIKIADYIAKKSPDTQFIISQSPYTPLNQIVGSVIDQKCISALDGVSARYGKTEDNNVLVTEQGTVINIIHPDYQYEAYQVSDLAITLPGTNTAELAILGIPMVVLMPLDRLENIPIEGFIGLISDLPIIGKYIKSFLIKQALKKIKFTALPNQKLGQMVTPEFTGTNILPVEVANTVYNIISQPYKRREISLNLKKAMGSTGAVKNIIVNIIDVLLKKYPDMEILETNNNFSDWTKRESDTES | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Length: 442
Sequence Mass (Da): 48976
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A0A1D8MMI4 | MSTHWLFSTNHKDIGTMYLVFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFFLLLASSTVEAGAGTGWTVYPPLAGNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTILNMKPP | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 173
Sequence Mass (Da): 18570
Location Topology: Multi-pass membrane protein
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A0A942G2B9 | MTFLSLLCVLILEQIRAVPAARLLAAQSAYADYLEGRLNGGEARHGMIAWVVGVAVPALLALLLHFALARVHVLLAFGFNVLMLYFLLGFRQFSHFFTDIQLALRMGELERARQLLAQWRGKSGDRLGSAEVARLAIEQGIVASHRHVFAPLFWFLALGPAGALLYRLALVVAEGWRGAGGPAEANPRFDAFACRAFHW | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 199
Sequence Mass (Da): 21924
Location Topology: Multi-pass membrane protein
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A0A7X9DF92 | MNRLFIALPIDEGIIQNLKPVYATLSQYDDVLKVVEPSLYHLTLKFIGECEGNVARAIESEFASLRFTILPLPYVVKSIGMFPNSKNPSVIWTAIETNQKSINELVTCIQNFTKKYGIKEEDRPFVPHLTLARIRKGRKLTETIHKRLQTFATQEFGSATFPRVILFSSKLTPQGPVYTELQEINFKS | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 188
Sequence Mass (Da): 21436
|
A0A1I3PU99 | MAFCFDDTIAAIASAPGPALRGLIRISGANVREVLERLLGSEFAAASPRKETSELTGACGTDAVQGESNDNSAPHPRPLSPEYRGEGSLKTTSKTARQLSVAIPVADGTLQLPAQLLYWPNRRSFTGEPLAELHLPGSPPLLEEVLARIFLCGARPAERGEFTLRAFLAGRIDLVQAEAVLGVIDAADPKELETALSQLGGGISLKIALAREQLLLHLADLEAGLDFVEEDIEFVSRPALQARLDEALQLVQGLLNQTAARMLSTGRLRVVLAGLPNAGKSTLFNLLLGADAALVSPVAGTTRDYLTGVLNCDGTTCDLVDTAGWETARDGIEEAAALLREDQFDRAQLIVWCTAADLTSEMAALDARLLEQCRAACDNVLQIATKSDLAGESRAQLLSVSAGQGSGIAELRKEIAGRLSTAGSGSEIIGSTAARCEESLRHAWLGIERARGLIDTAAGDELIALELREVLEHLGRIVGQTYTDDILDRIFSRFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 498
Sequence Mass (Da): 52922
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F7XN80 | MRSETIIKVDNIYYSYPDGTPALNGISLDIKRGEFVALVGKNGCGKSTLIKHLNGLLIPDRGAVTVNGMDTSLPSNLWTIRQVVGMVFQNPDTQFVRTTVEEDVAFGPENLALSSENIKKRTDRALSDTSMEEFRDREPKSLSGGQMQRAAIAGVMAMDPECIIFDEVTSMLDQGGRLEILTYLNNIRSSGRTMIYVTHMLEEVLNADRIVLMDNNEIRYTGPPSEFFMQEGLEEMGIDVPDIIQLIRRLQQANIIEPDFHFTDINRLADRICQSLSGI | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Location: Cell membrane
Sequence Length: 279
Sequence Mass (Da): 31224
Location Topology: Peripheral membrane protein
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A0A532V312 | MHPAIGTLRFIDLSAMIISDLHVHPSPWKFGEGTYRQFVKAALDRNVAILGFSEHGPEIGSDQCYRGLKLNEIGDYVESVLKLKEEFSGLIQIFCGLELSYHPDLFDSYMKLQTEFPFDYFLVSLHTIDDWHVDNPDSLSPSIHGKKTEKELYRLYYGKIIDAARCGLFDGFAHIDYLRRSLPHPPGEPPEYALEIYDEVAGEISRSNMTVEVNTRGFSIESMKEMYPTLPFVKKLVHAGVKFTTGSDAHEVGRVGDGLAKVRQLVAVNGIRATHYFKNREVLGLAL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 287
Sequence Mass (Da): 32414
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A0A5C9CX79 | MIARSIPFAKMSGLGNDFILVDDREGVLGGLNKSFLASKLCTPRLSIGADELMIIEQPRSGGHLFMRTFNPDGQEVKMCGNASRCVARYAAKKGIAPPAMVIETLGGPVKASVEGDLIRVELSVTAGPESLELQASGRDFHARWLEITGAPHAVVQFPEVAQTQDSVIQELGAAIRWHPCFPQGTNVNFVEIKDSHTLAQRTFERGVEGETLACGTGAIASVLALADLGLLKSPVSVSTRGGILSVSFEQVDGNFHRIYLGGEARFIAEGTIDPEAWDF | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
EC: 5.1.1.7
Subcellular Location: Cytoplasm
Sequence Length: 279
Sequence Mass (Da): 29878
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A0A7C4J400 | MNSKQLMQLVSRHYYVLTVLFFLVSFLTPLNLHVPLLSAFAWVCLVPLFLYVHNKPLKEVYIVSFITGLFGFGVVYYWMGDFGQALPFGKVVIIALIVPCISVFFATKILVAEYLRRIFPRLTMIVYPSVWIAFDWVQTIGTMAFPWNFLGYTQYPFVNFIQIASITGIFGITFIIIFANISIAELIKARIFVGNYRPALLACIMVCLVVIASTLFGFIRLKQHHEYTNSHLKVAMVQSCFSPWKNWVKNRYMYLDILRTLTNQAMEHEPDIMVWSESATLENISYSYFNGNLNHFEEEVLALAAQNRVPLLTGEIGIIEDVVHRRYYPQNSMVLINSAGQVVDTYAKIHLVPFGEWFPYGELFPFVNDIVDAFGGSNFMPGDSPRIFTIGSFRCAPLICYENIFHRLCRSYAKAGIDFYVNITNLLWTENPIGPMQHFYFSVFRAIENGVWFVSAGNSGFTALIDPYGRVTTSVPLMKKTYCVGNIDLSMNTSTIYRTCGDIILYASFAFLFILCAIVTRNKFIAYTRKR | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 531
Sequence Mass (Da): 60787
Location Topology: Multi-pass membrane protein
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A0A8U8AZF7 | MRDPVDLKRESKAMEDKGFCAVPQVDFSADGKSLGLEGDGALLARDKPFLLPLLRALNTPEFTVDFSSLPEEVKSLARDGCRALQEQQCHGAERAFSQLLSIFYASGFAYVNNVNILNINYVIFLYGHATALLGMGHPEALAKAEVQFKKIIEQYPEESCFCLAHYGIGRVYLRQNRFVHALDQFLRSKLMIDFNIVPGVLTWPGTTQVIEETRIENLQMALRNYIEECKFPPEPDAVCRYQQCHGYSKIQIYFTDPDFKGFIRVICCQQCRVEFHISCWKKLKTTSYSDKNDKDFLKEMCFTPDCKGLISKIVIFSSSRLVKCEFEQKIPKLKEPPRACIKQKCSSLRKIKKKQEKKQRRKRAREEARNSARKKAEEKQEGNEQCQFSQYRDSGQDLYAGDQILQHIRRNSEQIKAAVPDPAQLLKELLAWGVIREEDFGSYCQISTPQEVLEQLLSSLIQEKSRVQSRGFLHVLSQLGEVDPKVHKWLQHLDHLGGF | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length: 499
Sequence Mass (Da): 57322
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F6SUD7 | MPRHLALLPGLALLLAAARPAAASDVLELTDDNFESRVADTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANSNTCNKYGVSGYPTLKIFRNGEESGAYDGPRTADGIVSHLKKQAGPASIPLHSDDEFEKFISDKDASVVGFFKDLFSEAHSEFLKAASNLRDNYRFAHTGQEKLVKKYEPDGEGITLFRPSRLANKFEDNTVRYTEDKITSGKIKKFIQENIFGICPHMTEDNKDLIQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVARKFLDAGQKLNFAVASRKTFGHELSEFGLDSTTGEVPVVAIRTAKGEKFVMQEEFSRDGKALERFLQDYFDGNLKKYLKSEPVPENNDGPVKVVVAENFDEIVNDEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKQSPKKYEGGREVSDFLSYLQREATNPPVIQEEEKPKKKKKAQEDL | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 505
Sequence Mass (Da): 56640
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F6Z764 | MAGGAWALRCVAWALLWGCGAPGPGTGPQRQFVNQWAAEVPGGPGAARAIADELGYDLLGQIGSLENHYLFLHKNHQRRSRRSAVHITKRLSDDDRVSWAEQQYEKQRSKRSVLRDSANNLFNDPMWTQQWYLQDTRMTPTLPKLDLHVLPVWQKGITGKGVVITVLDDGLEWNHTDIYANYDPDASYDFNDNDHDPFPRYDLTNENKHGTRCAGEIAMQANNKKCGVGVAFDSKVGGIRMLDGIVTDAIEASSIGFNPDHVDIYSASWGPNDDGKTVEGPGRLAQKAFEYGIKQGRKGKGSIFVWASGNGGRQGDNCDCDGYTDSIYTISISSASQQGLSPWYAEKCSSTLATAYSSGDYTDQRITSADLHNECTVTHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTSEYDPLALNPGWKKNGAGLMVNSRFGFGLLNAKALVDLADRSTWRAVPEKKVCIVRDKTFEPRALRANGEVTIEIPTTACEGQENVITSLEHVQLEATIEYSRRGDLHVTLTSASGTSTVLLAERERDTSPNGFKNWDFMSVHTWGENPVGTWTLRITDMSGRIQNQGRIVNWRLILHGTSSQPEHMKNPRVYTSYNTVQNDRRGVERMTDLAEDETTPDTLSETPPVSEGPNGYNSSRADKLTEQTPLDVIRRILQNALNKQMVPNRAPKKTSKEELRILHRLFYQALERLNKLSPIRDSEDSLYGDDVDVFYNTKPYKHRDDLLRQALLNILNGRN | Function: Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin, insulin and AGRP.
