ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A286XVW4 | MSEFWLCFNCCIAEQPQPKRRRRIDRSMIGEPTNFVHTAHVGSGDLFSGMNS | Function: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages.
Subcellular Location: Cell membrane
Sequence Length: 52
Sequence Mass (Da): 5959
Location Topology: Lipid-anchor
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H0UYI9 | MLASGLLVVALLACLSVMVLMSVWRRRKLLGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISKRYGPVFTIHLGPRRIVVLCGQDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSITTLRDFGVGKRGIEERIQEEAGFLIQAFRDTRGAFIDPTFYLSRTVSNVISSIVFGDRFEYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFSSVMKHLPGPQQQAFKELQGLEDFITKKVEQNQRTLDPNSPRDFIDSFLIRMLEEKQNPNTEFYMKNLVLTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKIHEEIDRVIGKNRQPKFEDRAKMPYTEAVIHEIQRFGDMIPMGLARRVTKDTKFRDFLIPKGTEVFPMLGSVLRDPKFFSNPRDFYPQHFLDENGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFLTTIMQNFRFKSPQVPKEIDVSPKHVGFATIPPNYTMSFLLR | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases.
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
EC: 1.14.14.1
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 494
Sequence Mass (Da): 56868
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F3KYJ9 | MHFLGLLSSIWLVLNVLQNQLGPDPVKQLVLLTGERGFQFLLFSLAISPLARLLTAPLLIQWRRPAGLWAFYFLSLHLLVFFQGYIGWSWTILIEELKERPYISVGALAWLLLVPLALTSTRRARLKLGRRWRLLHRLVFIVAALACLHIIWQVRSDWINAGVYTLTCVLIVGSRYRNLRCFSKAI | 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: 186
Sequence Mass (Da): 21450
Location Topology: Multi-pass membrane protein
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A0A923XKS1 | AQARQTRELQRDLLRTRMVEFEGISDRLYRVVRQASKEIGKQVKLDITGGSIEMDRGVLDRMTPAFEHLLRNCVAHGIEAPDARLAAGKEAVGTIVIGLSHEGNDVSVQFDDDGAGLDIPRIREKAMQQGLIAPGQEISDQDAANLIFMPGFSTASAVTELSGRGIGMDVVRAEVNALGGRIETRTQAGKGTSFKLVLPLTTAVTQVVMIRTGTLSIGVPANLVELVRRAPAKEVQQAYNSGSYEFGGVTLPFFWSGALLQASQRSAEPQGKTLPVVIFRSAAQRIAVHVDEVLGNQEVVVKNLGPQLVRLPGLAGMTVLASGAVVLIYNPVALTAVYGEVARQLSADNAQPEVLAQAGITLPAVAAAAPQVPLVLVVDDSITVRRVTQRLLAREGYRVALAADGIQALAKLAEERPAVVLSDIEMPRMDGFDLARNIRGDARLSKLPIIMITSRIAEKHREHARELGVDHYLGKPYSEEELLSLVKHYCSAEIPA | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 496
Sequence Mass (Da): 53367
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A0A525D908 | MDSQDDMHNTASNHSQAIGETFAGIDFNVVKGSFRDDLVITSITADSRKVTAGSIFVAVRGLKSDGHRFIEQAVKAGAVVVVAEQGNFSADKSLTGQAVVVTVEDTELILAYLAANYYQHPAKQLFISGVTGTNGKTTVTYLIERVLKELEIPVGVIGTIEYRFPDPAGELIIIPAPFTTPDPILLHAVLRRMVDNGVSHVIMEVSSHALEQKRLGPITFSQALFTNFSQDHLDYHHSMEDYFEAKCLLFREHSNGSTQAIIYDPDHHDREKSLWAQRLVTLCKSLQLPVVTCGDSAQSQVRLNRCTGDRHGIYLEFLDSSLTHRILSSPLVGRFNVENLLLAYTALEQMRFDSDRVCSILSTAPGAPGRLDPVSFHQLSDNLPSTYVDYAHTPDALEKVLQTLKKLPHRTLFCVFGCGGDRDRSKRPLMAEIAVSYSDVVIVTDDNPRTEDPDKIRQDIIEGVETERMALQPRTWLFERAGEAKGVVEIGDRARAIEDAVRAATSDDIVLIAGKGHEQYQIIGQEKSFFDDRLAACQASIGWDEQTISNALKLDYHAKPGATTFTEISTDTREIKQSAVFVALKGDNFNGHDFINLALDKGAACLIVSERPREDVRGTPVLSVPDTLRALGDLARWRRSALRQMTNPVVVGITGSCGKTTVKEMTASIMEQQWPERIDRPVHRVLKTQGNFNNLIGLPLTLLPASVTQRGVILEMGMNQFGEIERLTEIGDPDIACITNIASAHLEGLGNIEGVARAKGELFQGTGDRAIHVVNLDDSWVVKQAKSYTNQTIRFGISDQALAAKPDVWATETSLDSNGMVRFRLHVGGQNQFVRLNSPGMHNCINGCAAAAIGVAAGIDIETIVEGLQQFQPAPNRMAQLMTPAGLNLLNDTYNANPVSMSSAISTLAGLSARKRVAILGDMLELGETSNKLHHELGQIAAAAGLDLIAVTGNFSEHIRRGALDAGMNEHQVISFNEKQRVVDWVKELVHSGQLQSNDWILLKASRGLALDTVVEDLMQDC | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
Subcellular Location: Cytoplasm
Sequence Length: 1022
Sequence Mass (Da): 111961
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A0A1G0FDR0 | MKFNLLKGKKVWPIIFFLIFVLFFLDIFYFFFTPILSHRDTPVVYSLWPGTSYWKSANQLHSRGLLSRPSYWLALGFLEGNLKNLKAGDYQISPGVTTPHQLLSQMLVGKGVLYSVTIPEGWTFAQMKEAISKNPYLKHMENASTDILSRLNLIIKFKYPEGYFFPETYYFVRWTPEEKVYEKAYQTMEEKMNTAWLARAPDLPYNNQEEVLIVASLIEKETAQHDERPLVAGVILNRLKKRMYLQIDACVIYGLQDNYRGKLTKEDLKTETAYNLYLHKGLPPTPICLPSFDSIHAALHPIQTESLFYVSRGDGTHQFSKTLKEHQTAINKYLRHKT | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 338
Sequence Mass (Da): 39297
Location Topology: Single-pass membrane protein
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A0A1G0JYB2 | MKGNLAQREPDMLRRWQEMDLYGQLRRRRTGRPRFILHDGPPYANGEIHIGHAVNKILKDIIIKSRGLDGLDAPYVPGWDCHGLPIEHQVEKKLGKAGANRKAFRAACREYARGQISRQKADFQRLGVFGDWERPYLTMDFVTEANIIRALGRMIAAGHLVSGVKPVYWCIDCASALAEAEVEYQDRKSPAIDVCFAVVDRADAARRFGLPQPLPVTGDLSVAIWTTTPWTLPANQSVTLHPDFQYALVEYGRAGEPDWLIVAETLARQVLQRSGFEQYRVAARVSGRELEGMQLQHPFLSRQVPVTLGLHVTLDAGTGAVHTAPGHGLDDYHVGQSYGLETMNPVGDDGRFVAGTEFVSGMNVFAANATLLDVLRDRSMLLCEENVVHSYPHCWRHKTPIIFRATAQWFFSMDGHGLRANALRAIDEVKWTPDWGQQRIRGMVADRADWCISRQRTWGVPIAVFVHQETGALHPDTAGLIEKVALRVEQGGIDAWFDLEAAELLGADAAAYRKVMDILDVWFDSGVTHASVLEVDARLGFPADLYLEGSDQHRGWFQ | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
EC: 6.1.1.5
Catalytic Activity: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Sequence Length: 558
Sequence Mass (Da): 62389
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A0A1G0K2B7 | MKISEKWLREWVXXXLDTAALAEQLTLAGFEVETVQRCDSGLDGVVVGVVEQCEPLAGSDHLHVCKVDAGNGPVLQVVCGAPNVRRGERYPYAPPGVVLPGGRRIEPAVIRGVQSTGMLCSAVELGLGEGTVGLLVLDEGAAPGSDLVSVLALDDSVLEVAITPNRGDSMSIAGLARETGVLNRMQVAGPAITPVPAASTRCRAVQLAAPEACPRYVGRIIDDVDLTRLSPLWMRERLRRAGVRTINAAVDITNYVMLELGQPMHAFDDAKLHGDIVVRYAGVGERLTFLDEQERELAPDMLAITDARGIVAMAGVMGGLATSISTSTRSIFLESAFFVPAVIMGRARSMGMQTDAAQHFERGVDPDLPVRAMERATTLLLSCCGGQAGPTVDTCNRAALPQPQAVTLRHARVNRLIGVDVSAETITDILRRLGFETVVDAGSWQVTAPSFRFDVGIEADLIEEVARIHGYGQVPSRNLGGRVGMHQDGPDPRIRDWRRVLVERGYLEAITFSFTDAAYQDLVLGAGDALALRNPIASDLGVMRRGLLPGLLGAVTFNLKRQQTRIRLFETGRAFRMENGKITQPLLLAGVIFGNNYPEQWDIKNISSDFYDVKNDVESILAAAGISTGLRWRPQIGPGLHPGQHAEVFVQDQRVGYVSSVHPRVLQALDLPGPMLVFELDVEHIPARASAQLQLVSRFPSLRRDLAIVVDQDLPVYRVLDAAAAAAGEALTNLELFDVYQGEGIDLGKKSLAIGLIFQVTSSTLTDEAVDSVINSVLSALREEFGGRLRE | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 791
Sequence Mass (Da): 85326
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A0A7S0YSR4 | PRGIPCVFPVRAVFPKGPMVCVRTLCLLLVLAAAAGTLAFLPMAGPRIGAPSPYRHFSAKSEGTASSMRVSHRPLSLHMSVLEDMVARKQKVIEELKANPPPGVAERLEAMSEANKPKKTPIFKALKKPKGTITVMPQMKFKTPKLGKFCEPPEADILSGHYYEAGAAAIACSTDEELFGFTLKDLKIAKSVQDKKKGEFPSPLPVLAYDVMLDPIQLAEAAEAGAQGVFLNVAALGDRTKEMGEAAENLGLEWIAEVHSEEELQTAADAGCTIFGICNRNMETYDLLSPVDSVLRDWTTPIEETIFALGDKVPAGCLKVAMGNVNETLMAWKLRDAGYNCVMIGETLMRGSEMRMASGPYQSAYNEAKGLIKAFRSKGSVKYGPSSTASFYGKGEGAKETLGMLSM | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
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: 407
Sequence Mass (Da): 43860
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A0A429XSQ8 | MDTEILQIKNSIKKSLELLRGYLDLEVAKERLKKLSLEVEDPNLWSNQTRAKATLKEKTYLETNIEKIVTIEEDLKSYIEMIELAEIEGDEEIFKETLEQLKKLSESVKNQEIECLLSDELDENGCFLEIHSGAGGTESDDWASMLMRMYQRWIERHKFHYEIVDSLIGDEAGIKSVTLKIQGKNAFGWLKTERGVHRLVRISPFNSAGKRHTSFASVWVYPKIDNDVSVDINEADLRIDTYRSSGAGGQHVNTTDSAVRITHLPSKTVVQCQNNRSQHKNKEECMSMLKSKLYELELKKLEAKDDKKDSEKTQIGWGNQIRSYVLHPYKMVKDLRTQFQTSNTTAVLDGNIDQFIYEALITSTIGQGMKIKG | PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Subcellular Location: Cytoplasm
Sequence Length: 373
Sequence Mass (Da): 42744
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G4ST60 | MTELTRRQRQIFEFLRDNYERFAYPPTLDELCESLGMASRGSLHKHISALIDAGLIEPFAGSKQTGIRLTAQAQRDYAACEHALPYVGKIAAGKPIEALADVQYLPVPELLKSDKPCYVLQVKGDSMKEAGIFDGDWVVIEQRDYARNGEIVVALIDNHEATLKYIEQSPGKVLLIPANSAMTTQIYAPEQVQIQGILVGQMRSYRAH | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
EC: 3.4.21.88
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Length: 208
Sequence Mass (Da): 23206
