ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q965W9 | MELSELIEVTRVRDAFMRKGPRPAQVGDICIFGHHLIFAPTTVGKEVPDNAEEFWLLHKAVDRVLCEPISKENPQRGGLLALKCKNFLLIIFEIGDLEICRATARTIESLSNINGFLHDYAFFYNSPFTILDDGWSAFDLEQEFARLMLSTDAFRISSVNENFAICPTYPEKLIVPKGIGDDYLKISATFREGGRFPVLSYFHKETKSPLVRCSQPLIGPTNRRCREDETILNSMITVNRGYIIDTRSKSSATAAKAKGGGAEPQGNYRQWRYIQCPIPRQREIHDALTRMVDVCSERKVTSDRWVSRVGQAGWLSSVAASLEAAANVAQCIYNERLEEVPVVIHGGDGLDSTLIASSLAQILLDADARTIRGFESVIEREWICGGHPFSLRNNHCAYAEGTVTGPFESPVFLVFLDAVHQMIAQYPMSFEFDENFLIFLFEHAYASEFGSFLGNCEKEKKDNGIRKKTVSLWSHVHHPENMKQFVNVCYDPTPGVIWPSIAPQCIKIWDRLFFRWQRPDNSWSTPETETIQSLADHWKLREKELIAKASSLRRSVVELSRELRVLSPM | Function: May act as a regulatory subunit for mtm-6. In association with phosphatase mtm-6, plays a role in endosome trafficking probably by regulating phosphatidylinositol-3-phosphate levels . Regulates fluid phase endocytosis in coelomocytes . Regulates posterior migration of QL neuroblast descendants and the anterior migration of QR neuroblast descendants and HSN neurons during larval development probably by controlling Wnt ligand secretion through the regulation of sorting receptor mig-14 trafficking . Involved in the formation of correct synapse number in DA9 motor neurons .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64537
Sequence Length: 569
Subcellular Location: Cytoplasm
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Q96QG7 | MEFAELIKTPRVDNVVLHRPFYPAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGSLGTIIIKCKDFRIIQLDIPGMEECLNIASSIEALSTLDSITLMYPFFYRPMFEVIEDGWHSFLPEQEFELYSSATSEWRLSYVNKEFAVCPSYPPIVTVPKSIDDEALRKVATFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYIIDTRSLNVAQQTRAKGGGFEQEAHYPQWRRIHKSIERYHILQESLIKLVEACNDQTHNMDRWLSKLEASNWLTHIKEILTTACLAAQCIDREGASILIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCNTKQKWEAPVFLLFLDCVWQILRQFPCSFEFNENFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNQPSELSKFTNPLFEANNLVIWPSVAPQSLPLWEGIFLRWNRSSKYLDEAYEEMVNIIEYNKELQAKVNILRRQLAELETEDGMQESP | Function: Acts as an adapter for myotubularin-related phosphatases . Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5-bisphosphate and MTMR6 binding affinity for phosphorylated phosphatidylinositols . Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3-phosphate . The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels . Stabilizes MTMR8 protein levels . Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles . Negatively regulates autophagy, in part via its association with MTMR8 . Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6 . Does not bind mono-, di- and tri-phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63462
Sequence Length: 549
Domain: The GRAM domain is required for cell membrane localization.
Subcellular Location: Cytoplasm
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Q9Z2D0 | MEFAELIKTPRVDNVVLHRPFYTAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGSLGTIIIKCKDFRIIQLDIPGMEECLNIASSIEALSTLDSVTLMYPFFYRPMFEVIEDGWHSFLPEQEFEFYSSATSEWRLSYINKDFSICPSYPPTVIVPKSVDDEALRKVAAFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYLIDTRSLNVAQQARAKGGGFEQEAHYPQWRRIHKSIERYHVLQESLIKLVEACNEQTHNMDRWLGKLEASNWLTHIKEILTTACLAAQCIDREGASVLIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCSSKQKWEAPVFLLFLDCVWQILRQFPCSFEFNEHFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNRPGELSKFTNPLFEANNLVIWPSVAPQSLQLWEGIFLRWSRSSKYLDEAYEEMVNIIEYNKELQAKVNVLRRQLAELETEDGL | Function: Acts as an adapter for myotubularin-related phosphatases . Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5-bisphosphate, and MTMR6 binding affinity for phosphorylated phosphatidylinositols (By similarity). Positively regulates lipid phosphatase MTMR7 catalytic activity . The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels (By similarity). Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles (By similarity). Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6 (By similarity). Does not bind mono-, di- and tri-phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62908
Sequence Length: 545
Domain: The GRAM domain is required for cell membrane localization.