Catalytic Activity: Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
EC: 3.4.21.93
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 753
Sequence Mass (Da): 83892
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A0A4P5UV26 | MFITFEGIDGSGKSTQIYLLANSLTELNFTVKVLREPGGNIVSENIRNLLLHTDDIVEPRCELLLFTAARAQLVSQVIKPALDNGDIVLCDRYIDSSVAYQGYGRQLPIDDINNINAFATAGLVPDATFILDLAPLEASNRADSRFDLTSTSPDRMEKSGNEFFTRARNGYLHIAHMNPERVHVLNARSSIQDLQESIWKVISGLLQRKKQ | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 211
Sequence Mass (Da): 23521
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W4F115 | MEKIIDIEERIPTLRERRKKRTNQRFTILLAIFGIILLALLYFQSSLSHIGEIKVTGGQLKKAEYYTKHSKIRVGDSLWAFKPKKIEETLQKKDWVESVSVERNWLNTVTIKVKEYDKKAFIKNGGQYNLVLQNGVIYSLDEIPHDLNLPILVGFQEDALLLKMIKQLDKVDQELKTLISQVNAIPTKSNPYAVRLFMNDGFEVRATITTLAEKLRYYPSIISQVKKGEKGVIDLEVGSFYRSYSSEYGKPTSREEIDDQTTGQ | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 30422
Location Topology: Single-pass type II membrane protein
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K2BT52 | MDIEGIKILAAAGAVAIGGIAPAIAQGKMVSQTMESIGRNPSIQDGIFSKMVIAMAITESLAIYALVIALLILFV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 75
Sequence Mass (Da): 7702
Location Topology: Multi-pass membrane protein
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A0A522D9L6 | MKHVVRAVIIIIAILLMFMLLTACAPGKSLTKDSSTAIKKKEAPVNGDEYVYTYPDEPENEMVDPRAKHAGKKTEAKGQTDEIMVSGTADTPRKEQFYQTGMASWYGREFNGKMTASGEKFDMNGLTAAHKTLPFGSLITVKNLDTGKSVQVKVNDRGPYKKDRILDLSFGAAKQLDMVSTGEVMVGINLVKQEGDQKTAVREGDEVEPVSGDLKSDGADKGGRNGTKNDSEGRYSIQAGAFYSQKKAQDLKVKIESMVDRPVILIKEKEYFKVRIEGIHSKSDATAFKKKLSGSDISSYIIENKE | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 306
Sequence Mass (Da): 33647
Location Topology: Lipid-anchor
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K2EWU1 | MFYFIAGVLLIWRSLLFLFSFLGGVLLAFKPTFPYSDIYLISSGLPDWVWSFANFDGVHYLTIAKNGYSAQFTQVFFPLFPIIINILHRIFPIINPIIIGLFISNLFFLFTCLVFYKLLKLDYKNDVVRWGIIFLCFLPTSFFYGSLYTESLFLFLIIAAFYAARKKFWWLAGALGGLASATRFVGIFLLPALLWEWHE | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 199
Sequence Mass (Da): 23105
Location Topology: Multi-pass membrane protein
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E2BWQ8 | MHLRIAEGISWVDEGAIASGWINTMRVASKNEFVRDMSKLKLKLCNDIQELNRNDYVFDPICPKMINLHDKTRENLAVSDLVRDHRFVFLERSLCLGAATLAQAIRVARLCGPVVLTHSIAPRHSGYLAGLLADIEGAGRLLAFDAGDRRCEYENYLSTLGITLQQCRIYSEKYVSPPPSIELERATVVLATPPCSYTGIKDIVDLAVARGGDTGLLESLTSDTAATKQPRALLAEQFSTLKYALTRPNIQFLIYEVHTILPSETTEMIQRVVEYANQIATEKYIREHPVKRKTVSKESAGRVPKLAKAVTSPKPEQSREQLEVQSRQKQEEDEDETSTITDIIIPDSDLFEVGSIDEIYGEDSEHMLDPGCFIAIIKRKEMMQFDSLFMIKVAESKGLFGDSDKERSPKQKVDVSPACEVLRVRARKGSKRAKKFDLYRLDEGPPEKSTLSKEEATYALRTMNYIRRMENRAADLYRLRLINGFLHLYTGQEAVAVGLKMAIHKEDTVITAYRCHSFAVVFDISVRAVLAELMGRKTGASQGKGGSMHMYAPRFYGGDGIVGGQVPIGTGIALAHKYNSTGAVSITLYGDGAASQGQIYEAWNMAKLWNLPVVYICENNKYGMGTAVHRHSANTRLYTRGDLIPGIKADGMKIVDVREAIRFARDYALRNGPIIIEVVTYRYFGHSMSDPGVGYRTREEIKSVQSEQDPIMLFNQLVVQKELMTEEEIEDIRKSTYKEVDQAVEQAQADAWPEMTELATNVYVKPMEKVRGKVPWESF | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Length: 779
Sequence Mass (Da): 87388
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A0A6S4QEQ6 | MQLKQVNNDRRKNSSDSNIPADKTEDKKWAAADTINESSPVKADFSLKIALRDGKSIMLSRPYIMGILNVTPDSFFDGGLFSSDKAFFKKVNEMLLFGVDFIDLGGESSRPGAKPVSIAEERRRVIPKLKRLKKKYPHIIVSVDTRNEPIASEAIDCGADIINDISAGDDSNGAMLKLVAKTQTPIILMHKKGQPQTMQQNVAYDNVESEVFSYLEHKIALLKELALSEDKIIIDVGIGFGKEHHHNITLIKNLDKFKALGHPILIGASMKSLITHLTGCDPSERLAGTLGVHLAAIVHGANIIRVHDVKSARYSLAGFLPMLGDYG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
EC: 2.5.1.15
Sequence Length: 327
Sequence Mass (Da): 35896
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A0A7V3RJI6 | MNLGCIYKRSLEYLKDKKIPTPDKDAQYIIAHFLKISPHEIFINRDREVSPFKSFLIKRAIVSRGKFKPIAYILKRKYFYRDVFFVNNKVLIPRSDTEHLIYAVEEINTPFKNILEIGTGSGAIAVSLSRLYPVANIIALDIYTAIARKNIKRLGIKNIFLEKKNFFKWMPNNKNGLFDLIISNPPYLSEKDLKNLGKDAALYEPKKAFYGGKDGLDFYRAIAEFAKAGLLKLGYVILEVDYKWKKVMHIFEKEGFGKIVVKKDYNDLERVLVVQKDF | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Length: 278
Sequence Mass (Da): 32276
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A0A7C2KGD0 | MKRAVFPGSFDPLTHGHLDILLRSHTLFDQLVIAVVSNPNKQCTFTLQERKIMIEEVLKEEGLSDFATVKEFKGLLVHFLKDINAKIIIRGIRALSDFEFEFRAARMNNHLDSNIETLFLLSSADYEHISSSLIKEVFHLGGNVSHYVPKSILDRLIQKKELK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
EC: 2.7.7.3
Subcellular Location: Cytoplasm
Sequence Length: 163
Sequence Mass (Da): 18677
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A0A2N2F6C9 | MNLNLARKWRSKNFDTIVGQELTIKMLKNSLYLGHFFPVYLFSGQRGCGKTTTARVFAAAVNCALLPEFQKNPKQHAVPCLQCASCVAMAQGQHPDFIEMDAASHTGVDDVRAIVEAAALLPVMGRKKVYLIDEAHMLSKAAFNAFLKILEEPPRSVLFILATTDPHKIIDTVMSRCFQLSFKAVSEQPLLAHLQEICASEQIRYAPGGLEHIIQATEGSVRDALNMVEQARFSGGIITAEAVHSLLGQLTDEQALRLFELVLHKGPREVLSFLQAHRVSSFSASAVWRTLTELVRAALWVRHGVAPQAYKDFQAQLQQLVMSVSVERLRALAEILYEHEQLFLRTTAQHELIELLLLRMCKQINPDDTSGAAGVPSSPSAAASVSSASVVGSQEEETGEQEEDDEDSDEIIDDSQSRAPWDIFLADLEQLKDPLLSSIFTQGTFVAYHADAGTLEVQFSKELIFFKDWLEDTKKSWRPLLLKQFGPSVSFAPLFTGVSRAAEKKTHTGASNASQEPSLALAFSKTDQEKLVVHDSGVAQQSVKNSSMGFPGAPKNVPVKVGWAGQKSGSSWANNTGQRGQPYYAHSRNAGPRQKPERPLDVADASSWRKATMLVQYFPGTLSEIEEKMESLS | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 633
Sequence Mass (Da): 69724
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A0A6I8NQC8 | MKECEYQQITPGAAPAPAPAPSGGSGLGPAGRPPSGPCGVGPGVGPPGPPGSPGSPGSPAARPRRKWEVFPGRNRFYCGGRLMLSGHGGVCALTFGLILATTGLFFVFDCPFLARHLTLAIPAIAGLLFFFVVSCLLQTSFTDPGILPRATPSEAADLEKQIDSTGSTTYRPPPRTREVLINGQVVKLKYCFTCKMFRPPRTSHCSVCDNCVERFDHHCPWVGNCVGKRNYRFFYAFILSLSFLTAFIFACVITHLTLRSQNDSFLNTLKETPASVLELVVCFFSVWSILGLSGFHTYLVASNLTTNEDIKGSWSNKRGTESAANPYSHDSILTNCCSVLCGPFPPSLIDRRGFVPPDAGIPSPAKSDAKPAPGMDEACQDFAISCTA | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 388
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 41508
Location Topology: Multi-pass membrane protein
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A0A2N2F4K2 | MDHKTTPQNIFTVHVLILSACIVLLLQNSTRTTATCTSSAVTFFNARPVFACPGLPTSPRLLRTGPARQASSGKPASAPRTSGQLWHKKKHTRFAHADLVDIRTINPHIMVELRYASNNNFTGKKIYKTNTCYLKKATALKLNSVQKELELQGLGLKIWDGYRPPAAQKKLWKLVPDPRYVAPPEKGSRHTRGCSVDVTLVTSSGKELAMPTAFDDFSEKAQSNYQALPADVIKNRELLKKLMIKYGFMPVASEWWHFDDADWKTCPLLNISI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 273
Sequence Mass (Da): 30549
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A0A6I8P2G9 | MPRDWDKDVYPEPPRRTPVVESQTAVPNPLHFIVGVFDLLVDRPVTLLREFIERQHAKNKIYYYHRQFRRVPDITECTQGDVLCIYEAEMQWKRDFKVDQEIVNIVQERMKACQQREGDSYIQNCARELQQFEEVAKAYQDRCELAGGGGESRGWVALVGLFPARWDGMGRGFSSHPPHLDSDPVPKVIRAGGGVGGEWSYSRPPHSGHPPPGRSGAPHPGARGDPERPGQRSDHPVVGGSGERPLSAPPGLGLTGRSGPPIPPDQDLGGYSSARKCLAKQKERMIAERKAAKEAAA | Function: Accessory subunit that is involved in the functional assembly of the mitochondrial respiratory chain complex I. Complex I has an NADH dehydrogenase activity with ubiquinone as an immediate electron acceptor and mediates the transfer of electrons from NADH to the respiratory chain.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 297
Sequence Mass (Da): 32970
Location Topology: Peripheral membrane protein
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A0A496RA53 | MSYFLSPAKILYYAYLLVVLTITVRILLDNKSPESSTGWLLAVIFLPYVGAVLYLLGGENWKKRKILKHLPERRFKRELGTILEHQKDFMQHLASEVDSDILKTATLSLQCGNAVLSINNSSEFFFSGYEKFTSLLKDLEGAEESIHMEYFVYKEDETGAKIGEILKRKASEGVEVRLIFDGVGCFNRMSWKFKRDLRRAGVQIKYFLDPMNVLSGRLLNYCNHRKIVVIDGRTGYTGGMNIGDEYITGGKRFASWRDSHVRVEGEIVHLLQTVFLSDWENSGGKKLANARYFPEVKANFGETLPMQVLVSGPDSDWYSLEKLYLNLISNADKEVFIQSPYFIPSSSIQNALETASLSGVSVHLMLTGVPDKLIPFWVAHTYWEPLISAGVNIYLYESGFLHAKMVIADEKIATIGTCNMDIRSFHLDYELNLIYYDSQVARQLKSRFYEDLEHCRKIEKNDLQENGFFTRLRNSVFRIIAPIL | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membrane
Sequence Length: 484
Sequence Mass (Da): 55391
Location Topology: Multi-pass membrane protein
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K2BW41 | MKNNIQLLIELRARILRVLIMWGSIAALFSYFSNAIYEGFALPVLHQLTPHEHLIATEITSPFFVPLQSAIVLSVYVCIPVLLYQLWQFVLPALYQKEKKLVFGLMLSGAILFYVGTAFAYFIVLPMMFRFLAHFSPAQVVLMPDISAYFNFVSRMLLAFGFAFEVPIVIILLLWLHILSQEQCKKMRPYVIVGCFIVGMLLTPPDVLSQTLLAVPLWGLFELGVWVGKFLE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 232
Sequence Mass (Da): 26452
Location Topology: Multi-pass membrane protein
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A0A936HRI3 | MSLSQQLGDGLAAMGLALPAASQATLLAYVALLKKWNRTYNLTAIRDEAEMVVQHLLDSLSVLPAVQESALAGRRWADIGSGAGLPGIPLAIARPDLDMTLIEAVDKKSAFQRQAKIELGLSNISVLNRRVEDVEAGGFDAVVSRAFAEIADFIRQAGHLLAPCGRLYAMKGRLPDDELGKLPPGWTTVACMPLKVPGLHAQRHLIVIEKV | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 211
Sequence Mass (Da): 22637
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A0A4P5UT50 | MKYSSRFFTLSNIISLLRLLLAIPVCIGILYDWSDSLLLILALLAYISDILDGFLARKYNDISEWGKILDPLADKILVGSAAISLMLVGKLSIWYIALVLGRDIAILIAGLLSSRKLGYVLPSTYMGKVAVISVAITLICSFVDSLYIYIQASYILSSIMLIISFIHYGIRMKSFLSPIKNA | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 182
Sequence Mass (Da): 20148
Location Topology: Multi-pass membrane protein
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A0A3A1UVE5 | MDRLLHLSNNWDQTAFVAQYGSLFECSPWVAEKAWHSRPFRTREAMLKRMCEIVKDADEALQLKLLRAHPELGANIRMTKESVAEQRGAGLDRLERDEAYIFHQLNAKYRERFGFPFIIAVKGLTPDMIADSMQKRMMNTAEQEKERALGEVCKIASFRLEHMDINTEAS | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.