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A0A9E0VTL1 | MDAFFASVTLLRYPQLKGLPVVIGGSKASVFGSQVDAESISSHAHLAGPETIPLDDFARLRDYRGRGVITTATYEARQFGVGSAMGLQRAASLCPQAILLPVDFAVVKDYSNRFKAAVRELAPIMEDRGIDEVFVDISEQALAAEDAGEAIAAELKQSIFDATGLTCSIGVAPNKLIAKMASEFNKPNGICLLRAEEVAERIGPLPCKRINGIGPKTAAKLAAMGYERIEQLRQAPLETLQLAFGERSGRWLFDVAQGHDERPVQTRSEPVSMSRETTFSRDLSAKEDRAELSQALAELCQRVAADLQRKGRVGRCISIKIRYADFRSVTRDQTITDSCDDAETIRYWARQCLKRVALDQRIRLLGVKVGQLSKADDVVRDVAPAQLSFLDLIDDSASIGSGLAQVFAPGAIYLPRAALANAAELWQETQRLLALTPTRHSMTKRGFYMASALTAVGSWGWVSDHKGYRYEAFNPETGLPWPAMPELFFQLAQRFAAEAGYSNFQPDSCVINDYVVGAGMGLHQDRDEADFQAPIVSISLGLPISFQFGGKARQDTPHRLLLSHGDVVVWGGESRLNFHGVLPLKAGYHQLLGARRINLTFRMAYAHINASM | 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: 612
Sequence Mass (Da): 67036
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A0A523A8K5 | MYRENRKQTTVFCPVFCLVGPTAVGKTALALDLANHYGAEIISVDSVQVYRHLDIGTAKASPEERRRIPHHLIDIVEPDDNYSLARFITAAAIALKDIQQRGRTALFTGGSGLYLRGLSAGIFELTDADPQLRGQLRRRLQQRLQNEGHDALHAELTRIDPESARRIHPHDLQRLLRALEIFYLSGTSWSEHLRRSRQTALLTTETPIIGLVVERDILYERINHRVENMLAQGLVDEVRGLLEQGYDPELSSMQSIGYRHMVAYLSGRYSLKEAKDLMARDTRRYAKRQLTWFRRMKHIHWYLPEETNKIKLLLEQKL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 318
Sequence Mass (Da): 36686
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A0A1G0FE84 | MNIVYIGLGSNLNSPLLQLQMALEKIKKIPQTFLKSISSFYLNPPLGDQKQADYVNAVIKVETQLDFEELFFHLMRVEEEQGRVRTQTCWQPRTLDLDLLLFNKVQIETEKIILPHPGLMMRSFVIYPLLEIEKDLILPQGIVLNSLRERVKNNLIPIFSPIFNFDETCDFRTPH | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
EC: 2.7.6.3
Sequence Length: 175
Sequence Mass (Da): 20401
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L0P8V6 | MSCFSRKTILIIGVLFHLIYLRSIFDIYFTSPLVHGMQQFKVESHTPAKRLFLIIGDGLRADKLFESHLNIETNTYETFAPFLHSIVLDKGCFGVSHTRVPTESRPGHVAIIAGWKTNPVNFDSIFNQSRHTWSFGSPDILPMFAYGASDVSRVETFMYEKKMEDFSKNSTILDTWVFDKVTELFKNSTSNKTIKKALSQDKIVFFLHLLGLDTAGHSYRPYSKEYLNNIKVVDTGLKKIVKL | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
EC: 2.-.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 243
Sequence Mass (Da): 27799
Location Topology: Multi-pass membrane protein
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A0A3D1AMU0 | MSSGKEIRFLVQRRRLRQKSSKRAGGIQSLAGWLGAVVFLILTVFGLWLGAYAITPLPMREGVNQHVLISPGTSLIGIEKLLIANGVIPPGRRFYYLARISGLSQRLQAGEYIFSPGQTPYQILCLLATGATVRWSVTIPEGTNIYQLADILAAGKWGERELFLKLMRDKELLSRYGVGAKSLEGYLFPDTYQLLRGQDPREIIGLMVERGRQVRQELGDLRNNSLGLSSHQVLTLASIVEKETAVPEERPLIARVFMNRLRLSMRLQTDPTVVYGLTNFNGNITRKDLETPTPYNTYLINGLPPGPIANPGRASIAAVLHPASASYLYFVSKNDGTHHFSHDLGEHNRAVLKYQKGGGKH | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 361
Sequence Mass (Da): 40060
Location Topology: Single-pass membrane protein
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A0A3L6SJI4 | MQRDTSSSDASASHTGRVRRRRQPSEATEDGNRANGQPLLVNDRNKYKSMLIRTYSTVWMIGGFVLIVYMGHLYIWAMVVVIQIYMARELFNLLRKSSEEKQLPGFRLLNWFLLPASLIVINDIFAYLFGFFLGRTPLIKLSPKKTWEGFIGASVTTIISAFLDLSTGWLYCDPGPMFKPEHYSLGEWVPHWFPWKELAIMPVQWHALALGLFASIIAPFGGFFASGFKRAFKIKDFGDSIPGHGGITDRMDCQMVMAVFAYIYHQSFIAPQNFSVEIILDQIIRNLTYEEQKYLYKQLGEIFHERQQMQS | Pathway: Lipid metabolism.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 311
Sequence Mass (Da): 35809
Location Topology: Multi-pass membrane protein
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G4T303 | MISTLTTSFRKNDARRLIVTGQVQGVGFRPFICRLAHELNLSGWVLNRAGTVEILIQGEPNRIDRFMERLIDNAPPLSKPTLASWQTAEPDDLDTFSILDSITESASAIHIPPDYYLCGDCLAEMSDPKQRRYRYPFINCTQCGPRYTLIKKLPYDRVNTAMSEFELCSDCRKEYENRLDRRFHAQPLACPLCGPSLTFHIAGEKTISDTGKALTACIEALRAGAIVAVKGVGGYHLICDASSEAIVQRLRERKQRARKPLAVLLPWRGPKGLTAVMEYAEPDPAELTLLQDPLRPIVLVEKRNSSPLAESVAPGITEIGIMLPYSPLHHLLSADFGGPLVATSANISGEPVMTDGDEVERRLSRVADAFLHHNRPILRPADDGVFRKIAGSMRPIRLGRGCAPLEMTLPFTLQEPVLAVGGHMKNAIALAWDDRAVISPHIGDLGSRRSQEVFEQTIDELATLYGISIRKVIRDAHPDYRSSRWAEQSGFPVTQVFHHHAHASALAGEYGLFETMLVFTWDGTGYGEDGTIWGGEALLGKPGEWRRAGSLKPFRIPGGDKVGREPWRSAAALFWECGREWQECPFPTELLKKAWQHELNAPLCSSAGRLFDAASALLGLVSTADYDGQAPMELEALSADGGPGPMLPLAQDENGIWRSDWTPLLAMLQNKKLSKQERAGQFHASLAETIRGQAIRIRTTHRIDRIGLCGGVFQNKRLTELAINYLKQEGFEVYLPERLPGNDAGISYGQIIEACPV | Pathway: Protein modification; [NiFe] hydrogenase maturation.
Function: Involved in the maturation of [NiFe] hydrogenases. Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide.
EC: 6.2.-.-
Catalytic Activity: ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE protein] + diphosphate + H(+) + phosphate
Sequence Length: 757
Sequence Mass (Da): 83706
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A0A424SHS3 | MMNIKIKKIDSLNRRMSLKIPWKDLESDFYVSMKQFSKKIKLPGFRAGKIPRKVLMSKFLTSIEADFIESSINKYYLNALKEKQIFPINKGSISDVKFKFENDLEFNVEFEIEPEIKLPKWKKNLLSVEKPRYVSDEEDVKMALEEAQRNNAEIKSIDDGSKKDDFIIXDLQEVDSSGIPIIGKKLETRYVRIGQPPFDGNNQKKLTGLKQNDKVVIDVPINESGDLGRYELXVKNVERQILPKIDNKLVKXVDPESKNLSDYKKRIKVRIDESYQKKSDEIFENNIIDALVKKIDPICPPSMVDSYLSNILEDLEKNGNNQLDPEKAKQTYKPIAEKNIKWYLIRNSLLKEQGFKIESKELESEIKKLKSQNKSQASDVEKHFQKNENKKRLQDSMLEKKIIDFLLKYLKAKDVKILTKDLRNNVTQRVQNG | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 433
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 50443
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A0A7Y5HB13 | LHLDPALIPWPTARVDVRSAVSVAAAFEADRPGVVINCAAWTDVDAAESRPDEAFAVNAAGAAHLAEACDRHGARMLQVSTDYVFDGSKSSPWTEQDPVGPLGVYGASKLEGERAVAAHCRDHAIVRTAWLYGPWSRRSFVDTMLRLTAERPSVDAVADVTGSPTLTFDLARALLFLARHTFRGTLHAANTGVTSWHGIAAEIVRLTARTCEVRPVPQTAFPRPARRPANSALDSSRLREIGHPMRPWGEALADHVGRQSRR | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 262
Sequence Mass (Da): 28409
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A0A2H6JTF7 | MSGEKLRKQIKKRAFEQGEFILASGRKSNYYINIKNAYTEPEVLRNIAKYIAEKLSEIEYDLIAGVAVGAVPIVTAVALEVNKPFLIVRKERKNYGTGMNIEGKFSKGERVVVLEDVTTTGGSVIKAIKELREKGLECSTAIAVVDREEGAGENLKKEEVELISLMEVSELMR | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Length: 173
Sequence Mass (Da): 19239
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A0A517PDC2 | MAKRNKQSASSGRKTPAPKASAGGSSPGGLLNRRAARLADFVLKRLDELGVDLLRLSTGTTVLDFGAQAAGGLEAGRVLARLSAADLLDVTVDPGTLAGRPWPTVNVRTDDPVSACLRCQYAGRKVQLAEPGGGEYFAMASGPLRVAAGGEELIAKLGGVEEARRVVGVLETRRIPPPNVVAHLADSCSVAPDKLVLCMAPTASLAGTVQIAARSVETALHKLDALGFDVTRVRSGVGSAPLAPAGGDDVAALGRTNDSILYGSRVVLWIDAEGQELAGLVNKVPSESSAQHGRPFAELLSEAGGNFYDLDPHLFSPAQITLISLRDGAAVSAGSVREDLLERSFFGENR | Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 3/5.
Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
EC: 3.5.4.27
Subcellular Location: Cytoplasm
Sequence Length: 350
Sequence Mass (Da): 36305
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A0A136JLP0 | MSETGALYRKYRPQNFSEVKDQEHIVTVLKGIINKDNIPHALLFSGTRGTGKTTLARIFAKEIGTSSIDLYEIDAASNRGIDDVRELKEAVHTVPYESKFKVYIIDEVHMLTKEAFNALLKTLEEPPAHVVFILATTEEEKLLDTILSRCMVFRFRSPSRAVLSEIVTEVAGKEGFKLSPESADLIAIAADGSFRDALGVTQKVIMALGEKLGEADEVAMIIGAPKRAIILALLKAFHTKNVELGLSVINQAVNEHVDIKLLLRLLLEHVRTIMLLRNLSNNQDVILEAYNPDMQSELKAITKESSTPLNSHLLLKLIATVEQTNRSPLPALPLEIVMVEHCESK | 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: 345
Sequence Mass (Da): 38298
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A0A2N6C4Z6 | MRGILHEVLPLFPSTPAQSLVSADSATLTTRKFIIRGMVQGVGFRPHLYRLARIHALGGRVANSLAGVELILAGSRAAMDQLIEELLHTPPPGALIASIEEEEIADRVYEGFTIAASLAAGTGTSLAPADFGMCATCEKELLDPANPRHRHPFISCTACGPRFSLLHGLPYDRAQTSMAPFPLCPLCRQEYTDPDSRRFHAEPICCPDCGPQLTLHHQKKNQTDKNGDRAAAILARGGLVAIKGVGGFHVAVDAADHKAVARLRRLKQRPDKPLAVMVRDLAGASTLAHMEPRAEALLTSPVRPIVIMPRKATAPLAALIAPGMTEIGIMLAYTPLHFLLFEQGPAALVMTSLNEPGSPMLTSSTAAVARFGHSCDAVLSHNRTIVSRCDDSVLRMHDEQAIPIRRSRGYAPLPLALPVSGPAILACGAGEKVTICLSRGANAFLSQHLGETASPAGRQGYTEACRHLQGLFKITPQVVAHDLHPDYFSSRFAADQTGCTRIGVQHHHAHIAACMAENNVRHAVLGLALDGTGLGDDNTLWGGEILHCTYRGYRRLAHLAPLAMPGGEAAIKEPWRLALAWLHEQGHDRHGFTFLRDIAEADQETLLHMVDGRLNTPLTSSLGRLFDAVAALINLRRRITFSGQAAMELEMISARDEEGHYPVRMTATAAGQPHVMETDQILAGLCGDIRAGVEQPVLAARFHNSVLRLLCDTVLRLAAEEEISEVACSGGVFQNRLISRGIQKNLGAAGLRVHIHQQVPCNDGGLALGQAAVAAALSGREDPHRQ | Pathway: Protein modification; [NiFe] hydrogenase maturation.