Subcellular Location: Cytoplasm
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Q0RQV6 | MSSPRPSAELALLDIEGTTSPTAAVLSSLFPYARARLGPWVRDHGDDPEVRRIVAEARSLLGEADAPVQRVVAALTRWSDDDRKVAPLKALQGLIWAAGFAAGELTGELFDDVAPALRRWHAAGVRLAVFSSGSVLAQRAWFAATPAGDLTGLFDGYFDIDSAGPKRDPAAYRRIATELAVTPRRAVFLSDVSAELDAASAAGFATVAVLRPGEPHHLAGNHPCVASFAEMAVDAA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 24894
Sequence Length: 236
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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A9H8G7 | MTASTDAIDSVLLDIEGTTIPVAFVHQVLFPYARAAMPGLLAQRADDPAVRAAVADIAALAPGVPPLDQLNAWMDRDEKIGPLKALQGLAWEEGYRTGALRATLYPDVVPALRRWRAAGLRLAVYSSGSEAAQRLIYGHTTDGDVAGLFSGFYDLRIGGKRAAGSYRAILAETGWAAGRTLFLSDITAELDAAEEAGLRTCQLVRPEDGTVAGDRHPVATTLDDVARRFALPVAA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 24955
Sequence Length: 235
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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P0C8L5 | MIXAIVTDIEGTTSDTXFVXNVLFPY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 2881
Sequence Length: 26
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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Q48389 | MIRAIVTDIEGTTSDIRFVHNVLFPYARERLAGFVTAQQFVEPVKTILDNLREEIAQPAAGAEELIATLFAFMDEDRKSTALKALQGIIWRDGYVHGDFTGHLYPDVLPALEKWKSQGIDLYVYSSGSVAAQKLLFGYSDEGDITHLFNGYFDTLVGAKREAQSYRNIAEQLGQPPAAILFLSDIHQELDAAEEAGFRTLQLVRGDRDPASHHPQVQRFDDIHPEQIPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25614
Sequence Length: 229
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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A6T673 | MIRAIVTDIEGTTSDIRFVHNVLFPYARERLAGFVTAQQHAEPVKTILDNLRRETDAPAASTADLITTLFAFMDEDRKSTALKALQGIIWRDGYLNGDFTGHLYPDVLPALEQWKAQGIDLYVYSSGSVAAQKLLFGYSDEGDITHLFTGYFDTLVGAKREVQSYRNIAEHLGHAPGTILFLSDIHQELDAAEAAGLRTIQLVRGDRDPASHHPQVQRFDDIHPEQIPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25502
Sequence Length: 229
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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B0SFG5 | MQIKHNLLDIEGTTAPIAFVHQILFPYATKNIHRFLKEYQLTELQWKEVQTEFQKDTSSGDPLFIEKFRIKNVPSGLIVNEVPNTLSKDMVSVYFEYLIEKDRKFGPLKEIQGKIWKEGYESGEIKSTVFDDVPKFLNDAIQSGIQNHVYSSGSVEAQHLIYQYSVLGDLRQYFTMYFDTAVGGKREKTSYERIASTLAVSPSEIRFFTDIVEEAEAANATGMDVVILNRPGNLAQKPHPFPVWEHF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 28335
Sequence Length: 247
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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Q72NW0 | MNIKTFEFYLFDIEGTTTPIEFVHKILFPYSVEKFDSFFQSNLLEKEWIEKLILEGKNDTTYSGKLSDSAFDLSEYCKHLVSLDRKSGILKEIQGRIWKSGYENGELKSSMFSDVPSFLKKIQASKKKSAVYSSGSIQAQKLIFEYSDFGNLTHFFYAYFDTGVGGKRESSSYSKISEQLGVAPEKILFFTDIKEEADAAKEAKLHSAILERPGNYPQPQHSHFKISSFEGLNP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 26678
Sequence Length: 234
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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A1TZ36 | MIRVILTDIEGTTSSISFVHDVLFPYASEHLPEFIRANHHTLPAVAEQLVRVAEISGTDRKDIDGLINVLQEWIAEDRKEGALKALQGMVWEQGYHSGELKGHIYPDAADYLKRWHDRGLRLFVYSSGSVKAQKLIFGHSNEGDFTVFFSGYFDTAVGGKKESQSYRNILAELGVDAGTVLFLSDVEEELRAAEEAGLKTAWLVREGELPDTARVVARDFSEVDALLRKR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25751
Sequence Length: 230
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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Q5YQZ4 | MTTAIVLDIEGTTSPTGAVREDLYGYTRARLPEWLARHRDDAAAPILAATRELAGRPDADTDEVARILREWLGSDVKAEPLKEAQGLICHEGFATGALHGEFFPDVPPALRAWHAAGHRLCVYSSGSLRNQRDWFAHARGGELGSLISAHFDLTTAGPKREAGSYRRIAEALGVEAGQLLFLSDHADELDAAVAAGWSAVGVHRPGEPNPPRPPHRWIGSFDELDLARTPVS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25107
Sequence Length: 232
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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A7HU88 | MTAVRAVVTDIEGTTTPLAFVHEVLFPYARARLADFVAANADDEEVAAALGDARELGGIAGAGDAETLQLLLAWMDEDRKAGPLKLLQGLIWRHGYEEGVLKGEIYADAAAALRLWHGRGLRLFVYSSGSEAAQRLIFGHSDQGDLGPCFEGYFDTRIGAKVDSASYAAIAQSAGLPTREVLFLSDHEGEIKAAREAGMQAVTIDRTLQEEAWMEGPKAGSFSAVERALAPGKSA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25065
Sequence Length: 235
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
EC: 3.1.3.77
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Q03677 | MVKVYIHDNKVDSDYRAPHNSGTELSLDELAKLGVIYKYCANEEEVNEIARQREYKNRDVVNICEGSFKSEAEFNEKLATFYQEHLHEDEEIRYCLEGAGYFDVRDASTPENWIRCLVESGDLLILPPGIYHRFTLTTSNHIKALRLFKDEPKWQAINRSNQADSLPVRKDYIALINQY | Cofactor: Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site (By similarity). Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway . Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway (By similarity).