EC: 4.1.1.97
Catalytic Activity: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2
Sequence Length: 170
Sequence Mass (Da): 19706
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K2B4Q3 | MLFEPIHKAIQAAKSSHNNIKEKILTIYLSPQGKLLDHELVMSLSQYQQIILLNGRYEGIDERIIENKVDMEISIGDYVLSGGELASMVLIDAITRQIPGALGHEDSAKQDSFANGLLDYPQYTRPDNINGYNVPKVLLSGDHLAIARFRRKQSLGRTWLRRKDLLAKIKLTESDSVLLNEFIKEEAIYA | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 190
Sequence Mass (Da): 21479
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A0A7X9GG50 | QMGVDPDVVSALAREIAEAAKTVEVAIVVGGGNFFRGAELQQAGIDRSRGDYMGMLGTVMNCLALQDFLEQEGQATRVQTAITMGQVAEPYIPLKAIRHLEKGRVVIFGAGAGMPYFSTDTVSIQRSLEIHCDEVVMGKNGVDGVYTADPRKDPNAKRFATLSYNRALVDNLAVMDASALSMARDNKKRIRVFGLEGAGNVTRALLGEEIGTLVSTAESTVVE | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
EC: 2.7.4.22
Subcellular Location: Cytoplasm
Sequence Length: 223
Sequence Mass (Da): 23868
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K2C2D1 | MTQPPLLILIDGSSYLYRAFHALPPLVNSKGEPSGAIYGVMNMIKKLLNDYSPQYVAVIFDAKGKTFRDDLYEDYKAHRDAMPDDLVTQVEPLKEIIQAWGLPLLTIENVEADDVIGTLTASALKKKWQVLISTGDKDMTQLVNPRVSLINTMTNTLLDSKGVQEKFGLPPECMIDYLSLVGDSSDNIPGIPGVGPKTAIKWLLEYDSVKNLLKHADKIPGKVGERLRENKDKIDLWKTLVTIKQDVPLKIKIDDLTQKDQDIPKLIKLFKHYDFKNWVSTLEKNEKFKENSSTSFDFKIINSEKDFEILLKKLNSTKSMGIQVHTSLPDDPFSKLISVSLFLAHDTLFYLPCQDKDDFRKLKNILENTEIKKWGHNLKFCKTALENNELSLEGIAQDIMVEDYLLHPAQNRHDLDFLVSHYLKNNKISYESIAGKGQKKLPFEKIPIEKAAEYTTQALSFIADLQKQFESELQAIPELKKVYTHIELPLIATLSRMEFHGVLIDEDLLKEQSKELEKRLRDIEHHTYKLAGRMFNIASPKQLQEVLYDHLKLPILQRTATGQASTAEEVLQILEKDYPLPKFILEHRTLSKLKSTYTDALPLQINPKTQRIHTSYNQTGTSTGRLSSSHPNLQNIPIRNEEGRRIRKAFIAPPGYFIVSADYSQIELRIMA | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 672
Sequence Mass (Da): 76727
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A0A1I7YKT0 | MVKRQITIRRECPRKLFYEKLLHDWKESTEDRNQRTTIYKAQQSIRCYPIEINGFSELKNIKGIGNNIATKLDDAWQVMCSQFQAIPSVGQIKELKKGEFVQFMNSAAGKKRGPVPVTVAPSAKTGIPRMRSVNLDLPSTSSSGPMNVVPASPGRAFQRWNSLPSTSGKPSGAGGPARPSPPSDMCEDLLRYSPSERDQVEVCLIVDNREKSGLLKKRDVSTFLDKLGTRYELRSLSIGDYLWVLRWKTSGLELVLDYICERKTWQDLWSSIKKGRFDDQKQRLMNCEVENIVLIVEGATPPERAMEQALASSSIRNSFMVQRTASIQDTAKFLHAVSNRLMDRIRTEHVSPVGICPNQVYCTDERHSLRETPERRQEDEVHDGLGRVGAAAYRMPANGR | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
EC: 3.1.22.-
Subcellular Location: Nucleus
Sequence Length: 400
Sequence Mass (Da): 45203
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A0A9E7H956 | MAGGGGDGSSSRSLVETPTWAVAAVCLVLVILSIIMEQVIHRIGKASLFHVPTICACWLDASSAIEMMLLGFISLLLTGKVPFVSSEGINQLHIFIFALAVSQILYCVVTMSLGRLKVCFIRQFVSSVPKVDYLTLRHGFIIAHLAPQSSSKFNFQNYIKRSLEEDFKVVVEISPTIWFIAVCFLLFNTHGWRSSLWLPLIPLIIVLMVGTKLQVIITKMAIQIMERGDVVKGVPVVRPGDKLFWFNRPGLLLFLIHFVLFQNAFQLAFFAWSWVLCSYVTLPLYALVTQMGSNLKPTIFDERVATALRKWHHTARKRLKENRRSGSVTPSLSTSRPATPTHGLSPVHLLQYHHNKAESLQTSPKKFTFDDDQYDPEKLTPPPHHSFDQSFSHYRKLETLEGLMKEEQEMKEYGGSLELQMAHETDGISVDFSFDKRQR | Function: May be involved in modulation of pathogen defense and leaf cell death.
Subcellular Location: Membrane
Sequence Length: 439
Domain: The C-terminus contains a calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion.
Sequence Mass (Da): 49654
Location Topology: Multi-pass membrane protein
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F7XKT9 | MIRITSPSRLHLGLIDLNAEFGRVDGGAGITLDYPCIRIVAEKSDTLEVHDGSHLKNKMKQAADSVLKGRGGICIHVEEDVLSHVGLGSGTQAALCAAMAACRLYGLEYTVRELAEMAGRGGTSGIGVAGFEHGGFIVDAGHRFSRKKSFSPSAASREPPAPVIFRHDFPDWDIILAIPRIKGAHDKEEMNIFSRECPIPLAEVQAVSHTILMQMIPAIMEKDIEAFGRAVNHLQTTGFKKREIAIQSPVVSELMETMIEHGAEGAGMSSFGPAVYAISDRRTNSERIAKKAGQVLNEGIGGDVMITRGNNSGAVIEEI | Pathway: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.
Function: Catalyzes the condensation of 4-aminobenzoate (pABA) with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P).