EC: 6.2.-.-
Catalytic Activity: ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE protein] + diphosphate + H(+) + phosphate
Sequence Length: 786
Sequence Mass (Da): 84474
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A0A286Y138 | MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDDILSDVASRLWFTYRRNFPAIDWRWAQRKRQPDSYFSVLNAFLDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKK | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine
EC: 3.4.22.-
Subcellular Location: Cytoplasm
Sequence Length: 121
Sequence Mass (Da): 14259
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A0A286XLF3 | CHTRAKDLLRQASFLKGRALWILGHHIVPRDQCHQLPEGAPQARGGGAVGSAVVNERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEILYSAHFLEWFSEEARRVYGDIISTPTKERRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAQLANQAGIPAGVYNVVPCSRAKASEVGEVLCTDPLVSKISFTGSTVTGKVLLRHAASTVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNAGQTCVCANRFLVQRGIHDSFVKKFAEAIHNSLHIGNGFEEGTTQGPLINEKAVEKVEKHVSDAVSKGATVVTGGKRHSYGRNFFEPTLLSNVTVDMLCSHEETFGPLAPVIKFDTEEEAIAIANATDVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLEIKYVCYGGL | Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
Function: Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).
Catalytic Activity: H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate
EC: 1.2.1.24
Subcellular Location: Mitochondrion
Sequence Length: 472
Sequence Mass (Da): 50718
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A0A136JL21 | MAKLVPENNPVLHIIADEITSEEFTNGTVKKIISDLRQAIKTYKVDGFTAVAIAAPQIGVGKRIFMIEDQSDEADRLPTIIAINPRFLKMSKKTHLVGEGCLSIPDRYGLVRRSTNVTIEATDENGKTFTRGAGGLLAQIMQHEYDHLDGILFTDRAEKVWIKKDGENIEITEDNNI | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 177
Sequence Mass (Da): 19709
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A0A433VR23 | MYASELTKYPVKGSDSIVPTDPFIYRFYEIMQVYGLPLKDVVQEKFGDGIMSAIDFTLNVEKEEDPKGDRVRITMSGKFLPYKKW | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
EC: 4.2.1.104
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Length: 85
Sequence Mass (Da): 9862
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A0A834H759 | MIYSVFPYIAWYCASLHIHVPCVIVRERERERERERERDSLEEAGMAVGITKGSEVAAGEYNGRVTSFVVLSCMMAAMGGAIFGYDIGISGGVTSMEPFLKKFFPNVYLRMEEDNKISNYCKFNSELLTSFTSSLYVAGLIASFFASSVTKAFGRKPSILIGGAAFLSGAALNGAASNVYMLIFGRALLGVGVGFANQSVPLYLSEMAPPRYRGAINTGFQLSVGIGILSANLINYGTQKIKGGWGWRISLAMAAVPASILTVGALFLPETPNSLIQRNNNHLKAKSMLQRIRGTQDVQSELDDLIRACEISRSVKHPFRKIIQKKYRPQLVMAIAIPFFQQVTGINVIAFYAPVVFRTMGIGESASLMSAVVTGVVGVAATILSMSIVDKLGRRVLLMVGGIQMLVSQVMVGGILSAQLGDQGEVSKGCAVSVLILICVYVAAFSWSWGPLGWLIPSEIFPLEIRSAGQSINVAVNFFFTFVVAQTFLAMLCHLKSGIYFFFGGWVAVMTVFVYLFLPETKNVPMEKMDGVWREHWFWKRIVGEEHAVNNMEGEDSDGDSG | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 562
Sequence Mass (Da): 61396
Location Topology: Multi-pass membrane protein
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U5LGK2 | MFKKMAQKLKNEKGLTLIELLAVIVILGIIAAIAIPSIGGLINKTKNDAKVAEAIQIVNASKTYIATNPTATSLAFADLDSYLDNVKDQEFTVKVDRNTTTGKFTYKIQNHEAAKIVKKNNEATEVTEVELQAFSGN | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 14913
Location Topology: Single-pass membrane protein
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A0A0G1D5I0 | MQSQNKKSLFAQNEEEVLRMWAEKNIFQKTLEKKSPKGNFVFFEGPPTANGRPGIHHILARSFKDIILRFRTMQGYHVERKAGWDTHGLPVELQVEKELGISGKPEIEKYGVEEFNQKCQESVWKYQDEWEKLTRRIGFWLDLEHPYVTYRNDYIESLWWIFKEIDKRGLVYKGYKVVPQCPRCGTALSSHEVAQGYKNVEDTSVYVKFKVKEQDKTFILSWTTTPWTLPGNVGLAVGSEIVYVKVKHNDEFYILAKTLVEQVLDASTEIVEEFKGQDLEGLEYEPLFPGVLDPQGKKAWFVGTGDFVSTVDGTGIVHTAVMYGEDDFNFGEKYNLPFVHTVDENGHFLPMVKNWAGQFVKNPEVEKGIIEDLKSRGLFLAEEKYAHDYPFCWRCDSPLLYYAKDSWFIKISAVQKDLLKNNEKINWVPDYIKEGRFGEWLSNIRDWAISRQRYWGTPLPIWICEKCDQKEIIGSLEELQKRAGALPKNKDGEVDLHRPFIDNLKFVCSCGGEMKRISDVFDCWYDSGAMPFAQYHYPFENKNLIDKGEQFPADFISEAIDQTRGWFYTLLAVSTLLGQGAPYKNVICLGHIRDKEGKKMSKSKGNVVDPWMIADKFGVDALRMYLFSLNQPGEPKNFDEKEVEEILRKVIMLLGNVMNFYEMYKKDTAQKYVGSPHLLDKWIIAKFFVLIKDMNRDLDCYHVFEASRRLIDFINELSTWYVRRSRERLKGEGEDKENCAATLRFVLENLVKLLAPFMPFVSERFYARLDGKEESVHLDDWPLAQEEKINWEILKEMELARKIVELGLSARAEKTLKVRQPLSAMCIANFQLNEELIKIISEELNIKEVRVVKDFSDLQGENWLIKIEGTLSIALNIKIDEQLKAEGMIREIVRALNQLRKNAGLTIKDQVVMTVETADGELQKVIKDSVDILSAQVLAKEIILGKVGEKGFQGEVEGKEIKVNFS | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
Catalytic Activity: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
EC: 6.1.1.5
Subcellular Location: Cytoplasm
Sequence Length: 966
Domain: IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).
Sequence Mass (Da): 111688
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A0A358C5I9 | MRRILQIVHAARSVFTPSRDAGQEHAAFLHAIYDSAPDGITLTDMQGRFVRTNPAFQRMTGFSEAELRAETCESLTHPEDFPRYRVLLEELLAGQRAAFRLVMRHRTKTGAAAWVRCTVSQLKENPDTPRYIVARTEDVTESWQQREQLLERTEPFHLLVASVTDYAIFILDPEGRVTSWNVGAERIKGYLADEIIGQHFSRFYPREDVEQDKPAHELQAALAQGRFEDEGWRLRKDGSTFWANVIITPMRDESGTLRGFAKVTRDLTVRRQLEERLRESEARLQAFLNHSPAVIFLKDVEGRYLHVNTKFLQCFGLCSEQVIGRSDAELFAPDQAAEFSANDHAVLASGTPLEFEESAQYDQGPSISMVSKFPVSDTSGRIIGIGGIATDMTEYKHAQEALRVSEQGFRELVDILPIAVYTCDASGLIEGYNRQTTELWGRAPRLGDVDDRFCSAYRLYRSDGVYMPHPECPMAEVLRTGRAVMDREIIIERPDGSRRAAVVNIIPRRDEHGTLTGAINCLMDITERKHAEHDLKMYADQLRVLSNRMVELHEEGRLALSRELHDRVGQNLSALNINLSIVLSQLPEAARCLVGARLKDSQGLVEATVDVITDVMADLRPPLLDDYGLLPALKSIAELFSRRTGIAVGVRGPAHLEGLPKQVEISLCRIAQEALTNLAKHAHAENVKIEITLPPDQITLTISDDGIGFDPSMQPLHSGRTGWGMLTMRERAVALGGTLAIDSEPGLGTRVTVTLTRKP | 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: 759
Sequence Mass (Da): 84872
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E4TJX0 | MCYLFFLIGAIFGSFMNVLIYRLPRGISIITPKSNCPNCKQEIRCYDNIPLISYILLKGRCRGCGVRIPIRYFIVELVTSLVFFLLCIKYGLSLNSLALLIFSFFILTAGFTDLYTAFEKDQFECGVIPSVILYAGIILGLILSFFNGFGIVNSILGGVIGFISLFIPAIVYKILKGREGMGDGDMYLMAMSGTFLGVKAILPILILSSFVGAVIGIVIIKVLKDNSFPIPFGPFIALGSIVYLFYGEELINLYIGLLR | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
EC: 2.1.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 259
Sequence Mass (Da): 28612
Location Topology: Multi-pass membrane protein
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A0A7W0IRE1 | MNLILIQTDELDDRQVHLKDRRAEHLRKILKVKVGDTVRVGIVNGLMGTGTVADISRHTVILTIEASTPPPVRLELDLILALPRPIMLKRVLAQIAALGVNHLFLINANRVEKSFFEASPTKYGDFAPFLHNGLEQAIDTIAPTVSIHHRFKPFIEDILPTVTASRKIIAHPDGITSIADNFCSTPPGKTLLAIGPEGGWIDHELSLFHDARFLPFSLGPRILRVDTAVPAIIAQIALLQQRATQGVAE | 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: 249
Sequence Mass (Da): 27359
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A0A7X6TIN8 | MTDQQPGGKDSFVLLGTVTRAHGLRGEVKVRPLTESPASFARYQHLYLSTAGDGEKVPHTALQARVSGQSVVLRLSGCTTREAAEQLAGSKVWLATSDLPPPGEGEFYLHTLEGKRAETIDGRQLGRVAAILSGGGQDILVIRTNEAEVLVPAVRAFIRAVEDDRVVLDPPPGLLELNQ | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 179
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 19174
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A0A849WLT9 | MLKLSLSELIQITGGKTGNSPIFCKDIQGLSTDSRNILPGQCFLAIKGEKYDGHNFILDAIQKDASAIIANESYPVASGIPIPVIQVPQTLDALEKIALHHYKQFPLLCIAITGSVGKTTTKHLACSILSNRFGVLKSPKSFNNSLGVSLTLLELESIHKVLVMELGANAPGEIAHLTKMIKPDIGLITCVAPCHLEGFHSLSGVEQAKSEILLGMGEESVFITNADDCACQRILSKFPGKTVTFSLEKTSDFHAQNIRKEKDGIAFKMNGEEYFSPLPGLHNLYNLLASMAIATQAGMTPEEIKDSLSSLQLPAMRMEVKQSGGITVINDAYNANPKSMTAALEYLEQFPSTRKIAVLGSMLELGKESHHYHALIGKEAAAKNLDFLFAIGKEAKDIAIGAKESGMPEDKIFFYDDNINIEKELLPLLKQGDVVLLKASRRIKLEELVSKIIC | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 454
Sequence Mass (Da): 49393
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B0DGX4 | MLRLGALASSLLFILSPVLAGVITSPTGVNGQTYDYIVVGGGLAGLTVAGRLAENPKITVLVIETGADNRQDPRVYDLYNYGQAFGSEIMTSWPADQGKLILGGKTLGGGSSINGGAYTRGLAAQYDAWSTLLEPSEASVGWNWQGIWNYMKKSETFSAPNSQQAAKGAQSLPDYHGYTGPVQITYPDAMYGGPQQSAFVNTIVGLTGINHYKDLNGGTPNCVSITPFMMNWHDGDHRSSSATAYLSPVETQRTNWITLTNHFVTKINWSNSVLPLRAVGVQFAPAAGSSTRYTALARKEVILAAGAIQTPALLQLSGIGDSAVLAPLGITTLIDLKTVGKNLQEQAMTTHGARSNGFDVGGRGPSDAIAYPNLYQVMGSQASATVTHIQQSIPSWAASQAGSGLSAAALQQIFQVQANLIINNNAPVMELFYDTGYPDTLGILAWNLLPFSRGTVQITSTNPFTKPQVKVNYYSVDVDLNIQVAGARLARKILTTPPLSSLSTGESRPAGAVPDGPDRGSDQAWKSWIQQGNFDSVAHPVGTAAMMRRSLGGVVDAQLRVYDTANVRVVDASVLPMQVSAHLSATLYGVAEKAADLIKAANP | Function: Catalyzes the single-oxidation or sequential double oxidation reaction of carbohydrates primarily at carbon-2 and/or carbon-3 with the concomitant reduction of the flavin. The enzyme exhibits a broad sugar substrate specificity, oxidizing different aldopyranoses to the corresponding C-1, C-2, C-3 or C-1,2, C-2,3 and C-3,4 (di)dehydro sugars with substrate-specific regioselectivity. Accepts only a narrow range of electron acceptors such as substituted benzoquinones and complexed metal ions and reacts extremely slowly with O(2) as acceptor. May play a role in the natural recycling of plant matter by oxidizing all major monosaccharides in lignocellulose and by reducing quinone compounds or reactive radical species generated during lignin depolymerization.