EC: 2.4.2.54
Catalytic Activity: 4-hydroxybenzoate + 5-phospho-alpha-D-ribose 1-diphosphate + H(+) = 4-(beta-D-ribofuranosyl)phenol 5'-phosphate + CO2 + diphosphate
Sequence Length: 319
Sequence Mass (Da): 34268
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F7BZ44 | MSGVSEPLSRARAGSLRPPEAPPEPMVPVPADVEQKEVRILKICFYSNSFNPGKNFKLVKCTVHTLVQEIIASILLSGRIGPDVQLLQCYGLRLKHVKSDEIHWLHPLMTVGEVQEQYQCLHLEAEWRYDLQIRYLPEGFLEQLKEDRTTLLYFYQQLRHDYMQRYASKVSEGMALQLGCLELRRFYKDMPHNALDKKSNFELLEKEVGLELFFPKQMQDTLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFASIDQETYRCDLIQGWNITVDLVIGPKGIRQMTSQDNKSTCLAEFHQIKSIRCTPKAEGTALLQLSIVGTPQSLSIKTSSLAEAENMADLIDGYCRLQCQTEGTLIVHPQKNGEKRSSLPQIPTPDRRSQLSESCSIESDIYAEIPDEALKRSSGVHYNVGREDVVLGRILGEGFFGEVYEGVYRNSKGEHIRVAVKTCKEDCAPDNKEKFIKEAVLMKNLDHPHIVKLIGLIEEEPTWIIMELYPFGELGHYLEQNKTSLKVPTLILYSLQICKAMAYLEGLNCVHRDIAVRNVLVAATDCVKLGDFGLSRYIEEEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDGCPPVLYTLMTRCWDYGPKDRPRFTELVCSLSDIYKIEKDIAKEQERNRYRPPKIMEPSPYQEPPPKPSRPKCKPPLPQANLLTPKLQFQVPEGLCASSPTLTSPMEYPLPADSLHTPPLQRHAVFKRHSMREEDFIQPGSREEAQQLWEAERTKMRQLLECQQKQMVEDNRWLRQEEKSLDPTVYVNDQSPVTPEKESGYMEFTGPPQKPPRMGAQSIHPTANLDRTDDMVYVNVMELVKAVLQLKNQLGQLPPENYVVVVKNVGLTLRKLIGSVDAILPTLPLSARPEIEGTQKLLNKDLAELISKMRLAQQNAVTSLSEQCKRQMLAASHTLAVDAKNLLDAVDQAKVHGQTQQPSAH | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.2
Subcellular Location: Cell junction
Sequence Length: 1006
Sequence Mass (Da): 114856
Location Topology: Peripheral membrane protein
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A0A7Y3NMN1 | MLGRRRGRGRGRRGGTASWLGELQAIVRLRSRLRCRGDRFAGERQLTVAFGAAFARAAEFGAGAVFEHGGKSDQVHRRLAHALAAARLVGDELHQPGALYRARRRWRRCDLVHDRDALARFVDRQFRLCAGSLLNRGDLLKDQLAHLFLRTAGLLDQRVACHLREACTLAPERRKRERRRGAAFLLACHDGKQRHAAELLLLRRGQGGGRDGERERSEEEHGLSCTPAQAGVQPRADLGPGLRRGTLSFPSHHAIAPRVFRYSKLLALAAGALSATGFAPLELWPVTLACFAVLIRLLFDAPGWRSSFARAWLFGLGHFTVGLNWIAHAFTYQDTMPHWFGYGAVVALSLYLAVFPAVGATGAYALSRSSRAKSRGADEESEKRPSTTLGTSELGSVLLFAATWILTEWLRATVFTGFAWNPLAAIWVPALPVAQLSKWIGTYGLSGLTVLGAGGLALLVRKAMWGVALVAPLLIGLLLPSGSVKLTSTNIRIVQPNVSQDEKHDPGAQVANLKRLVKMSGAPDDRRPRILMWPEAAIDNGFLLEEEPGLRRYLVKALGRGDMLLTGGVALEYDRAGRAVGGRNSVFAMGPDARIHARYDKAHLVPYGEYLPMRSVLTPLGLSRLVPGDLDFWPGPGPKTFDIPGIGPVGFQICYEIIFSGRVVDPARRPRFLFNPSNDAWFGSWGPPQHLAQARLRATEEGMTIVRATPTGVSAVIAPDGSVVGKIGMGKAAVLDARLPQAGRPTLFARFGNLLSGLVALFLAALAVVIARRAR | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 775
Sequence Mass (Da): 84291
Location Topology: Multi-pass membrane protein
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A0A059X1N6 | DPETTPEGFLTLLHPEDRGPVGQAINRAIIDGVPYESEFRVPHRDGSIRWIRGIGKVVFDEQGKPLRMIGINQDITGQKNSDVQLRQSHRQIRALAGRLINAQETERRRISRELHDDLNQRVATLALAISRLKRKLTAQPEIMADLNALYDQTNDLSDDIRQLSHQLHPVALEHLGLAGALQGYISEFEKETGIPTSFSARIRRDKIPFEISVCLYRIALEALRNIARHSQAKSAAVVLEEDDQVLQMSVVDSGIGFEVETGRRGSGLGLLSAQERVNLLQGTFDVVSTPTKGTKLTATIPLR | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 303
Sequence Mass (Da): 33729
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A0A935RBG6 | MENLLRRIAPAGWDLAVLDAVPYQIALLDAQGVIVAVNAAWRRFALENGVGGANAPACTDVGVDYPALCDAVQGASAEGAAEAAAGIRAVLGRQQTEFTREYSCHSPDRQRWFLMTVVALDQADVAGMVIHTDVTARVLERLRRRESEIRLQLALDTTLDGIWDWDPSTGQGYLSPSYYAMTGYRPEDEPGSLDFFRRLVHPDDWPHVMATIEAHLRGDTPVSDIEYRMTTASGEIRWIRGRGRVVERDAAGAPVRMLGLVTDITARKRVERALHESEVRYRTVVEDQTEIICRMGVDGTILFVNEVYLRFFGKTVEEVVGSTWHPVAHPDDLPMIEARLAELAVNRPVVVIENRVCAGDGSWRWMQFVNRGRFDGSGRLKEIQVVGRDVTERHELEAGLRRLLDENKRLASALIRQQEKERAGLAKELHDELSQQLVAIRAHAGAIAHRTTDPLDRTHLDAQAIGNAARDIYAISHRLMEGLRPQALDNAGLIGAIASLANQRLQSHPDVRVRLRAATVGPYGDELRSNLFRIVQECLANAFQHGRIRRIRIFVGERRSGTRRWLSIVVRDDGIGMALDAPRTGYGLIIMRERARNLGGSLDLRSRPGRGTRVAVEIPLPA | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 622
Sequence Mass (Da): 69271
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E0QPE9 | MSLKVAVVDRAHTLFQGEAHQVVVPSVNGDLGILPGHQPLLVVLRPGKVRVTSNGKTQELAVTSGFASVDNNTVTVVLGSDLSESDNGSGTPCDTLSAPPNASGE | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 105
Sequence Mass (Da): 10731
Location Topology: Peripheral membrane protein
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A0A1B1YVS1 | MRRGALQARLWAAGLWTLALTPALVLLARALGNRLGANPIEELTLELGQWALRFLLLTLAATPLRRLTGWTVLLRHRRLLGLTAASYALLHLLVYAVLDQGLLWSQIVGDILKRPFITVGMAAFVLLLPLAATSFDAAIRRLGARRWQALHRLVYVATGLALLHFWWKVKADTAEPTIYLTVFALLLVARFVAPGHRFRRRPPAGRQPA | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Subcellular Location: Cell membrane
Sequence Length: 209
Sequence Mass (Da): 23315
Location Topology: Multi-pass membrane protein
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A0A9E7GUC2 | MKETLHRIVDELVGSTNHQFQIAGFVVRAIPWLKSLFVGVSAPFRVFQDSIKLLGEGTVPCITLILGGNLTQGLRKSQIKPVVVFAILCVRFAILPDCCGKSSLRIRIRAIRSIVPIRADDTVYCPTCHEYR | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 132
Sequence Mass (Da): 14708
Location Topology: Multi-pass membrane protein
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A0A9E7L7J9 | MDEPRPLRRALIDSLSGAISGGISRTVTSPLDVIKIRFQVLNVKEEGKWSLGEYEGFWRGNVPALLLYMPYTAIQFTVLHKLKTIAAGSSKAEDHLQLRPYLPYLSGALAGCAATIGSYPFDLLRTILASQGEPKVYSTMRSAFVDIIRTRGIRGLYAGLSPTLVEIIPYAGLQIGSFDTFKRWMMAWNRYRFSNISPVRLDDSLSSFQLFLCGLAAGACAKAICHPLDVVKKRFQVENNNKLALALQIEGLQRHPKYGARVESRTYKNIYHALQQILRSEGRHGLYKGIFPSLIKSAPAGAVTFVSYEYTSRWRTLFRCYVLVASYKSPPLTRPNQQLKEEEKRRQISSCKMAEKPTTMESMRKWVVEHKLRAVGCLWLTGIGSSIAYNWSRPNMKPSVKIIHARLHAQALTLAALAGAALVEYYDHSTGSGSKSYSKHRSQKAPTLHNPVMGSELIYRGHDSLPLAESEGYTSKPEKRLLWLLRPLRYLLCEQRLLFMLVGVALATIVFAFSFSPASPSAAGAFHAKLADQAAWRSSGAHHRAAFELAAVGSVGGKLPLGLKRKRLRVVVTGGAGFVGSHLVDRLMARGDSVIVVDNFFTGRKENVMHHFGNPNFELIRHDVVEPLLLEVDQIYHLACPASPVHYKYNPVKTIISFLRLRSSGSLNQLRFSNLASYTIIMFLNPLPLICFQLIVSEGKVPSMWLFKCLNSFVHKTNVVGTLNMLGLAKRVGARFLLTSTSEVYGDPLQHPQAETYWGNVNPIGVRSCYDEGKRTAETLTMDYHRGAQVEVRIARIFNTYGPRMCIDDGRVVSNFVAQALRKEPLTVYGDGKQTRSFQYVSDLVEGLIRLMEGEHVGPFNLGNPGEFTMLELANVVQETIDPSAKIKFRPNTEDDPHKRKPDITRAKELLGWEPKISLRQGLPLMVSDFRKRIFGDHSDSNPTTTGIIIEST | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step 1/1.
Function: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.
EC: 4.1.1.35
Subcellular Location: Membrane
Sequence Length: 953
Sequence Mass (Da): 106479
Location Topology: Multi-pass membrane protein
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A0A9E7GVB1 | MEFPTRSRNVVFAVAGAQKESMGRSEAENINPAEEESREGMDLLSHARPRNLQSREEEVEAESRRVQDGFFFPFSCVLLTSMAVAASSSSSSSSLIILFLDLPRLLRQNHRSASQSPLLCPPAKNPSRSARRTKLLVPAAAFSPLLPSLRRKLTPPPSRSLADDRSGDDGAAVVEYVADVVDNGSIRAVGIGARPGSPRPQRNAGSADSISLGIKEPVYEVIEVKSDGTMYMKKINRRQLLKSSGLRPRDIRSVDPSLWLMNSMPSLLVREQAILLNLGTLRAIAMHECVLIFDYNCKGGKAFLKSLLPRLNPRNMNVGCAMPFALEVVEAALLSRIQRLEQKLMEVEPRVASLLEVLPNRLTADVLEQLRLSKQTLVELGSKAGAVKQMLLDLLEDPHEIRRICIMGRNCTVRHGTNYMECSIPLDKQIAQEEEEEIEMLLENYLQRCESCHGQAERLLDSAKEMEDSIAVNLSSRRLEVSRVELFLQVGAFCVSVGALVAGIFGMNLKSYLEEKVGTFVLQITVSRTPALRTCARLVANSPLLLAPKVLAVVRFTAELSRADAGPEALKISNQIGSDSDLECIYTVTCSLVTRANSSDEALEIAKLISAKFVQQPTDRPVLQLKITMLPMGLAQLKPTIRPKDYKECKG | Function: Magnesium transporter that may mediate the influx of magnesium.
Subcellular Location: Membrane
Sequence Length: 651
Sequence Mass (Da): 71772
Location Topology: Multi-pass membrane protein
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A0A4R4QYA5 | SGGIDTNAWYELLNRNSGKALDVCGVSTADNACIQQYTRTGGQNQQWQFVDSGGGYYRIRARHSGKVLDVSNNSTADGAAIVQYGDHGGANQQFRVADSGGYVRLISRSSGKVVEVQGASTADGAPVIQYTDRNGTNQQWQLARVGGPTTPPTPTPTASTTPPPGSCNLPSTYRWSSTGVLAQPRSGWVSLKDFTVAPYNGKQLVYATTHDYGTSWGSMNFGLFTNWSEMATASQNTMSSATVAPSLFYHAPKNIWVLAYQWGGPAFSYRTSSDPTNPNGWSAPQTLFSGSITGSNTGPIDQAVIGD | Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
EC: 3.2.1.55
Subcellular Location: Secreted
Sequence Length: 307
Sequence Mass (Da): 32661
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K2E089 | MAGAVRISGEAALRVGAGLVSVATRKEHIAAINAARPEIMCHGVACVADLTVLLEKATVVIIGPGLGQSDWSKLLFHAAINLNKPMVVDADALNLLSQSPQKNSNWILTPHLGEASRLLGNTMVAIQENRLLSAENLVKKYSGVVVLKGAGTIVAAENAAPTMSHFGNPGMGSGGMGDALSGVIGGLLAQHFTLLDATKIGVIIHAKAGDMAAKAKGERGLLAMDLMDYFRKLVNP | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
EC: 4.2.1.136
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Length: 236
Sequence Mass (Da): 24475
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A0A9E7EJ38 | MRGETSGSGGGEAGPSSRPAAAVGERRFTPAAQPEIMRAAEKDDHYAVYVHDACRDAFRHLFGTRVAVAYQSEASLIKLLGQTLYYILTTGSGQQTLGEEYCDICQVASSYGLSPTPARRMLFIVYQTAVPYLAERISFVFSELKDYGEVICLQLQLLFIIHLLEATSHPQVEDGKMALCETNPPDANTDLGTGRDLPVLNEDGNPIPDNNSNKGSWATDSFALSEPQSSAGTSKCTLCLSSRQHPTATPCGHVFCWNCIMEWCNEKPECPLCRTPITHSNKGTLKVVIVDGEMLMGIMPYVQESWHLHAMKRARGSGGRFLDTKQLQQQDAWPSAITGCWNASSSNPCLDGGPISSSETSSSPNMMSISTSGSIIPQDEFGCSSPKYHSHATLNVQGGGSSTMQTGTKHRVPSTR | Pathway: Protein modification; protein ubiquitination.