Catalytic Activity: a pyranoside + acceptor = a pyranosid-3,4-diulose + reduced acceptor.
EC: 1.1.99.29
Subcellular Location: Secreted
Sequence Length: 603
Sequence Mass (Da): 63793
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C8C1A6 | MDPVDPNLEPWNHPGSQPSTACNSCYCKQCCFHCQFCFTKKGLGISYGRKKRGQRRGPPQGGQTHQVPVPKQPSTGTSREQKHQEEQEKEVEKKTGPD | PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1.
Function: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF.
Subcellular Location: Host nucleus
Sequence Length: 98
Domain: The Arg-rich RNA-binding region binds the TAR RNA. This region also mediates the nuclear localization through direct binding to KPNB1 and is involved in Tat's transfer across cell membranes (protein transduction). The same region is required for the interaction with EP300, PCAF, EIF2AK2 and KDR.
Sequence Mass (Da): 11012
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A0A7Y5LUW2 | MASILPSTRRWFGTGLPYVPLDDCAGKLIVVEGTDGVGRSTQTALLREWLQIQGFSVVETGWTRSKLLGPLITEAKQGHSLNRLTFALMYAADFADRLENEIIPALRAGSIVLSDRYIYTAFARDTVRGVSPDYVRKLFGFALVPDLTFYLKIDIETLVPRVLRARRLNYWEAGVDLGLGWDLYDCFVKYQTRLLATYDDMEREFGFATLDARQPPDQIQKAMRREIEKRLFATRKRSHERDGRAGGDAAEGAGAAGAAAGDGAAPIA | 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: 268
Sequence Mass (Da): 29755
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A0A0D0CCX2 | MPSTPGTPSGKVAPVAALSETQTIVQDEPETIFLAAQRGDLPLLQSLLAQGALTTDRDSQNITALHWAAINAHLHICRELLERGAEVDARGGDLDATPLQWAARNGYLYVVKLFLEWGADPTLKDGQGYNTLHLITHSSAVMPLLYLLQQRKVDVDSADLQGHTALMWAAYQGDAVSVDILLKHGADVGTKDEGGLTPLHWAVVRGNKTVIKKLLESGADVSAKDSGGRTPRDMAVELKSIGPWKRAMEEGGWDEYGVPRSPLFSDPKYTSLAIFILPTPLLVLVFNTIAVSWLPWYTSLILAAAECFAAAHILTRVLLGRKPQAESPFFAGIIFASLLIVVWCYATILTNVHDHPSAHLVFIVSASLCLYNFWRAVCLDPGFVPNRLLNDVEDLASEGRLNGQTFCVSCMARKPLRSKHCRICNKCTARHDHHCPWIWNCVGSNNHRQFVLFLLNLVIGIISFLYLTYQYFSVVPESEPSVTCPLPDPMCRILGAKSNIFLLTTALWSALQLTWTIILLGAQLWQISRQMTSFEVSNVGRFGFMGGRGVIGVGQMGAQQHSHGSPLSASESLDAASGGPHSHSHNHPQSLRGSGGLLTLPCKICSLCASCPGASFVLRITGLDRFSARGGAARGLASSTAPQNPFDLGPYLNCMDFWGMGKEVGVRWETCYDIPDEGFKKAREMRLQEDRERGERGEMDPSGGRKGRRFWPGVRRVLSMRMGRPSSYEYEPLAQV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 736
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 80729
Location Topology: Multi-pass membrane protein
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A0A0D0D4D0 | MPYSHHSHSGQFCKHANGTLKDVVLEAIRKGFRVYSLSEHVPRYRTEDLDGARALGAQFDAFLDEAHRLKVHYASQIILLVGLETDYITSIDLDRFDALLERHGDRIEYIVGSIHHVGGILIDFDIDTFNRALAHQPGGSVDEQMEAFLCSYFEAQFELMQRYRPEIIGHVDLCRLYNPQLRFAEYPPAWELLNGTYLVATEENSFPEPFFHIGTLLKKIIQKAYG | 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: 226
Sequence Mass (Da): 25929
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A0A554K362 | MTGNLRRGKFIVFEGIDGAGKATQTKLLLTYLQKRRQPVEKLAYPDKKGEVGKLIYKYLHLQYGLSSQTQFLLHLADFAKDREKIRSWLRKNKTVVADRYFTSALAYQGAQGFSFNKALLLAKTFELVSPDLVIFLKISPKTSLKRKHKEKKLLDRNEKDKKFLAKVAKFYEKMIKNQTFARWLLVEGEAPKKEVFAAIKKELKL | 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: 205
Sequence Mass (Da): 23760
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A0A286X7B8 | MEHEFTPLEPLLPAGNLRYCLVILNQPLDQCYRHLWNKALLRACADGGANRLYDITEEERESFLPEFISGDFDSIRPEVKEYYTVKGCELILTPDQDHTDFTKCLQVLQKKIEKKGLQVDVIVTLGGLSGRFDQIMASVNTLYQAVHIIPVPTIIMQEESLVYLLQPGKHKLHVNTGLEGDWCGLVPVGQPCNQVTTTGLKWNLTNSMLGFGVLVSTSNTYDGSGVVTVETDCPLLWTMAIKV | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.2
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Length: 243
Sequence Mass (Da): 27155
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A0A3R9XKZ0 | MKLQRIRGTADLYDKDIDRFNHVVSYAKQFAELYCFDEIATPIMENSEVFHRTLGETSDIVNKETYHFLDRDKTNITLRPEFTAAIVRSIISNGMLQSLPLRLFSYGPLFRHERPQKCRLRQFHQINFEYIGSNSLKVDVELINLAYDILNSLKILDKIKLKINTLGNFDCRNKYKEALKSYLLKYRNDLSDISLIRLEKNPLRILDTKNEKERMLLDDAPNLYNFIDNNSKSTFEKIMLNLQDLDIEFEHEKRLVRGMDYYSGFVFEFMTEDLGSQGTVIAGGRYDSLISTMGGKETPASGFAGGIERLMELLSISSNELQDKKPLYLIPIGEFAESKSLKISDDFRSENIITLVDYEISLKKRMQKANKLNVDFAIIYGDNELQNKTFILKNLNSGVEEAMNKEQLLNYIKKSIK | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 417
Sequence Mass (Da): 48345
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A0A924K6L4 | KGDCSSGDGMSTGGHFNPSASPHGQHGAGPHHSGDLPSLKADANGVATINFMSSMLTVGSGATDIVGKGLIVHRDPDDFKTQPTGNSGLRLACAVIAAR | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 99
Sequence Mass (Da): 9895
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A0A484GC86 | MIDYQDKKVVIIGLGVTGLSCVDYFLSKNVIPRVIDTRQQPPALEHLDQRVVFHRGDLRVDWLLEADLIVVSPGIALSTPELKLAAENGIEIIGDIELFCREINQLKDKKVVAITGSNGKTTVTTLVGEMAKATGKSVAVGGNIGEPVLTLLSNDYDIYILELSSFQLETTFSLHATVATILNITEDHMDRYPEGITQYMQAKQRIYHHAQVCLFNADDPLTRPKAGYCDSCRQFGIAQGEYRLDSHAQSLVIDGDAVLDTTQMNLFGLHNYMNALVALAIADQLAITREISLTVLKQFKGLAHRFELVHEKHGIRWINDSKATNVGSTEAALRSIKCTGRIHLLLGGDGKQADFSPLKPYLQNNITIYAFGRDRQLLAQLNPDSTTQFETMAQAMNQIIVNLHAGDIVLLSPACASLDQFKNYMERGKLFAMLAKELGA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 440
Sequence Mass (Da): 48628
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A0A091C2N9 | MLNQLVLSVADVQNTTISNIVVVTGSFVLLLALLKKFAWNAIADMMNKREKKIANDLDSAEQSRTQAKELEQTRQEQLQSSKSEASDIIKNAKSSGETSRQQIISDAQEEVSQMKENAQEDISNERQAALSSVKGEVGDLSVQIAEKIINQELSKEAHEALINQSIESIGSEDETR | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 176
Sequence Mass (Da): 19418
Location Topology: Single-pass membrane protein
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A0A834FWY5 | MAQVISPLMDFILNTEFIMLMVGLCSILSTDPGFVMTESSHLNNFVERPVSVFEAHSKELVPSTCDMPYEFSAEETAIPLQRVRHCGHCKAYVKGFDHHCPAFGNCIGQKNCVLFIILLAGFVFTEASWISDTAKVKILDKTGHLASLYINLAISTMIFSLLQLLWQGVFLAWHIYCVCFNIRTDEWRAYKKLGYCIASTVDGSSQINWKRYPEFHLIVHPETGQTPSGSETRFTNPYNKGILSNVKEFLTAVE | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 254
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 28661
Location Topology: Multi-pass membrane protein
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B0CVK5 | MHLLATYSLTSLAFSSLIVCVACDPGPANLIPSQQGANTDADDEISLTDALMPNEDYTAPGRWCRKCWAPKPERTHHCSICGRCVLKMDHHCPWLGSTCIGHRTYPAFVHFLCSVTLLATYIAIISISALLDAFHNPFLVHEFTPVHELRLAFAGIVFSLVIGSFACYHLYLISYPHLCCCAIFLHYRRLVIHSPIHRFSPN | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 202
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 22584
Location Topology: Multi-pass membrane protein
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A0A6N9DWQ7 | MNSGFQRWGILLGVGLVIVVLDQITKTLVMHTMHLHESIPVIAGFFNLTYIRNPGAAFGMFATTNSAFRLIFFVGTSIFAMGLLGMIFYRMHPADVWGRLSVAGIFGGAIGNLLDRLQYGEVVDFLDFYMGGYHWPAFNVADSAISVGVVSLLILFAMDNKGETPAPIEPTEEGTSNDKGKRTSHDL | 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: 187
Sequence Mass (Da): 20452
Location Topology: Multi-pass membrane protein
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L0P9C2 | MDSINDTFYHKDQRLLQKQRVKHMGRSWNTEVICLNTSNELDLTRNLEKKNENYCVNTEKLPVVEKTMKENEIHELLNELSLKPARKKMSDYKFWNTQPVCSFDEEISEEGPIDDSKDLEKVRKEPYPLLKEFEWVTLDVDDEEDLKNLYQLLAKNYVEDDDSMFRFDYSEAIKPPGFHKNWHIGVRVAASKKLVAFVSGIPISLRVKDRVIKCSEINFLCIHKKLRSKRLTPILIKEITRRCNLSGTWQAIYTAGVILPSPISSCQYYHRSLNWQKLYTVGFSPLPKNSTIARQIQKFKLPNETSTPGLRPITVHDLEQVSELLRSFLKKFELSQIFSNDEVKHWLIPRENQNDEEATIFSYVIEVRSFGNILI | Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
EC: 2.3.1.97
Catalytic Activity: N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]
Sequence Length: 375
Sequence Mass (Da): 43947
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A0A842HF33 | MASPTEIRKGRVLTYQDAPHLVLDMQHRTQGRQAGFVQVTLRNLNTGSSTNVKFRSTDSVEFCHTSTAKLEYSYIDDLGYHFLDPETFEDSVLPSEICDEIAKFLIETKVYDVLLVDDKPVEVNLPAAVEMKVVDAPEGVKGDTASNVQKPVITETGLSVQVPLFIKKDEVIRVSTETGDYLGRA | Pathway: Protein biosynthesis; polypeptide chain elongation.
Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Subcellular Location: Cytoplasm
Sequence Length: 185
Sequence Mass (Da): 20551
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A0A849WHQ3 | MRAIKDYYEVLGINKESSEAQIKTAYRDLAKKYHPDKNPGNKEAEKKFKEITEAYEVLSNEQKRKQYDQFRDGGFRGFGAGNPFDGGSMGGSAFGFENMDLSELFNSFFSGGESMFGSTTREPRSRAVKGEDMYVKLDVPFDVAAKGGKSTITLNKDSSCDSCNGSGIKAGGQKKRCSYCDGTGQIQNQKGTFSFQRNCPRCMGQGVLIDSPCSVCHGNGFCKTKRKLSVSIPSGIESGQKIKLSGEGHLGSNGGSSGDLYIEVNVLSDSPFTRDGINILSEYTIDLKEAMLGSKAIIHTLQGDVELKIPAGIQPGTVLRIPEQGIAQGKRKGDHLVKIQVHIPGKLTRKQKELLEEFSSLGLD | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Subcellular Location: Cytoplasm
Sequence Length: 364
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Sequence Mass (Da): 39588
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A0A0Q4KNY3 | MTLTLYNSLTRQTEAFTPIHAGEARVYTCGPTVYNYQHIGNMRAFLFADTLGRVLKWNGYALTHIINITDVGHLTSDADAGEDKMEKAALAKGASIWDIAAHYTHAFKRDIRRLNITDPAEWTVATDYVPQMIDFAKRIEKDCYTIDGGLYFDVSKVPNYGSLARATTEDGESRIEPVDGKRNPQDFAIWRTSPPDEQRQMEWDSPWGKGAPGWHLECSVMSHATLGHPFDIHTGGIDHREIHHPNEIAQNQAHCDCSDPGARIWMHNNFLIDRGGKMSKSTGQFLTLQVLVDAGFHPLAYRMLCLQAHYRSELEFSWDNLAAASTRLKRLVQTVERLRDRFASEPRGTLETPEVDEAKAAVSDDLNTARALVLLESVAGGKGHAGDRFTAVRKIDRVLGLRLAMITRDELRIRPAHATLEEDAIEARLVERREARAAKDFARSDAIRDELTAAGVEVMDGDPLGWDWKVVLP | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 473
Sequence Mass (Da): 53042
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R7M174 | MQNIVQKIDKNSKIAVLCGGMSSEAEVSRRSGKGVFDALQRLGYTNSELVEVDKNIAQKLKDGNYDYAYNVLHGKYGEDGCIQGILEILQIPYTGCGVMSSAVCMNKEFTKRMLSSCSEIPLAKSAFVRKGEDVMEKTKDLKYPVFTKPVSEGSSFGMTKVNSREELKTAYDEAIKYNDDVLIEEFIDGLFVTVGVLEQDGKNFATEILEIIPKNEWYDYESKYTPGMSEFILPAKFDAELTAKIKEIAIKSHETAGCKGVSRVDFMVSKDGIPYVIEINTSPGMTTTSDLPAQAKVMGISYDNLVQIVLNGAGLNK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 317
Sequence Mass (Da): 34987
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G7VYQ4 | MDALAPSSGPLPSPETSKPVGRGGYIRDWLVTLLIAMTVLLLLNLFVFNLSTVRGHSMQPTLMESQHLFVNKLIYNFHDPGRGDIVILQDPDSKPSSPRFLVKRVIGTPGDVIRVEHNHLYVNGELQNEPYTDSEIEDGDYGPFTVEPGHFFVMGDNRHAAGSKDSRYFGSIKSQDLLGRAELVFWPLSEWKWL | 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: 194
Sequence Mass (Da): 21793
Location Topology: Single-pass type II membrane protein
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A0A417TTM2 | MVGKIRILLADSDGDFCAEMAALCEDAEDMELVGIAESGEKALTAVGELRPDLLITELSLPGMDGVLLLEQLRAAGNMPAVFVLSAFSSTQVCAECASLGVDVFLRKPIAAEKVCERIRLWRSGRKRMAREENAVALEVRVTEVIHQVGVPAHIKGYQYLREAIMMAVEDIESVSAITKVLYPSIAKKFHTTSSRVERAIRHAIEVAWDRGDLETLQSYFGYTVSGVKGKPTNSEFISMIADRLRLQMRFGA | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
Subcellular Location: Cytoplasm
Sequence Length: 252
Sequence Mass (Da): 27721
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A0A7Y5HAA1 | MSRLSELLRTLGKPRILVVGDLLLDRYLWGKVDRISPEAPVPVLNIVREEERAGGAANVACNLVALGASASLAGAIGPGAPGERLVGLLREAGIDTRGIVVDPGRPTPIKTRCIAQSQQMLRVDRELAAPLAKAAEKKLLRHLQQAVAKVDLVLLSDYNKGVLTDAILAAIMRAAKKHGKPVVVGPKGLSYDKYAGCTGVVPNLKELALATGLAVGTDAGVRAAASALLRDLGCGFVLVTRGDRGMSLFREGSDPFHVPSRPRQVYDVAGAGDTSVATLGLALACGAAAEDAVRLANAAGGIAVTKVGVATVSRAEIQADLEEEHSTRPEKVRTATELVPVLAAARARGETVAFTNGCFDILHAGHVRTLHFARSQGDLLVVGINSDASVRRLKGAQRPIVPERERAAVLAALQDVDHVVIFGEDTPVELMALLKPDVIVKGGDYTADKVVGAAAVKAWGGRVAMAPLQKGASTTNIVEKIRRLK | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-D-glycero-beta-D-manno-heptose + diphosphate
Sequence Length: 485
Sequence Mass (Da): 50793
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R7BUU4 | MINIAIDGPAGAGKSTIAKAVAKDLGIIYLDTGAMYRATAYLALQKGIDVKDEEKVAEMLEDLTMDIKYDENGAQRIIVNGIDATPYLREHYMSKAASDISALPCVRYKMVDLQRDFASKNDVVLDGRDIGTFVLPNANCKFFLTATPQERAERRMKDLQEKGETVDFDQLLQDIIQRDYNDSHREVAPLKQADDADYVDTTSMSIDDVVAHVKEVVHIKTKKADLTVQNTEKQPSTIIPSSEMDKKTLARIKTYYKPEKSFAFYRFLRVILRPIQMLVWPTKVIGAENAKKVTGALFTCNHYSKMDSMIPYFVLFKKEAHALAKYELFTNPVAGWFLHKMGAIPVRRGEADIESVKQVLRVLKDGKQLLIFPEGTRNKEGTQQMAEFKTGTARFAIKSKVPIVPMIYYQSPKAFRKNWLYVGEPFTLEEYYGARTIDENHAATQVIKEKMDETRRLCNEYVESVTKKKKKSTKKNK | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 477
Sequence Mass (Da): 54266
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A0A932KXK1 | SKTFTTQETITNAKTCRDWLVTRLGEAATPFHFVALSTNTKAVAEFGIDPANMFQFWDWVGGRYSLWSAIGLSIAMAVGYEAFEQLLAGGHAMDEHFRTAPLDSNMPVILALLGVWNGNFLGAEAYAVLPYDQYLHRLPAYLQQLDMESNGKGTAKDGARVTWATGQTVFGEPGTNGQHAFYQLIHQGTRLIPCDFLVAARTHNPLGEHHTLLLSNVLAQAEALMKGKTEAEARAELEAAGMNADEIAFQLPHRVFPGNRPSNMLLYPRLDPFTLGMLIALYEHKVFVQGVLWDVFSFDQWGVELGKVLAKAILPELTSSGPVLGHDSSTTGLIEAIRQMRQ | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 342
Sequence Mass (Da): 37648
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A0A9E0QJC6 | MDELSSRLLARLQDAFSMEEMAQTAVNGLINIATALAVFMAFYVIWRLLRVALNVASARSSVDETTVSFMQTLLKYGVLAVGFISALDTAGVQTGAVIASLGIAGLTIGFAAKDALSNLISGILIFIDRPFVIGDLVEVDGQYGRVDRITLRSTRIITRDGKMLAVPNTEVINQTVASYTNFPNLRIDIAVTVGVEESLGRVRELLLGILRDKPEYMSEPAPRVVVTALNDYNLALELQAWIINEREHVELRFALRESVFETLRAAGVEMPLETLQLVAPNTEEPVPRAS | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions.
Subcellular Location: Cell inner membrane
Sequence Length: 290
Sequence Mass (Da): 31724
Location Topology: Multi-pass membrane protein
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A0A520ZY01 | AARELDLTHFGEGDYIGAVQQKVSSETISKVLYPPDHNYAGQELRLRQQYFFVAATFQDIMRRYKKNNDTFDDFPDRVAVQLNDTHPAIAIPELMRLLLDIEGLNWEKAWDICTRTFAYTNHTLMPEALERWSVELIGKVLPRHLQIIYEINQRFLDQVAQKYPGDIDKLSRMSIIEEGYPKKVRMAYLAIVGSHSVNGVAALHTQLLKDKVFKDFHKFYPNKLNSKTNGITPRRWLLKCNTELAQLINDQIGSGWEIDLDRLRELEPLATDKDFQARFRQIKLNNKLKLADYIGISTGVLVTPETMFDVQVKRIHEYKRQLLNALHVINLYHRFVTDEQADLAPRTVIFAGKAAPSYWRAKLIIKLISSIGEVVNNDPRIGDRLKVVFLPNYNVSQAELIIPAADLSEQISTAGTEASGTGNMKFALNGALTIGTLDGANIEIREEVGAENIFIFGLTAEEAEYERIHSSRKPVQICRENEDIAQIMESLSDGTFGHGDRHLFQPLFDSLMSPHDQYLLLRDLESYLESQDRVNETFLDPDLWTKMAILNVARMGKFSTDRTIRQYSNEIWGIDV | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
Sequence Length: 576
Sequence Mass (Da): 65920
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A0A7Y5HCM4 | MRKLKGIVLLPTLVTLGNILCGFAAVIFAARGFADARMNLAADAAHHFEIGAWCVIFGMVFDALDGRVARMTGQASKFGAELDSLCDVVTFGLAPAFLAWVTMQTCGTIIPQKVATAMCGVYAACAALRLARFNVETTLDEEAHMSFRGLPSPAAAGVVASICLLRNSQGDSPLAVWIVLALPFAVLACGLAMVSNVRYAHMVNKLLRGRRRFTRMIEVVLIAVLVALEKEMTIAFGFCAYAASGPILWVFRRGGAPEIPILPPTPGRRNRSSMASFVIGTAGHIDHGKTRLVRALTGVDTDRLAEEQRRGITIELGFAPIRLPSGARGGVVDVPGHERLVRTMVAGATGIDLALLVVAADEGVMPQTREHLDILRLLEVSRMVVALSKTDVVDADLAELAAEEVSSHLQGTPFAGSPVVPVSSATGDGIEALRALLDAVVTRLPRRPHEGPFRVPVDRAFSMRGFGTVVTGTCVSGRVSVADEVEVLPARVRTRVRGVQVHGQTVPEAGPSHRVALNLQGISTEDIPRGSVVCAPDSVPVTSMADVRLHYLEGQPIREVAASLRTSVNSVKARLYRARRKLRATKEGGSGG | Function: Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 592
Sequence Mass (Da): 63012
Location Topology: Multi-pass membrane protein
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A0A1D9ML01 | MSKAKPSNSANPQDEVAETPFNPTKEVLLSTWGRDIDPELLVLALTHRSFANEQGGLPNNERLEFLGDSVLSIIVTEYLYRRFPDRPESQLSKMRSGCVSQTPLAIVARELKLGDYILLGHGEVISGGNDKDSILSDTLEALIGATYLCHGLEATRETVLAHLEPILRQASERGAAMDWKTTLNVLTHAEGLATPEYQVESTGPAHQRHFAATVKIDGKVWGRGEGSAKRYAERNAAQEAVEKLQAELDKADNA | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
EC: 3.1.26.3
Subcellular Location: Cytoplasm
Sequence Length: 254
Sequence Mass (Da): 27802
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A0A1D9ML09 | MRLAELDENQLLQALSPYFRHNQETLVGVGDDCALIAAPDSQYVVSTDMIIGEQDFKADWSRPWQIGRRLAMQNLADIAAMGARPTALVLSLALPNELELDWLKSFYQGLDSAAKQVGAVIVGGDLSRFHTLILNATVMGSLDGTNACTRDGGEPGDLVAVAGHLGFSYAGLDLCRQGYAQDLSALPAALRPLAAQCRDIFKSAEPPLAQGPRAAKAGAKALIDTSDGLLVDLTRIAKASQVSIELSIQALDQAMAPLRPLADFLGKDAKEWVLYGGEDHALAGLFPPDATVPKGFQLWGKTLAGSPGTITLAGTKVASQNRWDHFGGTHE | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 331
Sequence Mass (Da): 35187
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A0A286XLP2 | MSSKTASTNNIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLIGIPTSENPFKDKKTCTLL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequence Length: 72
Sequence Mass (Da): 7994
Location Topology: Lipid-anchor
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A0A1Q5ZX94 | MNSRQSTNVKTTAGHQFTDLRVVLTKYVYHWPLFALGLIVALTGAYIYLHNVNPVYEISATILVKDEKKSPQQEKSALPELDQTSSPKNAETEIEILKSKNLVKQVVNNLQLWVNYKSGVDFKTQDLYETSPVKFLLVQKTGSLTGKKISIVIKDKNTFVFDNVSGQKQSAAFNTPIKNGFGTWLLKPTGFIDQYIGSTINIDLNEPEMVSNNYVKTVDAHLLDKLAPTIGLFVTDEVPKRGVDFLDNLITAYNQAALLEEKRTTKSTIDFIDHRLASLTGELSHAEKNVEGYRSSQGITDISSQSQVYLENVQNNGIKLNEVNVQLNVINGIERYVNSNSETGTAPATIGITDPALNSLIEKLSDLQLKRSALLATTPEGNPMFEPINKQIALTKASIKQTVQGIKASLLSSKKELQSFNSKSESSIKDIPGQERQFVDMKRQQSIKENLYVYLLQKREELALSYASTFVDARIVDAANVGDITWPKKSFVFAIALLCGLGLPFMVIYFRNSFTNKITERRDIENALNIPVLGEISYEDLNDDVIVVTNKHHLIGEQFRALRTNLHYAHTNQNASPISLSNMPKASLNVVSNHDLNVEGRVTLLTSSVSKEGKSFVSVNLAVSLAATGRKTVIMEMDLRKPKILKIFNLSNSNPGISEFLSSNISVDAIINPSGKIANLDVIGCGQIPTDPSELLEHERLVELISELKDRYDDIIIDTPPLHLVTDAMIIAKLADVSLYIIRQGYTGKNELDFISEIEQTEKLPNMQIVFNGIKKNKYGYGYNYDNSYYNPDPAKPQFNMAWKQFLSRF | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 810
Sequence Mass (Da): 90435
Location Topology: Multi-pass membrane protein
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A0A1G0HEJ2 | MTKIIRGLQNLPDDWSDCAITIGKFDGLHLGHQYVLEWLHKLAAGLPTVMLSFYPNPLKFFQSDTEFQAILNLRDQLFWLNEYQIDVLLLLPFNRSIQTLSATNFLILLQQQIKAKKIVVGDDFRFGYQRAGDVDLLKHFAKAHDIDVLASLDQYVLENASEAVSSTEVRQLLQDGQLHAVHRLLSRPYAITGKVIQGDQIGRQLGFPTANIHLKNMRPALRGVFAVKVFQGKHFVADGVANLGQRPTVSGLKLVLEVHLFVSDIDCYGVFLTVEFIEKIRDEQKFDSLDALKQQIAKDVIEAKRIFRSH | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 310
Sequence Mass (Da): 35179
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R7LU17 | MENKKIKIGLIGLGTVGSGVFKTLQNFKNVEVVKIAVHNKNKKRNIEGLDESIITDDAYEVVNNPEIQIVAELVGGINPAFDLIKTAIKNGKHIVTANKELLAKHGEELFNFAEENNKVVLYEAAIAGGIPLIMPIKTILAGNKITKIKAILNGTTNYILTKMDVQGASYTDVLKEAQELGYAEADPTGDVEGFDAAYKITTLATIAFGKRIKIENVYREGITKISPDDMKAANEMGYKIKLIASAELNEDSKADVRVHPMLVPKTKTLAHIDYVTNAVSLSGHPVGDVTLSGPGAGEFPTASSVVGDILAIASEIDKTDYLLPMMRCNHHENAVMTPIEDTRNKYYISITAHNRLGVIGRIGKACEDHNISLASIVQKEVAGDNAAKITVITEICKEKDMQNVINIFNNDPAIASVNSLIRVQF | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 425
Sequence Mass (Da): 46122
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A0A834HCR4 | MGFATTICTDKTGTLTLNQMKVTTFWLGQDCIEEKGISSVPTSVVELLHHGIGFNTTGSVNMSTSGSEFEFSGSPTEKAILSWAVSELNLDMEGLKQSGEILHVEAFNSTKKRSGVLMRNKEQNTINLHIKGGAEMVLAMCLNYYNVTGTIKVLDDDERKIFDGIIQGMAASNLRCIAFAHKQVPKEENEEGKNQIEENCLTLLGLVGLMDPCRPGVKEAVQEFQYAGVNVKMVTGDNIFTARAIATECGILKPNQDMESGAVVLGEEFRNYTPEERMEKVNNISVMARASPRDKLLMVQCLKQKDHVVAVIGDGTNDAPALKEADIGLSMGIQGTEVAKECSDIIILDDSFGSVATVLRWGRSVCTNVQKFIQLQLTLTVATLAINFVVSVSTREVPLSVVELVWVNLIINTSGALALATEKPTKELMEKPPVGRTKQLITNVMWRNLLSQALYQTAVLLTLQFKGEALFKVSANVNGTLILNVLVLCQVFNIFFMWKLENKNKFEGIHKNHLFLVIIGVTIAVQVVAVEFLKKVADMERLNWWQWGVSVGFASVSWPIGWVVKWIPPDGEN | Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
EC: 7.2.2.10
Subcellular Location: Membrane
Sequence Length: 573
Sequence Mass (Da): 63150
Location Topology: Multi-pass membrane protein
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A0A0S2SL20 | MNKIYLAVALACWGSSALAAELVTIERVAGPQQVSADGKGVSALVGGGDYRAVRTVILPNGEKRVRFEQTWQEVPVWGSALVAEQGASGIERVSGQQLVGIDQDVASPQPAFNAATAAQKARGQQQGRNEKVRLFVMQDESGQARLVYQVSYLVEGSETPSRPFVIIDAQTGAELKRWEGINHQDATGPGGNLKTGKYFYGSDYGPLQVDANCRMSSTNVDTINMNHATTGGTVHQFTCPENTVKEINGAYSPLNDAHYFGNVVFNMYRDWYNTAPLSFKLKMRAHYSKNYENAFWDGSQMTFGGGATTFYPLVSLDVAAHEVSHGFTEQNSGLVYSGQSGGINEAFSDMAGEAAENFMKGSNDWLVGAQIFKGNGSLRYFEDPTRDGKSIGHASDYYDGLNVHYSSGVYNKAFYLLANSSGWSTRKAFEVFVLANRLYWGANTNYDSGACGVTKAATDLGYSLTDVAAAFQAVGVNASCGTTPPSGNELQNGVAVSGLSGAKGAQLNYTMTVPAGVSKLVFAMSGGSGDADLYVKFGAAPTSTSYDCRPYKGGNTETCTMNAPKVGTWYVQVKGYSAFSGVTLKGSY | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 588
Sequence Mass (Da): 62854
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L0PGR3 | MKRNQILWFIFPYLSIYGFSVYDDILSRPRYQVKFKDIPISAQIANDRLLYDSNTHNQSIDHEILKLNNEKYFCTTPKVEHEPIDSEETPDAKAKKENETKKALENGLKLISPLENSCIYYLEGWWTYVLCYNKYAKQFHPLDWDGSQKSLRILENQSEIYYLLGRFNTSIKEGISTFSSKIEYNGDSYYISQKVGGGTYCNFIQENRHVEIQVHSFSFLQTIER | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 225
Sequence Mass (Da): 26537
Location Topology: Peripheral membrane protein
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A0A969FLA7 | MIATQHLRYFIQIAILAVLYIIMSRAIALIPDSTLAACFIGLPNAISLSILLRTRRNSPWPGMVIGSFLAAQMTDYGFWSAILAGSGDSLFVTVSLWILRALNFDPSIARLGDVLTLIAVTVSTSLLDAIATTVANINNFTELNPLSVSWSTAGIGDAAWSLTIIPVILALTDRSNDLDSGYIRRPWSRVTECIVLLLLSFGLGWLIFCSRTRASNYTYPLEYFPLILLMWSSLRFGKRGTMLLNFGIALMAIFGIARASGPFLMSNLSAEQSVVSLQIFLFSMSGAALSFATVIVGRSRAQKLQQNSRRRLEQAQRIACLGNWELDLRRNVMTWSPEMWKILNLMSRRHETPTRSLLVEAVHPDDRPMLEAAFTALLNDGQSFCLGYRLSGDDERIVREQCERQDQYLIGTLQDITEHQRSEELREAKEAAEAANRAKSAFLANMSHELRTPLNAIIGYSELLEEDALDLGHEEFAEDAHKIRGAGEHLLSLIGDILDISKIEAGQLRLTPITFSIAHLIDEVVLNIQPMVDANGSTFKQDCPPDIGCMCSDNTVVRQILLNLMSNAAKFTHAGTIVLTVKSVAASDPGLNLGTVTAPLSVSPPSNSQPSNSQSPQLIPKTSPLQDSDYIQFTICDTGIGMSPEQLTQIFQPFTQADSSTTRKYGGTGLGLTIGQKLAHKLGGEITVSSVLDQGSCFICTLPRSLTILSNEFEDDGILD | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 720
Sequence Mass (Da): 78912
Location Topology: Multi-pass membrane protein
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A0A4Y7K0H0 | MVSINFRSLLIFSAALRIFLIIYGEWQDTHMEVRYTDIDYYVFSDAASLMASGRSPYERSTYRYSPLLAFLLVPNSFIHQSWGKFLFSASGSVLQAAIWYGLVVHFRVYPIIYALPILLVLHPLNLQTGQKLVIQKWSQIQQESSLHSSIPNLSCMANPLLLLRNLFTRRRLTFGLLSGTFLIFTGVSFYLYGWEFLHEALLYHLTRTDPRHNFSIYFYHIYLHHEHAFSVVEKLISFLPQLIVQLALIVRFAQDLPFCLFVQTVAFVAFNKCPPSYCNLTHSPIFPPFHFTVTSCSTVSDVHKVHTQMIKHGNYSDGFIGNRLVTMYATFGSVDSALKLFEEIPDKDLISWNSMIGVFAQRGNVNKCFSLFSKMRSEMGVEPNEVTLISLLPVCINMRALTEACELFNTISSKNLVSWNSMIAAYSQNGFLEDGINLFNSMRRVGFRPDRATIVTLLQVCAELAAEKQGKAMHGYILSSGFSSDMPIATALIRVYAKSGRLDASYEAFSEISFPDKIAWTAILAGYAIHGYARKAIKVFDLMVKNGAKPDHVTFAHILSACSHSGLIEEGKHYFQSMSKVYGVEPDVDHYSCMVDLLGRLGRLDEARELIEAMPTDPNPGVWGALLGACRVHHNIKLGKEIAEKLFMLDPTDPRNYIMLSNMYSASGLWREASQVRALMKERGLRKHPGCSFIEHGGKVYRFVVGDRSHPESDDIHSMLDELITKIQKAGYVPNTDLVLHDVDEEMKADMISKHSEKIAIAFGLLVTNHGRPITITKNLRICGDCHNAAKFISVVEKRKIIIRDSKRFHHFLDGAFRVRFRIVTPLSGSLPHSSKRVHHLKCFGDFGWKKSTVYDIFLGSSSPVQDRDNVFRFAEPRSGSLHRFQDRRNIKPPLQGDVVQR | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 902
Sequence Mass (Da): 102268
Location Topology: Multi-pass membrane protein
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A0A1Y6EZ43 | MKTYFITGTDTDAGKTVAAVALLQAFAKTGLRTCAMKPIAAGCEQHSEGLRNSDALLLQAAASVPMTYQQVNPIALVEPIAPHIAAAIAGKPIQVADLVAAWSALQQLPADLLLVEGAGGWELPLSANQTMPEFVKQTADGVILVVGLKLGCLNHAMLTVQAIRAAGVPLVGWVGNQCLPQKMPYQAENIDYLRAKIDAPWLGTLPYSQSSDRLELADHLQLNMNLSEFS | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
EC: 6.3.3.3
Subcellular Location: Cytoplasm
Sequence Length: 230
Sequence Mass (Da): 24440
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A0A924H0R2 | MALFELVIMLLLSAVALGWIARHFKFPYPIALVAGGAVLGLVPSLPQFVFDPQLILVAVLPPILYQAALLTSWSDFKANIRPIGLLAIGLVVVTTLAVGAALKWMVPDVPWAAAFVLGAIVSPPDAVAATTILSRLNMPRRIVTILEGESLVNDASGLVIYKFAVAAVLTGAFSLTDAAVQFAIVSVGGIAIGAFLAFVYIAIHRKLGDPFIEVLTVLTIPYVAYLAAEDLHVSGVLAVVAAGLVRGRYAPEIVSAEMRIMARSVWNLLVFLLNSLVFILIGLQMNGVVIEILGQYSGAQLATIAAVVTAVAVAVRFLWVFPIAYLPRWMIGNLRDDDDPRPDTREIAIIGWCGMRGIVSLAAALALPL | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Subcellular Location: Cell inner membrane
Sequence Length: 369
Sequence Mass (Da): 39269
Location Topology: Multi-pass membrane protein