Function: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Subcellular Location: Membrane
Sequence Length: 416
Sequence Mass (Da): 45041
Location Topology: Multi-pass membrane protein
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A0A6S4QF88 | MENLLEFYQNLPSFVSPVIFSIGAFQLRWYSLGYIVTFIVAGEVIKWRIRHKENTFPITALDVYDAYFYTLLGVILGGRLGYLIFYDFNFLQNYPMQAFLPFKIDENGWTFTGISGMSYHGGLIGFIVAFYVFIRRKQFSFFKVLDFFMPAIPLGYTFGRLGNFMNGELYGRVTEVFWGMYFINPNTQLPFDTLRHPSQLYEAAIEGIGVFAVLWTVRNYKLPTGTLSGLYLVCYGAGRFIAEFFREPDEFFKDPGELVGTVWGFMTMGQVLCLVMVLCGGFILYWARTVQKPATS | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
EC: 2.5.1.145
Subcellular Location: Cell membrane
Sequence Length: 296
Sequence Mass (Da): 34056
Location Topology: Multi-pass membrane protein
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R6F787 | MRGEENKARQQKEKISCQAEEEVGRLVRRLIETNPDRVIVCTEIGYGLVPVDAFDRAYRETVGRICTGLAGKAAAVDRIVCGIDTRIKEM | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 90
Sequence Mass (Da): 10067
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Q07FS8 | MDSNTITSFQVDCYLWHIRKLLSMRDMCDAPFDDRLRRDQKALKGRGSTLGLDLRVATMEGKKIVEDILKSETDENLKIAIASSPAPRYITDMSIEEISREWYMLMPRQKITGGLMVKMDPL | Function: Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in the host nucleus and are no longer exported to the cytoplasm. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism. Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated RIGI ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors IRF3 and IRF7. Also binds poly(A) and U6 snRNA. Inhibits the integrated stress response (ISR) in the infected cell by blocking dsRNA binding by EIF2AK2/PKR and further phosphorylation of EIF2S1/EIF-2ALPHA. Stress granule formation is thus inhibited, which allows protein synthesis and viral replication.
Subcellular Location: Host nucleus
Sequence Length: 122
Domain: The dsRNA-binding region is required for suppression of RNA silencing.
Sequence Mass (Da): 14056
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A0A930SVP5 | MGLTPLIEVHSQQELSAILPLLAALPAGRILLGINNRNLKTLQVDLRTTAELLPAIPAALRRQLPVICESGLHRHSDLLQMQALGCQGFLVGTALMRTGQPGAALRQLLQGEAAQKGSGPSTVSAVQVQPAVRAIGTAQKMAKTRAKTAARPVQPFSPRPWLKICGLTRAEDVQQVLRGGADALGFVFYVSSPRALAPSAAETLFARSGLLKLPAVAAQNSDQPARVGVFVNAAPAEVLTLARRLRLSHLQLHGDEDLAYIQALQALMTPAEATGLQLIKALHLQHTSDLKAAAGWPAEIQLLVDASPAPGSTARGGLRRPANWPLAAPLARQRPVILAGGLQPGNLASAWARVGPWGLDLASGVESAPGHKDPDKLRALFAAHHSLPAAPHNRPESKERAL | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 402
Sequence Mass (Da): 42390
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A0A9E7H7D6 | MESIRIVEFFKNKSILVTGSTGFLAKIFVEKVLRVQPEVKKLFLLVRAGDATSANQPYVAGEQSGLILEKKFLMGETLKGDSYLDIEAELSLADEKKRELRAEDAPEEAEKLAMKELGIRRTIDSVIIGYAKGKITCFFGDLDIIMDVVPGDMVVNAMMATMAAHSGQQAEFIYHMGSSVRNPVTYDTLEHCHFRYFLANPRVGRDGSVMPMKRLRFIKSMVVFRVFMTLRYKLPFEVSPPTHLCTVLPHAL | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 252
Sequence Mass (Da): 28372
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K1ZWQ9 | MLMKDIVFFGGAFDPPHLGHLAVLQFLETISRFDEVWVVPSFFHPYAKKMISYDHRIKMCELMLPYLSSKVLVSDIERQWGQHPCYTLDVIRYAKKKDPLQNFWLVVGSDCQKDLPGWYQYEKLKNEVNFFFLPRPGFKQSPFPNISSTVVRECLAKRNGMDNLVTKEILDYIIQNRLYC | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 180
Sequence Mass (Da): 21222
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K2CVE3 | MHKRLAALGIQSVEDLLQHYPSRYEDFSQIYSIAEAPLDSAVTLNVTIKKIASRTSWQRRRFTLVEATVTDDSGQLKVVWFNQTYIAEQLKVGMMVMLSGKIKQTKYGKQLVNPVFEKTKSETVHTARIVPHYPTTYGITQKQLRYFISQELTHTFTDWLPPEVIEQYDLLDYNQAIHHIHFPDSYEQLEQAKRRLGFDELLLLQLVSLQLKQSLAKEKAVAIPVDEASLQQFTKQLPFTLTTGQRQAAWDIMQDLAKPQPMNRLLEGDVGAGKTVVAAMALYAVARRGYQAVMMAPTEVLAVQHHHKLSQLLQPYGLTVGLVTAHHRTDQAASIIVGTHALLTGGLQLPKLALAVIDEQHRFGVAQRQLLKQKSGLGVTPHLLSMTATPIPRTLALTAYGDLSLSIIDELPSGRKPIKTIVVQEGERATMYTHVAKRIAAGEQVYVVAPRIEDEEESEKTSVEREYKRLQAHFPNVAMAVLHGQLKAKAKAAIMDSFRSGEVALLITTTVIEVGVDVPNATVMIVENAEVFGLAQLHQLRGRVGRSDKASTCYVCTNGRDAINRVSTIKRLQFFAKTSSGFTLAEYDLDRRGPGDVYGRTQSGFLNNLKIAKLSDHQLITMAQHAAKQLLPKLPKRVEQAIRQVHLE | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 648
Sequence Mass (Da): 72380
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A0A7C5IL46 | MKRLFIPAEEIKGNTAKIKGGDLHHLKNVLKKKVGDEIEIADDNGRIFKSIIKEIKEKEIIIELVAFKLINPSPFYIRLFQAIPKGKSFENILQKVTELGINEIYPLITERTVVVYEKERIKAKVEKWQKIIKESAKKVGNQFLPEIKFPISLNEIKTCISGEQKILFWELEEGVSLWTILEKNGFSKNIDVVIGPEGGFSIKEVEYLKELGFTTVSLGKRIYTVETAVIVALSNLIFCLERKVNT | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 246
Sequence Mass (Da): 28091
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A0A1H7JB32 | MVLGVSATSATASGDGPERLHILLTNDDGWDAPGITAVYDELVGAGHHVVLVAPATNQSGKGAALTFGGSLTVAQPADGKYAVTGTPVDAAEFGLSAVFDENDPPDLVISGTNVGENVAEGIIHSGTVGAAVNALADGVPAIAVSTEVDGDDVGPFAETAQFVVRLVDRLQDRAHRGDLLPDGIGLNVNYPLVEDGGQPEGVAATETGRGLFDLDYAGALPEPGQSSSFTFEYGLGLSADVRNSDLAALEADLVSISPIEADYDAGAGELRWVRGVVRELGRR | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 283
Sequence Mass (Da): 28890
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K1YPS5 | MKKEYRDNVEIILVSPSEPGNIGGTARAMNNMGFSHLGLVTPVDYKIPETYKFAWNSHEIVDNAKVYDSIPSAIKDKGYVVAMSTRKGRDRGRFEVLNDVVPEIHELAAKTKVAVIFGCESWGLTNDDLLHANRVVRIHTADKFPSLNLSQAVLVTCYELFNSKAKIDRDRLEPASREALELCFTHIEKVLAMIGYGDRGDRLLPKNIIKSVKKLVGRAILDPHEVAMLRGMCSQVEKTIEGFKLRKDKQDGIEK | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.200
Subcellular Location: Cytoplasm
Sequence Length: 255
Sequence Mass (Da): 28640
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A0A6I8N172 | MASGRIEVECKFVPGPGTEERLRALGGTLEHRTSFSDSYYDTAELTLMRADHWLRRREGSGWELKCPGPGVVPGPHTRYDELSAEPAIAARLGEVLGAGPRGADRVEVLLGPLGLQEVATFATQRSSWRLRPAGEEAVGPLTVDLDRADFGYAVGEVEALVGEEAEVPGALERIHNLRRLLGVPELERPPAKLLVYLQRFRPRDYRRLLAAATGQRRDGGGLRGRGR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
EC: 3.6.1.28
Catalytic Activity: H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 24884
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A0A9E7FM00 | VIQAPRFGKHKLDARSVASIILGGGAGAQLFLSLGTADAVRQFTWVFEKHFDTGADITISCVPVGVSRASDYGLIKIDKACKIIQFSEKPKGGDLETMKDENTFFRLSHQDPKKYIASMGVYVFNRNTLLELPRWTYPKANDFGSDILPSVVKDYNVQIHDAIISHGCFLHECSIEHSVVGMHSRVDYGAELKHTLMMGADIYETEAEIASLLAEGKVPIGVGENTKIRNCIIDMNARIRKNVVIATRDVCTTNKSFV | Pathway: Glycan biosynthesis; starch biosynthesis.
EC: 2.7.7.27
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Length: 258
Sequence Mass (Da): 28509
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A0A9E7EWB9 | MINIPTEAVDTYKQADFLDFDHDSATLEKCSYSTAETYMPIVLDSIANIPVGDAMCRNSVYADAAQSSFNLRACTSFDPPMHKPSANNAAKGNDNALAMPPYRSGEKFEDIYDVILILDDRENFGSRSRKIVDNIHTQFNILVEFRRLPVGDGIWIARRRGCNIEYVLDFIVERKRVDDLCRSIRDNRYKDQKLRLQRCGLQKLIYLVEGDQNCLEAAESIKTATGTIIDGNCTHESFGYKRMNAVIHFDLILKLDAEVVKAGTRSKQADGDSWTVGTSF | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
EC: 3.1.22.-
Subcellular Location: Nucleus
Sequence Length: 280
Sequence Mass (Da): 31585
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A0A0X8D690 | MEPYLTFLFSLSVFLIACVIVLENRNPSRTVAWLIVLNFLPVVGFIFYILLGRNVRKRKLFRNKFISNAEVLKKLETVPAGMLDENDFWDYPHLASKRRLLNLMMNVAESPFTLNNRSKILTNGDETFRQMIQDMSEAKDHIHFQFYIIRHDTTGQQFKQVLIDKAREGVKVRVIYDGVGSVHLDKKYIAELREAGVEVVTFFPVILPFLSNKLNYRNHRKIIVIDGKIGFVGGLNIGDEYLGKDTRFGFWRDSHVRLEGESVYLLQNIFLKDWFFVTNENINDDRYFPPLTESPGEELIQIAASGPDSDWESIWQMYFSIIATAQEKIYITSPYFIPDDSISMALKTAALSGLDVRILLPSRPDHHTVFWASRSYFQELLEAGVRFYLYQPGFVHAKILLVDGVVASIGTANMDIRSFQHNFEVNAIIYNSNSVYKLEEDFLRDLVDSKELTLAEYNQRPWHHRVLESVARLLSPLL | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membrane
Sequence Length: 478
Sequence Mass (Da): 55312
Location Topology: Multi-pass membrane protein
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A0A3M1LYB3 | MLDSFGVGASEDHRDRTRKIRDVQTVIGNLTENAARHRQFGRLERNNATELGCGHGQIGLGTIRDDADFQLVDNIALGNTRTFPCGLRTQTHSNCQEHDTQSEEHPAERGFNQWRTKLHRSFAAPMANSTIANWRWWLRATRPRTLPLSFFPTAIGLAWAWRDGAFNSATAGGTLLCAVLLQVLANFVNELGDYERGADTPDRIGPPRAVALGAISPAAMRNASRVLSAIILALGVWLVTLVGWWLLAVGLVALALAWLYTTGTRPLAYVGFGEVAALVFFGIVPAAGAYAVEHSRLATEPILSGIAFGCFAAAVLGINNLRDVEHDRACGKRTLAVRLGTTRATTLVQFLLGVPYAVAIVLSSATAEAAVPVASLPLAWRIGRELPLANGAEYTVLLGRTVLTASLYGVLLGTAIVVATMQ | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
EC: 2.5.1.74
Subcellular Location: Cell membrane
Sequence Length: 422
Sequence Mass (Da): 45342
Location Topology: Multi-pass membrane protein
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A0A364K399 | MDKIFFNKMVFYGYHGVYEEENRLGQRFHVDLEMKLDLSIAAKQDDLHQTVDYGRVYEVVKQEVEETRVQLIETLAENIAAKLLANFRIMEILVRVTKPDPPIPGYYESVGVEIVRRRK | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 119
Sequence Mass (Da): 14005
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A0A841R367 | MIGYLHGKITRLELDWCLLDVGGIGYRLRLPASTREAVGLGETVTLYTYLQVREDALSLYGFASEAEYDLFTLLITVSGVGPKVAIGIVSAIAPEAFFEAIRIRNKAVLMKLPGIGKKSAERLVLELKDKVPAASGASVDWPEDVATAQSATGPVAETVQALVGLGYTEQEVRGAAEKLAAQYPQTDRLLRAVLAQLGKERG | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 202
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 21675
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A0A7G9G532 | MKIIGVTGGVGAGKSTVLEILKEDYGAGILMADEIGRELMEPEGACFAQVRDAFGEGVMKRDGTLDRGKIASAVFRDQAALKRLNGIIHPAVRKETERRLQDLEISGKEIAVIETAILFEAGYEDICDVVWYVYADEETRIQRLMKSRGYGRDKCREIMANQMPDSEFRRRSGVVIDNSGSREDIKEQIATSLSL | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Length: 195
Sequence Mass (Da): 21663
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A0A1I7ZFG8 | MAAQRWSAFLLLAFLALGCAAQKPILKPEELEVSVELGETKEISFHIDVELDADVLVTFSNTSGYIELSAEEFVLSGTNKTGSVTVKGVKVTSITYLRIATCRYKDGSEDSKCPLNIEQSSVHIKVVHSNALSIVIIVVGWMYFVAWSVSFYPQIWLNFKRKSVIGLNFDFLQLNIIGFTCYTIYNALMYFDSYIQTLYHKEHVDALNPVLLNDVVFALHALFACIVTVVQCLIYERGTQRVSYICMGLSSVFILFAAVSLVLSVVDVLSWLQFINNLSYVKMGVTLSKYVPQAILNYRRKSTIGWSIGNVLLDFAGGTMDICQMVLQAINTDDWSGFYGNPVKFGLGLVSIVFDVFFIVQHYCLYRHVKVNDAIYEGITNSATSTTISQNNVEAGSTEGVGTVYGANASTVAVRDNNS | Catalytic Activity: H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in)
Subcellular Location: Membrane
Sequence Length: 419
Sequence Mass (Da): 46458
Location Topology: Multi-pass membrane protein
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A0A660TR21 | MEDVKHRKSIMDKIKKNVSLSGYTTFKVGGPADYLVEIVNEFEFKEAIQWAIERDIRYFILGKGSNVLFSDDGYRGLIIYTGRYKRIFRIDNRIIAEAGAMIDELIDYATDNSLTGLEFLAGLPGSVGGAVYMNARAYGGEISRVITEGRVLIVDEKDKKIKEAKLNREAMDFSYKKSIFQSGNIYLMDAVFYLKKGNQLEIKEKISEIRTLRKSKGEYLFPNAGCIFKNDYSAGKSSGRIIDECGLKGMRVGKAEVYEKHANFIINKGGANASDIYKLINFIEEEVMRKTGIKLQKEIVLVGFDQ | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 306
Sequence Mass (Da): 34584
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A0A364K2X0 | MNNKNAPFPYWIIILLITLAIAYFIRHDVFTPYEVQGKSMYPTLYGGEILIVNKWIYQFDEVEFGEIIVFHMHEPGKKSKDFIKRVIGLPGDHIIIQAGKLIRNGELLQEDYINEPMNNDRPVDITIPKEKLFVLGDNRNNSKDSREIGLVDLHDVVGRVEVIIYPWERMRCLSDDDGAN | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 180
Sequence Mass (Da): 20875
Location Topology: Single-pass type II membrane protein
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A0A9E7F3K4 | MAFYKRSRVARDAPPLRRVLPLVLVVLASVLFVVFMLKNRAVAGPSSFPFPNLENPAAILADPSFKLKLPKQTLLSVSLDQRNRLPPRNTDLFPTLAKDHTKIVLYVHNRPQYLRAVVRSLAGVEGIGETLLIVSHDGYFPEMDGIVRGIRFCQVKQIFAPYSPHLFPDSFPGVSLGDCHDKDDPAAKKCNGTADQYGNHRSPRIVSLKHHWWWMMNTVWDGMEETRGFDDHILFIEEDHYIYPNAYRNLQLLIGVKPTKCPECYATNLAPSDVKFKGEATDMLIAEKIGNMGYAFNRTIWRKIHAKAKEFCSFDEYNWDITMWATVYPSFGAPVYTLRGPRTSAAHFGKCGLHQGQGKSGACIDNGEASFQLDQIDKILNIKPDWQVLADFLSSTLHLAPLAEGSITLQIIPRMEFIGTAMQIVPLEFSLFFAAIIDLVDKLFLNVAMGRPTRDRQYLFTSTMADEELVDPKKYLEDSCKPKCARPLHTYQACVRRIKGDVSGHKHCTGQYFDYFSCVDNCVETAKTCDLRLVFGLPTIIFWGKMQHLRNSITKHVRLGCSTGLSEFGAAGRQLNSPCQRFCVSSSNTSMADLTARVLELVKKFDKLDASKVTEKADFQKDLCLDSLDRVELVMAIEQEFSVEIPDQKADKLSCCADVVKYISEAQAEKKAST | Pathway: Protein modification; protein glycosylation.
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Catalytic Activity: N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP
Subcellular Location: Golgi apparatus membrane
Sequence Length: 674
Sequence Mass (Da): 75870
Location Topology: Single-pass type II membrane protein
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A0A6P3V5L5 | MLSEKVNIVFHAAATVRFNEPLHVAVNVNTKGTDRIIELWNQLKHPISFVHVSTAFSNANLHEIGEKVYTTSLKPSEGDKNSINLMEKGILKTYPNTYAFSKNLAEQIVASKCKDLPVAIVRPSIVGASLQEPCPGWIENISALTSTIVLIGRGCATAIRGRRDAISDIVPVDFVVDMIICTAWHVTLHRDHEVKVYNCTSNACPFK | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 207
Sequence Mass (Da): 22838
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A0A0E1SJJ9 | MPPRSEPGARRGEPRAGGEPAPRASMARALVDRFGRAVTYVRLSVTDRCDFRCVYRMAQDMRFPPRSDVLTLDALAALARACVALGVRRIRLTGGEPLVRPGLTTLVERIARLPGLDELALTTNGARLAQFAAPLKAAGLARVNISLDSLREDRFGTLTRTGRLRDVPAGIAAAKRAGFRRIRLNCVILRGRNDDEVLDLVRFARAQRLDLAFIEEMPLGAIDEHDRASCFVSSDEVLARIRGRYALFPSDVSTGGPARYFRMADSEIRIGVIAPHSHNFCGDCNRVRVTASGRLLLCLGNEHGAELRDVLRTSPGDDARLRGAIAAAMPLKPERHRFDLDAPHIVRFMNMTGGGREDVRECPRNRAVRSSLERHAVQLQDDARAGLAFQDRPVRDDRARDRRAAADARLQCRQRALRRSSGVLQHQGARRPVDLAAAAFAGRRQIARRGQADRFADHRQSAAGQASLSAVDGHGARALHQRDPRSRLLRRVRQDRAHARRALEERARLFRSHHDRIARKRVLRRSRARQADLLPERDARDVRASGAADRADRIGQAVRRRRAAAARSRGRSRDGLRRPEHARRSRRDAGAARLCRRHEPCAGRLRDRARVRREMTRRVGA | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 621
Sequence Mass (Da): 69445
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A0A6S4QH43 | MSSFLMQLDPFWVALLSLGVYATVLLLFFKYGGQAGLYVYMAVAIIGANLQVLKVSYFEFLQSPVALGTALFSSIYLATDLLSEYYNPAAARKGVLLSFAALLLWTILTTLLLAFAPLTPAQAGADYQWALTIHPALIHLFQPVPAIFVASLTAFLISQSLDIFIYSAIKKRTHSKWLFVRNNFSTILSTLIDNAVFSFIAFVLLAKNPIATKELIFTYILGTYALRILYALLDTPFIYLARFFKPKALRL | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell membrane
Sequence Length: 251
Sequence Mass (Da): 27978
Location Topology: Multi-pass membrane protein