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A0A2D4I058 | PLAAGSDGHGGELHLWPIENCSSTLQSNTTSAPCPSQGNTRYCLAASYVGLVLVGLSVGSVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAILSLGGIAYIQQNVSFAIGYIIPTVCIGVSFVVFLCGQSVFITKPPDGSAFTDMFRILAYSCCNRKQPERFSSPRGSQGILHQSQPSKDSILEAAKASNGGPFREDKVEDVKALAKIIPVFLALIPYWTVYFQMQTTYVLQSLHLRIPQFSNSTSNGTTNAHTFPAAWLTMFDAVLILILIPLKDKVVDPMLKRKGLLPSSLKRIAFGMFFVMCSAFAAGILESDRLRRVKTKTIDQKIGTAVYHAADMSVWWQVPQYILIGISEILASIAGLEFAYSAAPKSMQSAIMGLFFFFSGIGSFVGSGLLELVSLKSIGWMSNHMDLGNINGCHLNYYFFLLAVIQGVTLLLFLIVSVKYDRQKSRTNAGRT | Catalytic Activity: a dipeptide(out) + H(+)(out) = a dipeptide(in) + H(+)(in)
Subcellular Location: Membrane
Sequence Length: 465
Sequence Mass (Da): 50934
Location Topology: Multi-pass membrane protein
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A0A1Y3WPP7 | MAAPAFADEPASAEPAATQSAQAETEAGDSTTGKAIASAVAVGLAAAGGAIGMGLLGAKATESIARQPEADGKIRTTMMLTLVFIETAIIYALLVDILIIFVL | 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: 103
Sequence Mass (Da): 10263
Location Topology: Multi-pass membrane protein
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E4TFP8 | MELSKLKDFYWGNWNRIKKEQFNNNQFITWDFLSSISNLSDETIRLAFKSFDIDSSEIAIIPLGGYARKEMCPFSDIDILIFHTKTLRKKDEEFIQSFISRLWDIGLAPGVQIKDIDELCEPSYLDEIVKNSLIDHRFLEGSFLVYKEFERIVSNYILNRGRYNFLVAKINDVRNRMKRYRDSMYKIEPNIKDGIGGVRDYNAVYWVNKVLFESENLVTLVHEKIINYDEYESFKKSVEFIFKIRIRLHYFYNRKNDILNMESQKYISESLGYMDTSYSLGVELFLRDYYRSARTISDITHKVFEKVFTNYTINNNMKKIYMEDLGFGLVKYENTLTVRDSRIFEKYPLLLINIYTIAAKNGLKISDGTSQLIRENLFLIDENYLRKNGYFFLKAISYFPYSFKVANSMLKDGVLTRFIPEFEDIYCKAQFNTYHHYTVDEHTLLALKFIDDLANIFTSKYADYQKVFTEIERKDLLAMSMLLHDIGKGQGKNHSEVGAKMSRIISGRLGFKLDDIDTIANLVEHHLLMAHISQRRDINDLDVIKHFISFINSEEELKMLYILTYADSRATGGNNFNDWKKSLLTDLYHNALRYMQSEDMLKEFVSIVSNKKAKLKDRVGSNVLMLNMIDSLDDDYIFSNKINHIVRHLDMAIKLNDDNRKIIYGEIREDLNCFEITICTFDSIGLLKKVSGVLASFNINILGAQIYTLNRMIAIDKIQVNMNNESVEFIAERFPDIERRIHDVLSGKVNVEDLLSKTLGTIYSRKKIFKVNRKIEFDNVTSPIYTIVDIYAEDFVGLLYYILSVFEKLRISVQKAKISTDVNRVVDSFYITDEFGNKIEDKSMLQTIREEIFKVI | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Length: 856
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence Mass (Da): 100459
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A0A834H385 | MLYALSVPTQTLYQVHDAASIKSRKQFELSYPRGFTDCIQPFVCQANMAADSEGCCYWSLFSFLSFVADSGMGVVIMGVSGAGKSTIGEMLAKAVNCSFLDADDFHPQSNKEKMHKGIPLSDEDRIPWLNLLRDALRASLVSRKTMILGCSALQKQYREILRSADPNYVPGSYFSVMKFVLLDAGAEVLAARLEKRAGEGNHFMPAKLLQSQIDLLQIDESEGIVKVDATISPLVIVDTIKALFFDIYSHRGTSDESEGSTNSSAVKTRTRCPLQDQLLQRKISRDNVCNIVVATYLDRFIPNRSAMDFDYAHYMLTEGRKGKENPAVSSPSREAYRKQLAETFNMNRTRILAFKNKPPTPVEAIPHDFSGVQQSKPTKARRYIPQPQANMCLSYIKIEHPMGLTRLESGHGIVAFAIVVLNITSERTLDAPDLLDDYYLNLLDWGSSNVLAIALGSTVYLWDATDGATSELVTVDDENGPVTSVKWAPDGKHIAIGLNNSDVQLWDSTSNKQLRNLRGCHQSRVGSMDWNNHILTTGGMDGQIVNNDVRIRSHIVETYRGHHQEVCGLKWSASGQQLASGGNDNLLHIWDRSTASSNSPTQWLHRLEDHTAAVKALAWCPFQGNLLASGGGGGDRCIKFWNTHTGACLNSVDTGSQVCSLLWNKNERELLSSHGFTQNQLTLWKYPSMVKIAELTGHTSRVLFMAQSPDGCTVASAAGDETLRFWNVFGTPEVAKPAPKANPEPFAHLNRIR | Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 753
Sequence Mass (Da): 83268
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A0A0C3PXK6 | MLLPGARMQISFLKDLATLRSPQSEITFVSYLHSQNRLLDFINRGSNFPTRKEYSDYLAWAARFVQGKGVTVVYGENVVGVCKKDTKTIEIQSTVLSTGKRVARLTKNLIISPGGEPRIPKPLESIQDQLMGRIIHSSTYLMSVEVLLKSLQGENSLGRPFRIAVIGSGQSAAEVILELRSRLQSVTHTSEDNHTLDMIIRKGSLKPSDDSPFSNEIFNPDDTDIVFGLRSSSGRHRIRKEYANTNYGVVNHQTLERLYEILYEQKLDDGIYKRTGSLVPEKIPRINILPYSEILSADVHNLEGRRASGNKRPGPISVTVQHTLTHQIYQKVYDAVICATGYERKRWLQLLASSNIGKYFDLDPGTQEDVRLDVETGPEERGMAGELLTSESVDHIADDEGNSGGGTTSTGPSTPITPQSSVEVHFPKRQKTVHISRAYRLLPKPQDPNECLEARIYVQGVAEETHGLSDTLLSVAGVRAGEIVDDICSGLNDVGLAAPRAL | Pathway: Siderophore biosynthesis.
EC: 1.14.13.196
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 502
Sequence Mass (Da): 55535
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A0A0P0Z8A6 | MPDGFFQRGQPITLTALAELCGASIEGVTGAGDVLIDGIGALDMAGPRDIAFLADANYVDQLADTRAGAVITSARHRKYARSSTPLLIVRHPSVAFATVGRVLFPAALRPGPMTSSGISPQAYVAPDALLEDDVTVEPFAMIASGAAIGAGSVVGVGSAIGPGCQIGRECRIGPNVSVQFALIGNRVILHPGVRVGQDGFGYAADATGLTKIVQVGRVIIQDDVEIGANSTIDRGAVRDTVIGEGTKIDNQVQVGHNVVIGRSCIIVGQVGIAGSVTIGNGVSIGGQTGFKGHVTVGDGAQIAAVSVVASDVPAGARWGGMPARPVREWIREMATLSAIAKDRQGAGRDDGHGNDA | 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: 356
Sequence Mass (Da): 36198
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A0A9D9QQF6 | MFDIGFSELIVIGIVALIVIGPEKLPRVAKTVGHLLGRAQRYVSDVKADINREIQLDELKKMQSEVVESARGIEDSLRKDLEATRTAIEAPVSAVAAEVEAALPAAASLDTPLPPPADGATPKTTA | 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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 126
Sequence Mass (Da): 13325
Location Topology: Single-pass membrane protein
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A0A366EVW4 | MSRMVRNIFSVGGWTVVSRLTGFVRDMALAALLGGGALNDAYVAAIKLPNQFRQIFGEGSFNAAYLPTYTRVLETKGPEHAGQFASQVFTLLILSQVVLLALVYLDMPLLVELTSPGFVREPQKFAAAVAMSRIMFPYIAFIAVFALHQGTLNANNSWSVPAAAPAAANLCMIAFLAWAAWFPKLSPGVASMASWGFLASGATQLAIAMADARRRGLLERLMRPRWTPEVRQFFWMLGPAIGISASYQIGALADQIVGSLLPTGGLSAISYADRLYQLPGGVIVIATGSVLLREMAGLVARGDDEAALHAQNRAASLTFALGAPFVVVFLLIPDLIIAAAFEHGAFKASATQQAAGVLAAYSLGMPALFVDRIVAASFLSRGDTATPMKATLAGVALNVALKVLLYRPLGAPGLALGTAAGLWLKVGSVYALARRRGWAEPDDRFIGAVAATLFASGALALALTLADAYLADALAHTAFSREIRLAALAGLGVSVYFPALALGLGLSGAAPTGALARVLRAVRPGDS | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 527
Sequence Mass (Da): 55163
Location Topology: Multi-pass membrane protein
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A0A346DZI5 | MCILMNILNKICNIVRIAGDAVMKIYHGNLCLYIKHKYDCTPITIADYISNNIIINKLSLYTPNIPFLSEENLLSWDKRKSWRNYWLIDPMDGTKEFLNRNGEFTINVALINEFGLPILGVIYAPAINIMYYAYENKAWKEDAYGHRERINISNLYPPTVIISRSHYDNRIKDYLDILGKHNLILSGSSLKFCLIAEGLAQYYPRFNATSIWDIAAGHAILLAAGAYLHDWNGNSINYIPKRSFINSGFLVSVKCNI | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell inner membrane
Sequence Length: 257
Sequence Mass (Da): 29467
Location Topology: Peripheral membrane protein
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A0A849W8G8 | MNWLSSKIKSHRCSLSRLTKKVAHINELEPWAEKLSLQEIREEFQILRNKIRSGIPLETLIEKAFALVRELSKRTIGKRHYDVQLMSGIGLVLGNVVEMAAGEGKTMVALLPGCMHGLTGKGAHIVTVNRYLAQRDFELMGPVYRELGISVGLVKEDDTPDKKAIAYQSDVTYGVSYAFGFDYLRDQLQLLEHSQNFLGYNLLKILEGKPVTSNVLQRGHAYALVDEVDSILIDEARTPLIISGQSKDSDKLVHNAKMYEEAYRLAEKLQQGEDYFLEDQNKNFQWTQKGQEKVNIHLATLRCDGMKRPWIQYVEQGIRAKLFYRRDKDYLIDSENKIVIVDEFTGRRFADRTWGEGLHQIIQAKEGVAITEEHRSVARITRQRYFKMYEVLSGMTGTASGAEREFSEIYDLPVVHVPLRKPSQRKVFPPRLLVSWEAKWKAIEEEIARIHKTGQPILVGTRTIQQSEECAQRLKNLNLEFQLLNAKQDSEEAQIISQAGEEGKITIATNMAGRGADIHIPPDVLNKGGLHVIAVERHESQRIDNQLIGRCARQGNPGSAQFFTSCEDMLFDLYDPKLGKKLISLSENKNELDPSYYKHFDRLQEKVEKEHLSIRKKMLYYDNWLEKLMESL | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
EC: 7.4.2.8
Subcellular Location: Cell membrane
Sequence Length: 632
Sequence Mass (Da): 72434
Location Topology: Peripheral membrane protein
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A0A1Q5ZZZ4 | MENYSIVIFIMAIMIGLSAVADKIKLPYPVLLIIAGIGLGFLPNLPDIELNPEIVFLIFLPPLLYDAAFNISYQEFKTNINTIITLAVTLVFVTTTGIAVVAHYLIPGMTWPLSFVLGAILSATDAVAAMSITKGLGISHKTSTILEGESLINDASALVSYQFAVAAVTGTAFVLWKATLQFAILMGGGFVVGSIIGQILAFVIKRIHQNRLATISFMLLTPFVTYLVAEEIHVSGVIAVVILGLSIAHFSRTVFPEDLKQQSKSIWDIIIFLLNGLIFILIGLQLPQVIKGITQAQLLPYIGYGFIITVVALVLRMGRVFLQQLNLQQAFKKGKGRITENALLDFKNSLIISWSGMRGIVSLAIAIGLPITLSSGSPFPQRSAIILISVIVVLFTLIGQGLSLPWLVRRLKGK | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Subcellular Location: Cell membrane
Sequence Length: 414
Sequence Mass (Da): 44860
Location Topology: Multi-pass membrane protein
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A0A1M5VRV0 | MSFKITILGSSGAVPAYGRYTSSQLVEIQNRHFLVDCGEGAQMQLMKLQANFHRIDHIFISHLHGDHFLGLMGLIFTMHLQKRTNELHIYSHRGLDEIITTTFRYTRSVPNFNIVFHRLEKDAREVIFEDEVLTVETIPLKHRIRCSGFLFKEKIKPRRIDKTRLPEGLPLLQVANLKKGDDITDAEGNILYKNADLTFDPRPSRSYAYCSDTAYNESMIDQIRDVDMLYHEATFEEEEAQKAAETFHSTARQAATIALKANAKGLLLGHFSARYKDLTPILKEAHATFENAHLAVEGDVFTLSD | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