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A0A9E7JD98 | MIPFSFHSLFSCVVPCATILFAGALSPFQVERKIDLVYGGGSVGLMGLISKTVLDGGCHVLGVIPTSVLPSEVSGESIGEVKVVADMHERKSEMAKHADAFIALPGGYGTMEELLEIVAWYQLGIHDKPVSSHLIQLAPFHHDIELHEGLCCVVQVGLLNVDGYYNSLLALFDKGVEEGFIEGSARHIVASAENAEELIRRMEENET | Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
EC: 3.2.2.n1
Catalytic Activity: 9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-phosphate + trans-zeatin
Sequence Length: 207
Sequence Mass (Da): 22378
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R6EMF8 | MIGNGSNLLVGDGGYRGVVIQICKNMNKIRVEGDMVYAQAGALLSKTAAQALEHALTGMEFASGIPGTLGGAVMMNAGAYGGEMKHILYNALALTKDGEFRVVPADRMELGYRSSVFAKNGDIVLSAQLKLQPGDPEKIRAYMEELKEKRVTKQPLEYPSAGSTFKRPEGYFAGKLIEDTGLRGFRVGGAQVSEKHCGFVINRENATAADIVSLMEQVADRVEAKFGVRLEPEVRRIGEF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 240
Sequence Mass (Da): 25963
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A0A924IMG2 | MFTDPTIPDPQTTSLAVYTLSDSTGETAEAVARAAASQFPGQRLSIDRLPRVLEVGQIPRIVERLAQRQPCLIGYTFVVPGFREALETAASQHGIPCVDLLGTLIRTMGSMLGMQPSPRSGLLHTLDAEYFARMEAIEFAIKFDDGKDPRGLLAADIVLTGVSRTSKTPTCMYLAQNRGMRAGNVPLVKGVAAPPEMFSLERGRVVGLTIDPALLYEIRVARLAAMGLPRSSDYAKFENILSELQYAGDIMHRLGCPIVDVSHKAIEETASEILLLLR | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
EC: 2.7.11.32
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Length: 278
Sequence Mass (Da): 30240
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A0A0B4R6T4 | MIGWDFRLDALKRGLEPEAGAVKDRVSGLERADLFAREAGPLQPDEIQSDGNRPEAGVQEERRRVAVESRVAGDHCQLAYEGELVHAHPAGYECLVLHLDVTGQQGAATDHGVIANLAVVGDMSRGHDVVAVADPGDRFRLGAARNRVVLPDPVVVSDMKVTSFTRKRLVEGVGAKHGSGRDLIPVSERRPALDMDVGLQPAGCADAHVRLDHAVFADYGTRTDRRAGMHPGRRRDDGGGINRHNLVSYSVAGEEVTVRVRELAEWLGAPFEGDGEKDLDRAGTIESAGASELAFVSSRKAAKQAGFSAAGCLIVPLEHENTPPRTVIRVPDPRTAFARAVSRLHPFAPVVPGVHPSAIVAPDARIEPGVAIGPMAVVGEGSCVGAGSAIGAGCSIGRRVTIGERCIVHANVTVYDDVDIGNGVILHSGCVLGADGFGFVLQGDCYQKFPQIGRVSVGDNVEIGANACVDRAALGVTWIGEGAKLDNMVHVAHNCRIGRHVVVAAQTGFSGGVVVEDYAVIGGQVGVGDKARIESRAVLGSGCGVLTSKIVRAGQVVWGTPARPLKEHLELLANLGRLPDMRRELAELKKRVQALEGSRRE | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.3.1.191
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Length: 601
Sequence Mass (Da): 63509
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A0A059WIG7 | VKDLEISAQLREVMGAGEVRLYEPLSKHTTLRVGGPARFWVEPETRGGLANVLEFCAVSRLPVLFIGRGSNLLVRDGGIAGVVIHLNRGDFVELKVDGTELHVGAGIRLKQVAAAARNAGIGGLEWMEGIPGNVGGSLRMNAGAMGAETFEQVVSVQVVSSRGEFETLRPSEMQIQYRNAPTLRDRYAVSAVFRGEAASLEAIDLRLAESSHKRKTTQPIAASAGCIFKNPPECPAGKLVEELGLKNRRVGGGRVSEIHGNFIVNDGGARAEEILRLIAEIQLIAKEKRGIELQTEVQIVGVDDE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 305
Sequence Mass (Da): 32807
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A0A532V4V8 | MNFKALLGKPINIVMVVFAVIGVVLLSRVIVQTFVFSPPEQAVVHDGEASVHSQEREAKKEEKKKDSHGGGQGEGEEPEEGIHMIENLVVNPANSGGRRHLMVSLGLEYHELHVKEELERLDPPIRDNLITLLAGQEMGVLADIKYRERIRKSLLKAINYYIEDGRVEKLYFVRYVFQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 178
Sequence Mass (Da): 20173
Location Topology: Single-pass membrane protein
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K2B6Z8 | MNRFFGLIRKIIIMTLATCGVLVAGLLYYIEYELPDINALNTVQLQVPLQVFTKDNKLIATFGEKRRVPVPYAQIPTPLIQAVLATEDQRYFQHAGVDIPGLGRAAVQLVLTGRKLQGGSTITMQVARGFYLTRRKTFARKLREILLAIKIESRLSKQKILELYLNKVFFGNRAYGVEAASQVYYGKHLNELRLDQLAMLAGLPKAPSTLNPIANKEAALRRRNHVITRMHEEGYIDDATYHKAMNTPIDASYHELPTEIKAPYAAELVREQLEQMYGDSIYTDGFKVYTTIDSRLQNDASIAVRDNLLAYDQRHGYRGPEQNFGMPSLDSMNDWEQKLKKIPIINGLEPAAVIEMTNKTITVLRADGDLTIINWNGLSWARKQINADYLGAKPTRAAQIVKPGDVVRIISTPTGYQLAQLPKAEAGLVAINPLNGAILSMVGGFDYQTSKFNRITHAQRQPGSSFKPFVFSAAFEKGYTLATIINDAPIVVENPTDNSLWRPQNHERKFYGPTRLRIAITESRNLATIRLLALSGLSYTTNYVQKFGFARSQLPPGLSLALGTALVTPLQMAQAYSVFANGGMKVVPFIIDTIHNSQDQLIYQARPLEVCKNNCSKEVAAAPRVISEENAFLINSALHDVIQSGTARLAKSLNRDDIAGKTGTTQNQVDAWFAGYHPDLVAVSWMGFDQPQSLHEYGSQAALPMWIQFMQSALKGKSSHSLQQPPGIVSMRINPYNGKHVTGDDSNAIYEYFMEKFTPEKAAASDETPAYVNQENDQDYPGHPYDPSSVDDNSENKMVESVY | Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
EC: 2.4.1.129
Subcellular Location: Cell inner membrane
Sequence Length: 803
Sequence Mass (Da): 89465
Location Topology: Single-pass type II membrane protein
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A0A151FE90 | MNWETLVDALKRYGYIKSPEVEAAFQNVDREKFVLPEYKNRAYSDTPLPILCGQTISAPSMIAIMLEVAQLEKGLDILEIGCGSGYNGALLAEIVGEEHVITIERIPELAEWGKKNLEAAGYHVKVVVEDGTLGYPECAPYDRIISTAAAPKIPQPWVDQIKVQGLIICPVGSKYWYQELEVVRKTEQGNVETTHHGGCAFVPLIGKEGFRR | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.77
Subcellular Location: Cytoplasm
Sequence Length: 212
Sequence Mass (Da): 23532
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A0A2H5YTS6 | MQLARSTLGELAGKRALVIGAGEMGRLVAASLASYQPGWLGIANRTGERAREVARKVGAQPVPWECLDKTLATVDLAVVATGAPEPVLTRSRIERVLAERGERPLLLIDIAVPRNVEPAVAGLPGIELRDIDALETLCAEGRRARERAIPQVEAIVEEQVQEFLEWERARAVAPVIRQLRERVEAIREEETARALRRLGHLSERDRQVVLALSHGIANKLLHLPISRLRERGAQDLYIHAIADLFGLDDR | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Length: 250
Sequence Mass (Da): 27626
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A0A7V0SFN4 | MRYLFDVWEDFSNACLAASHIIFLSDYDGTLTPIVSRPEDALISTEMKERLTDLAKVPKFSVGIVSGRGLEEVQSMVGIGEIYYAGNHGLEIRGPGIDYINPEAEQSIAVINELAARFEELFRSTEGIIIQNKKLSMSVHYRLVKPDDEPMVEMTVRNTVKPYIDNRKVRLFPGKKVWEIRPPMNWDKGKAVQSIQDIIRKKEQKDDILTVFLGDDTTDEDGFRVVQPPDGWSIYVGPESMSSAAGHYLKDTGEVGRLLQRLAGLR | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 266
Sequence Mass (Da): 30007
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A0A4V0XB68 | MLLQTIFIALDFGNTRLKIYAEGPLLIKAIAYDKTNWIDEAFECIQSVMQQKSAIIGYSSVNAVDEAKLIQKCSKLSSISWINAGDIAYNASYPDFSCIKGIGYDRVLGIIGALQFTSAPFITIDCGTAITVNVLNIDGVCLGGAIMPGFSTMHASLHNSTAQLPKLQPDSLKYSIGKNSIDAIYAGINTAIKGAVKEYSSQFPEYSIVLLGGDAHILFELLEDEQKIKSSIHADCIATGIFTIIKDLP | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 249
Sequence Mass (Da): 26898
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A0A4P5UQS3 | MNTTIKHFIYAARMRILPASAIPTIAGIMLAAIDGAYDFFTAFITVLSAMMLQTTSNYLNDLYDFKKGADLKRIGPPRAVASGMISEKAMTIMSWVMFTLTFFIGLILVQKAGWPILVIGIASLWAAFAYTGGPYPLAYHGLGEATAFVFYGLIPVWGAYYIQSPDFAFRPQVILTGIIMGLFAAKILLVNNIRDIETDPIAGKITLAVMLGEKKSRLLYALLMVFSYGSLFLLARMQDNVVYLMPWILLPFAVYLTKGVLKTEKEQLNPYVFKTAIHLFAFGIILCIAMYVGMQK | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
EC: 2.5.1.74
Subcellular Location: Cell membrane
Sequence Length: 296
Sequence Mass (Da): 32871
Location Topology: Multi-pass membrane protein
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A0A4V0XAS9 | MQNQSEHIQDTNREELRFKGIPTSQGIEFGKAIVLFKEGPSSYPIHISEESIPEELERFSAALVNASEELQHIIDIAQKESAKISHILETYLLILMDSIMHESIRTRIKEGYTAENAVIHEFDVQKQFFTLAKDPIIRERSIDFDHVTERLLNGLRNRTISHAVAEGSIVIGSSITPTDLMLFHKAGCLGFITEIGGIASHASILARSLSMPAIIGLRDISEKVQDEDAIIIDGFSGILIVHPTEDTRSFYIQKKKEADDNKLSLGLLANTECTTLDGYPIHLMANIDSIEDLHVAMKYGAKGIGLLRTEYLIIARQHFPTEQEQIEWYKELSHISFPHPLTIRAFDVGSDKYAEGLAEEDNPALGLRGIRFLLQRKDIFKNQIRAVYIASKEKNIRFMLPMISTINELKISLAFIEESRLELEHEGIPHDMALPIGIMIETPASALISDSLAPLVSFFSIGTNDLTQYTMAADRLNEYVSDIYDPFNPAVIRLMKMAIESAKKYGINIGICGELAGHSAATELLIGLGIQEISVSPPLLLELKKRILHINYSEVSQLH | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 559
Sequence Mass (Da): 62537
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K2AH65 | MLNPFGWAGLGVLGLYLTAFFWGGSLAAKAAGKSVWLFGQAKGRHRLAAFGFRAAFGLALAGPLVWLALAPLHKADPLWTDGSLPLVSLAGLILSVAGAMLAFAAQMSMGASWRVGVSQGETGALVQGGLFRFSRNPTFLGQLLLLAGLVLAIPSLPTLAGVLLFFWSAHVQIRSEEQALSASHGADYAAFTRAVPRWIALGKGTSATPIGHLVLIAVAAVVVDQATKAAALRMLTEGDPVAVLPFFNLTVGFNEGASFGLLGGLMAGQPLAMAALTGAITLVIALWALRSQNWIERTGLALIVGGSIGNIADRLRQGAVTDFLDFYWKDWQWPAFNMADVAIFCGAVLILLSAVLAPRKDHGVV | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 365