EC: 3.1.26.11
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Length: 305
Sequence Mass (Da): 34812
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A0A6G8S6W9 | MSQSPASSLQNPNPMRKKVLAALIAVAIGHVGVLFAISQMSGPELKKIEKDPIKVRFVQITEDAPPPPPPPPPPVKPQVMPKPEPKVVEPPPVVKPKIIAEKPKPQVEKPKPVVDDTQEKQKREQERLEQQRQQQERLDQQKREQEQREQQARDQQMREQQAREQQAREEAERRAQEARNKPRSLSAGQISWVRSPRPSYTNADLKGSDRTIVVEIDADASGHVTNVKVIRSSGLDALDQKIVRAVRGAKFRPYKENGVAYPFKAQQPFELKLNSNG | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 277
Sequence Mass (Da): 31280
Location Topology: Single-pass membrane protein
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A0A136JL54 | MHFHIITLFPEICQAYTDASILGRAQKSEKGKGAKVKGKKISVSYYNPREFSKDKNKKVDERPYGGGPGMVMQAEPVLKAWEKAVGRKKDQSKVKTLIMSPRGRVFTQDVAKEYAQKYEHLVLISGRYEGIDYRVNEILGAEEVSVGEYVLTGGELPALTIVDATARQIPGVLGTFESLEEERVTSGKSYTRPEVLKYKKQEYRVPEVLLKGNHAEIEKWRGDK | 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: 224
Sequence Mass (Da): 25254
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A0A834GFM7 | MRPNAIWGGGEVSGQTVKRALPIDLEASLINALVACTHWCRNGVDDIPSVHIGSFSGENLWCIGSRDMAMDARSCRNSSFGAIHSDAPASRITPLALPQEEEAKTILRKIYPAEDVEAEIQALKESVETEIQEKGSSEKISFVKLLKTKTVRRGLIAGVGLQVFQQFVGINTVMYYSPTIVQLAGFASNQTALLLSLVTAGLNALGSIVSIYFIDRTGRKKLLVFSLCGVIISLGVLSAVFHETTTHSPAVIAAETASFGGYMCPDYSSAGSSGGNWDCMKCLKASSPDCGFCASSISCFPEPVQRGLWGIAATANWISNLIVAQSFLSLTQAIGTSWTFLVFGVISVVALFFVPETKGLPIEEIEKMLEMRGLQLKFWKKRGDSELKKNQNVLRRHTISVFVGDESGMINRIAGVFARRGYNIESLAVGLYKDKALFTIVVSGTERVLHQVMEQLQKLVNVLKVEDISKEPQVERELMLIKINADPMYRVEVMWLVDIFRAKIVDISEHSLTIELLPVLASIMNFMCGSVSCYLAHQDMKMAEFPKCSSSSFLFRGKMMLLQGVGLLDINGFGYGDRTGSIASFTFPENSSAFASLQRLLAGVGFPQSLVDTGDWRPRQNGCSAKKFKQIALRREKMGESAPFWRYSAASYPDLGGTMPVDAFVGKKKTTLNGESDTSVRGDVYPVETTDDFPISQVLDAHWGVLDDDDTSGLRSHTLSMLVNDKPGVLNILTGVFARRGYNIQSLAVGHAEVEGLSRITTVVPGTDDSIGKLVQQLYKLIDLHEVQDLTHLPFAERELMLIKIAVNAAARRDVLDIASIFRAKAVDVSDHTITLELTGDLNKMVALQRLLEPYGICEVARTGRLALVRESGVDSRYLRGYSYPV | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 886
Sequence Mass (Da): 97061
Location Topology: Multi-pass membrane protein
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A0A8J2ZSQ5 | MEWSWHPVQLSFYVAGTATFITFLLAVFAVFAVAVKKRKGRTLIETVFFMPLVLPPSVIGFILIVIFGNEGFIGKLIYRLTNSSVLFTSTAAVIAAVTVSFPLVYQSLKSGFLSVDKNIINAAKVDGATDWTIFWKIILPLAKGSALTGVILGFTRGFGEFGATFMFAGNIPGKTQTIPTAIYLAIEMGEMKIASYYALISIAFSFLFLSIIHLKDKKKPA | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 221
Sequence Mass (Da): 24141
Location Topology: Multi-pass membrane protein
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A0A7W8B6Y6 | MDQRTWREAVIGMTVQAGKLLESVICPRDVRALAPELLPQLATEIRAFLVEKVCTAGEHLGLNLGVVELTLALHRVFHTPRDAIVFDTGHQAYVHKLLTERQGGFARLRQEGGLSGYAARSESVHELVENLHASTALSYADGLAKGRQLAGERDRAVVAVIGRGAMTGGLAWQALNNLGAARERPGVVVLNDNGRSYAPTAGALAAHLNVLKAGVGAEDCRNLFTNLGFTYFGPMDGHNVAELEKALCRARQMGWPVVVHVMTVKGKGYAPAEQDTADCLHAVGTVEPATGRPAAPVPRMAGTGPKAAATDPEALARMNGTDILHRSAGHGLDVLIVAVGPLAGQALQAAHELEEFGIGSTVADPRWILPVNPALTALAASHRLIVSVEDNLRHGGAGTALLEACQNLRRHHPGGTPGPAARLHRTRPPRPAAGPLRAERGGHHQRRPHRPIHPRPRTVRARPIPCRCFRSCGPEEAVMTTIDLGLPTQPPPHTPVRRRTRQSRVGAVPVGGGAPISVQTMTTTNTADVDTTLQQIAEVTAAGCDIVRVAVPSQDDADALPVIAARSPIPVIADNHFQPRYVFAAIDAGCAAVRVNPGNIRKFDDRVGDIAQAASAAGVPVRIGVNAGSLDPRLLIKHGKATAEALVESALWEVSLFEEHGFTDLKIAVKHHEPTTMIAANRLLAERCDYPLHLGVTEAGPALQGTAKSAVAFGILLNEGIGDTIRVSLSADPVEQTKAGCHILASLGLRPRKLEIVSCPGCGRLQVDLHRLVAQVEAAFDDFPHPLRIAVMGCVVNGPGEAREADLGVSCGNGKGQVFRHGQVISTVPEDKIVDTLLEEALRLVEGIENVSGTGGAP | Cofactor: Binds 1 [4Fe-4S] cluster.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
EC: 1.17.7.3
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin]
Sequence Length: 858
Sequence Mass (Da): 90735
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A0A2D4IZ63 | MLKLWMDRKQWEEQDRKYLQWIWRQCSRGFRVPKMATKFLTWNVNGLNSPQKRRKVFHYLKQFKNDIICLQETHVKLEDHKYLMNAKLGTPYIASAPEKKNGIVIYVRPDLKVKVIEADKLGRYIIIDLTIETKNFKVVGIYAPNQQQGKFYELLHKKLIDSDCKSCIVMGDWNGVIDVKLDKKGSSKNIQTKAKLPKFFFDMKDDMELRDLWRERSNNEQDYTFFSDRHHSFSRIDFILITNDFCSRVKKIKICPRTLSDHSPVWLELEIGEKSRRTWRLNENLFRYDVNVLECKKQMKEFFILNMNKETPIDMVWDASKAFMRGVLINQNNAYRRKQRQKKEELEKEIKKKEQELILNPGDQKTREIITLLRSQFNMLISDQVATNLQYAKHNNFCNANKPGRWLAYMLRKKQKTRTIDKV | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.2
Subcellular Location: Mitochondrion
Sequence Length: 423
Sequence Mass (Da): 50694
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A0A3R7UZP1 | MFQDYHFEKWLINPDRVLILGILNITPDSFSDGGLYLNPKKAFNKAIKLLNDGCDIIDIGGESSRPGSTPISSQEEIDRIIPVIEKIKNEVECLISVDTYKADVASEAIKYGANIINDITGLSHDPDMIELVVKNNTPVVLMHMQGNPKQMQKNPYYNNVIDEISRFFSKQIRKLDKKAFPLDKIILDPGIGFGKTLQHNLKILKNIDIICKLGCHTLIGTSRKSFIGDILNCPPEKRLEGTISSNLFAITQGVKIIRVHDVLEMRRALTIFEKILKA | 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: 278
Sequence Mass (Da): 31257
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A0A3R9ZJN4 | MNITIIGTGYVGLVTGVCLAELGHTVICIDNDELKIKALSKGICQIYEPNLNNLLQKNIINKKITFTSDKKPLDKSNIIIIAVGTPLKENGEINMTFINDVLRDIISNVKKDTIIIIKSTVPIGTADEIKKNLDNTDLNYHIVSNPEFLREGLAVSDFMNPDRIVIGTDSEYAKKVISKLYNYFHALKVPIIYTDNKTAELIKYASNVYLATRVSFINQIADISESLKCDIKDIVYGIGLDKRIGNTYLSPGPGFGGSCLPKDTKALINIAKAKNIECPIIKSVYSYNNNRMKKLGIKIFNILLKHNVSKTKYTIGILGVTFKADTDDVRNSPSVTILKHLTKVIDCDYEIKIFDPKGLKNIKKYFKNKKIKYYEDVYETVKECNIIVILTDWNYFKKLDYDKIKNIIKNPIIYDCKNILSKKHIEDIGFDYYGVG | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 436
Sequence Mass (Da): 49268
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A0A969K5D2 | MIDILQLGHPQLRQSAQPITNFADDTLQTTIDQALTQLIQAGGVGIAAPQVGNDWSWCIVASHPTLRYPDAPYMSPLVMLNPLIIDRAETCDRGWEGCLSVPGLRGLVSRSTSVRVTYQNRDGEPRAETFEGFAARIVQHECDHLNGVMFIDRVERTADLMSEVEYRRQILKIPHDLPI | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 179
Sequence Mass (Da): 20021
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D9QE07 | MNIETCPIQGMMVIHLDLHEDSRGWFKENWQESKLVGLGFTGFRPVQNNISFNAEAGVTRGLHAEPWDKYVSVATGSVFGAWCDLREGSATFGATFTITITPETAVFVPRGVANGFQALEATAYTYLVNDHWAPDAHYSFVNLADPALNISWPIPLDQATLSKKDTAHPPLASAVPVPPKKVLVTGANGQLGRTLKKVFPHAEFCSRTDLDITTDITEARRWADYSVIINAAAYTAVDAAETDSTAAWRTNAEAPARLAAIAARYGITLVHLSSDYVFDGELPVHSEQEPFSPLSVYGQSKAAGDTAVSVAPQHYVVRTSWVVGEGNNFVSTMLSLAARRISPQVVNDQLGRLTFTEDLAAGIRFLLDNHAPYGVYNLSNSGEIVSWAQLAQRVFTLAGRSASDVQPVSTTEYFAGKAPAAPRPRHSALDLSKITGLGFTPRDWQDALASYCTTLDAKEG | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 460
Sequence Mass (Da): 49821
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A0A834GB81 | MVVSKASAYEESRLKRLEENKKRMEELNLNKLAQALSTPKSSPVCVLLGFWFSDLQMKRVKPKVPRQPVDLSAVRRSSRVADKPPTSYKEEPIEPLGRARRSYSFNRTNLANRVYASAEGRAYAIDRAEALQSGLESKFPSFGLPVQFCEKHLPSHDEFIALLDEDDNESPTKYLADKRGLSAGWRGFAIDHELVDGDALVFQLIEPTKFKVYIIRVNQVEDDDEAPNVTEVEAWKGLCVAVVIILVVGGGEGQLSENFYSLSCPNVESIVNQTVFTKFTQTIVTIPATLRLFFHDCMVELSQNIFKGLRFRFEIECFCCDLLVNSVGYKEDYEGGADASIMISSPNGDAEKDAPDNLSLAGDGFDTVIKAKAAVEAVCPGVVSCADILAVAARDVVVLAGGLSFKVELGRRDGLISKASEVAANLPDPSFNLSQLIAVFAKKNLTQDDLITLSGAHTIGHSHCSRFANRLYNFSLSSKVDPSMNPNYAQQLMQACPQNVDPRIAVDLDPVTPEIFDNVYYQNLLVGKGLLTSDEVLFTNPASRRTVKNFANNPSLFNSEFGNAMIKLGRVGVKTGNQGQIRKDCTAFNS | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 590
Sequence Mass (Da): 64938
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A0A5C7RZ30 | MTKHIAIVGGGPAGYVAASHAAAEGAQVTLIDPHPLGGTCLHRGCIPTKTLVEVCNLLEKMRRAESYGLHLSGTVEPDWPAMRAKAGKVIDLLNTGINSLMADRRVVHVQGRGRILDGHRVEVAGHGVIEADAVLICTGSSPILPESFMADRARVVTSDDLLHWDTLPRFLLIVGDGVVACEYAFIMNALGVQVTLVAMGERPLPFIDSDISAIVQREMRRRGIEFINKCAVESLMAIPDGVVALANDKVVASAERVLVAIGRRPNTHGMGLEEAGVELGPRGEIVTNGFMQTGLDGLYAVGDVNGRLALAHAASAQARLAVDHALGVECAPLDESVIPWAVFTMPEIGCVGMTEQQAVEKGHAVSAGRFDLRGLGKAQAMSELTGMAKVVTDRVSGRLLGVHIIGAHASDMVHEAAVLLRQGATVHAITQTVHAHPTLSEAIHEAAEDALGQAVHKPMKRKKTHHAHALP | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 471
Sequence Mass (Da): 49850
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