Sequence Mass (Da): 38227
Location Topology: Multi-pass membrane protein
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A0A847Y7S5 | MDFLRPDVDLEAHFARLAGGARGVLLCDYDGTLAPFREVPAEAVPHPWVPHLLEAIAAVGTRVVMVTGRAADDLAAVFPVRGLEVWASHGRERRFPDGRVSLLPPEPAAEEALNALHERLAGTLSAARCERKPGALAVHVRGLSPEHVARTEREVRRLADTPEAAPLQLLPFNGGWEFRAPGADKGLAVRTILEEEGRGRPVVAYLGDDRTDEDAFAALGPRGLKVLVSAEPRPTLADVRLDGGDEVRGFLAHWLMSVKEGRHAG | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 265
Sequence Mass (Da): 28626
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A0A841R363 | MIFPASLGQNAGLNFPEAILGFLFTGVGLPLLGVMAIGYSGSRDLQELASRVHPIFGLLFTILLYLTIGPFFAIPRTGTVSYEIGIKPFLGAATGNLELSIFLAVFFGLSWWFSISPAKLVSRIGKVLTPLLLLFLGILIVKSLISPIGPMQAPTKLYATSGLAFAQGFLDGYNTMDALASLVFGIIIVKSVKQYGAEFERDIAAATFKAGLIAAICLGVVYVFIGNIGATSVTGIGMQETGAPVLSLSTQFYFGDPGAFILAIIVVLACLTTSIGLITSCSTYFNELVPALSYRVWVCIFSVFSAVIGMFGLSTIISAAIPVLMFLYPLTMVMMALTFLAPLFDNRQAGYLITQLFTLVPALYDGLRTAGFEMPALTNWMATNLPLFDYGLGWVSFAVIGFILALCYVKFVKKTPTTV | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell membrane
Sequence Length: 419
Sequence Mass (Da): 44895
Location Topology: Multi-pass membrane protein
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A0A9E7FR52 | MEFWALLLVASRPVLQVLLVGLIGAFLASGFVNVLSSSARRDVNKIVFVVFIPALVFASLAKTVTAKDIISWWFMPVNIGITFLIGGILGWAAVKILKLEHHLQALVGNLFIWTHTYSLIRKSVSHSTGNHRHDVLTRMNKNPETNRKTRIFDAQEEQDYDDQEALLLPPSDTSDTTAEHQSIIGFTVGAVPWLKAFIVGETAPLKVVQDSMTLLGTAQVNSKACGDRSHHLCAITSFSLFFLLHRMQDTNLSHRELLKENAIGSRSFEMWPSVTLRSHYPVALLETMRSVSFPWKLTSEGVQTSTLTRPLRGLSWSAQSKNIIFSSNTAAFMSPNALRVPLYLKAQLPSTTPALPSPFRDEPMPPAARFLTTSAPPPEPNTNVVVILAALLCAAVSAVVLALVARCCACPWRSLGGGGSRAPPDKGLKRTALRQLPKVSYGGAAGGEEPAECPICLAEFEEGEQLRVLPQCGHGFHAACVDAWLGSHSSCPSCRRVLLVAAPPSLFQGCREGSVDAAAPASASAAGRGGEGERLFCPNGKELRDDLKWHALCFRNFQEHKYQSHGAHNCIYSKDTGKANRIEHNRKCVCDNDVTNPECEGTDGYAHTTDPSWEDLGTKNIGNWAESHDKAAEIDNNTDSREHGVNHSSHVHKSRLAHQSSSLNKFTFFRNINSWKGNKGTPPRPRNALLV | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 691
Sequence Mass (Da): 75593
Location Topology: Multi-pass membrane protein
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A0A3M1LTI2 | MRAVLAHPAFGLLARAIVGGIFVMYAVDKVAAPADFALNIERYQLVPLALVNLLAIVLPWLELVVGLCLLFGIRLRTNAVLAALMLVVFIGAIGSAMARGLEINCGCSARSETVGWGKIAEDAAYLLLTLRIAVKPDRVLTLEIQQGTAPGVVAR | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 16449
Location Topology: Multi-pass membrane protein
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A0A1J4S2Y8 | MEKNHTRKGKLIIIEGGDGSGKKTQLDLLVQYLENHSTKKIHALDFPQYYSSFHGRTVGRFLSGEFGTLQEVNPYLASLAYALDRLSVKEQMDEWLEAGDYVLCNRYVTSSMAHQTAKLSGIEREKFLDWIYELEYKKHKLPLEDTVIYLHVPFKVAQKLIAKKDKRKYLKDGKKDIAEEDTRHQLEAEKVYLKLTSRYKQWVKVDCVGANGRLRSKKSIGREIIRKLTGRKIIE | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 235
Sequence Mass (Da): 27310
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F7XQR7 | MNDNFINQEKIWPLIYVGFGGSSGAILRMGFLGLASTPFNILIINVLGSFMLGVLMYSTEFGNVNPHFRLFFGIGFLGSLTTFSNFALQTYTLASVSLIYSIANIFLNLILGIAAIIAGREAVIYVSSRRNR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 132
Sequence Mass (Da): 14484
Location Topology: Multi-pass membrane protein
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F7BNL7 | MGRGGGTFERLLAKYAVSSIKKKVNDKNPHVALYALEVMESVVKNCGQTVHDEVANKQTMEELKELLKRQVEANVRNKILYLVQAWAHAFRNEPKYKVVQDTYQIMKVEGHVFPEFKESDAMFAAERAPDWVDAEECHRCRVQFGVVTRKHHCRACGQIFCGKCSSRYSTIPKFGIEKEVRVCEPCYEQLNKKTEGKAASATELPPEYLTSPLSQQSQLPPKRDETALQEEEELQLAIALSQSEAEEKERMRQKTTYSMYPKADPTPVTSSAPAPGSLYSSPVNSSAPLAEDVDPELARYLNRNYWEKKQEEAGKSPTPSAPVSVADAAPPPGEGHATPGPGAETPLPDPDAQPLPPSGGPFGEQQYQNGESEEEHEQFLKGLQNAVTTFVNRMKSNHLRGRSITNDSAVLSLFQSINNMHPQLLHLLNQLDERRLYYEGLQDKLAQVRDARGALNALRDEHREKLRRAAEEAERQRQIQLAQKLEIMRQKKQEYLEMQRQMAIQRLQEQEKERQMRLEQQKQTIQMRAQMPAFSLPYAQLQAVPASGGVIYPPSGPGGFPATFSPAGSVEGSPMHTVYMTQAGGGPYPSVPAAGADPSMVSAYMYQAGAGGGQAAQAGQAVPTTNPAYSSYQPTPTQGYQNVASQAPQSLPPPISQPPQSGALGYLGNQSVSLGYQPYGMQNLMTTLPGPDPALPPQQPYLSGQPPMYQQMAAPGGPPQQPQPVAPPPPPPPGPGEAQLISFD | Function: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation.
Subcellular Location: Cytoplasm
Sequence Length: 744
Sequence Mass (Da): 81773
Location Topology: Peripheral membrane protein
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A0A345UNI8 | MIAYLRGLLTEKGTAHVIVEAGGVGYIAGVSSQTLEALPETGNEIRLDIYHHRTEADERLFGFAGSVEKQLFEKLITVKGVGPKVALGVLSALDGEQLVRSITTQDVRALSTAPGIGRKTAERIVLELSDKMTDLQGLSTAAETGTKGRGSGTAAAEALSALEALGYRRAVSEKALQAVLRTEEGSTADAQALIKAALRQLS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 202
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 21216
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A0A6N4E7E2 | MGTDYKGIILAGGSGTRLHPLTRSVSKQLMPVYDKPMIYYPLSVLMLADIREVLIITTPHDQSAFRHLLGDGSQWGLEISYAEQPNPEGLAQAFLIGKRFIGNRPVCLILGDNIFFGHGMDRLLGNATARGEGGTVFGYYVKDPQRYGVVTFDDYGKAVDLEEKPPHPKSNYAVTGLYFYDNDVVDIAGQVRPSARGELEITDVNRAYLERNRLNVELMGRGYAWLDTGTHESR | Function: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
EC: 2.7.7.24
Catalytic Activity: alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose
Sequence Length: 234
Sequence Mass (Da): 26060
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A0A660UBT4 | MNYFDSVDYYEVEKGRPNVVALKKGKGGGKSLLFNAHSDVVTVSKEQWENWSVLSPFDGGVKDGKVWGRGATDMKGGGTAMLFAAKAIKELGIELKGDLLLSYVDGEESGRAEIGIWSIPNRGYNADFAIMCEPTNLFNVYNKSKGEIYFDIKIKGQSTHICNRYKTIWPQKRREDQIGVNAIDKAVKLINAFAELERSWGIEYNEPSLDPGCTTLTVSMINGGESFSAQAGECTFTIASMFAPYLSVDEIRDQIVSTIEYISKTDYWLKNNMPEYSNPFPPKIPLNVPESDPGIQTIVGAFEDIFNKKPNICPSPFVGDVNYLFEKGVKGVNWGPGDLSMGIHGADEHVPVQQVLDAIKLYAATIIKWCGL | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Length: 372
Sequence Mass (Da): 41129
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K2BUS2 | MLGCLLIGVLFGLFEAKLLLNPLWRTGLMIGLLGGFTTFSSFSIDTIHLLQTGEYVAGIANVIISVVACLMATVLGIWCVAVFVK | Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Membrane
Sequence Length: 85
Sequence Mass (Da): 9076
Location Topology: Multi-pass membrane protein
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A0A924IKA9 | MIIHIDMDAFFAAVEQRDDPALRGRPVIIGGDRTSRRGVVATASYEARRFGIHSAMPLSEALRRCPDGIYLRGDFHKYRSVHEQLVALWRQFTPTMQVVSIDEAFLDIRGCERLFGPADVMAAEIQAITSRKLGLSASLGVARNTLVAKVASDHAKPHGLTIVAPGGEAAFLAPKPLRALRGVGPVLAAKLHQLGLRTVADVARAEPEWLRRAMPSGADGLQAMARGEGSEQLSADTPRKQIGSEATFAYDTAELEYLAARLLAQAREVAGTLRRRGQVARRLTLKLRDRSFQTQTQGLSLQVPSDQDQDLYRAARQLLDRHWHGEPVRLIGIAVSDLGEQTRQLDLFADPDAARRRQIGHCLDAVSDRFGQSAITWAKTLIPGND | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 386
Sequence Mass (Da): 42370
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A0A924BEV9 | MTTKERRTKIVATIGPACSSKEMIKTLINAGVNVFRLNFSHGTHEVHIESIKNIREVAKELNAIVAILQDVQGPKIRIGEVENGEAILNDGDTFFLTNKPVLANSQIASVTYEKLLEDIKVGSTVLIDDGKMEILVVGVDEEKLTCIVQVGGIIRPHKGVNFPGVSLGISCITEKDKEDMLLGLKQRVDFIALSFVQRAEDIMQAKDFLSRYNAKIPIVAKIESQSAIDNLEGILAVSDAVMVARGDLGVELPTEDIPLLQKKIIKMCNTFGVPVITATQMLDSMVSNPRPTRAETTDVANAIFDGTDAVMLSNETAVGKYPKEVVMMMAKIAQKADEELMKNFSLNYTGLQLYTISGSVSMAATYIAQSLNAAAIITATFSGSSAKKIARYRSPALVIAATPEPSTLRQMALVWGVKPVLVPPVYDTDTMIKNVLDISTRDGYIKDGDIAVITTGAPIGVAGTTNIIKVEVVSTVLANGTGLGKMIAHGNAVFANTADEAISRVSKGDILVTSMTDIDFIPAIERCGALITEEGGLTSHAAIVAMSLGIPLILGVAGIFDKIKEGDMITVDPRRGLVFAGNLKIV | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 586
Sequence Mass (Da): 62701
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