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)
Sequence Mass (Da): 20879
Sequence Length: 179
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6.
Subcellular Location: Cytoplasm
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B9DNJ2 | MIGIIGAMEEEILILKEKITDLEEISIAHVKFYKGYIDNQEVVLTLSGIGKVNAAISTTLLINTFSPDVILNTGSAGALDHSLNIGDVLISTEATYHDADATAFGYELGQIPNMPIAYAADDDLVTLAQSVVEQQEMNGKLGLIVSGDSFIGEVSQRETIKTNFPDAMAVEMEATAIAQTCYQFKVPFIITRAVSDLANGEANMTFDEFIGEAAKSSSEIVLEMLKSL | Function: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
Sequence Mass (Da): 24534
Sequence Length: 228
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2.
EC: 3.2.2.9
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P58525 | MKYDLIIIGSGSVGAAAGYYATRAGLKVLMTDAHMPPHQQGSHHGDTRLIRHAYGEGEKYVPLVLRAQTLWDELSTHNEEPIFVRSGVVNLGPADSAFLANVARSAQQWQLNVERLDATALMTRWPEIRVPDNYIGLFEADSGFLRSELAITTWLRLAREAGCAQLFNSPVSHIHHDDNGVTIETSEGCYHASKALISAGTWVKALVPELPVQPVRKVFAWFKADGRYSTKNRFPAFTGEMPNGDQYYGFPAENDELKIGKHNGGQLIQAPEERKPFAAVASDGAEAFPFLRNVLPGIGGCLHGAACTYDNSPDEDFIIDTLPGHENTLVITGLSGHGFKFAPVLGEIAADFALGKTPSFDLTPFRLSRFSQ | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidative demethylation of N-methyl-L-tryptophan.
Catalytic Activity: H2O + N(alpha)-methyl-L-tryptophan + O2 = formaldehyde + H2O2 + L-tryptophan
Sequence Mass (Da): 40664
Sequence Length: 372
EC: 1.5.3.-
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A7FH13 | MDYDLIVIGSGSVGSAAGYYASQAGLNVLMIDSAMPPHQAGSHHGETRIMRHAYGEGEKYVPLVLRAQALWDQLAAQTGEKLFQACGVINLGPDNSTFLQNVQRSAQQYDLPVETLNSTQIREKWPVFTVPDNYIAVFEPQSGYLRSELAVKTLIKAVTEAGCGILFNCPVTAIESHQAGVDVVTIDGTYSATKVVVTAGTWVKELLPTLPVTPVRKVFSWHQADGRYSEANHFPAFTVEMPDNILYYGFPAQNDALKLGKHHGGQLIESAAQRKPFGRYAEDGTEVFSFLRHFLPGVGVCLRGEACSYDMSPDEDFIIDTLPEDERVMVVSGLSGHGFKFATALGEVAALFAQDKPSPIDISAFSLARFR | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidative demethylation of N-methyl-L-tryptophan.
Catalytic Activity: H2O + N(alpha)-methyl-L-tryptophan + O2 = formaldehyde + H2O2 + L-tryptophan
Sequence Mass (Da): 40467
Sequence Length: 371
EC: 1.5.3.-
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A0A291P0C1 | MKKHLLAGACALAMGFAVIPGTFADETCNSPFTTALITGQEQYLHVWTLGMPGVGDESDKLVTISVDPKSDKYGKVINTLSVGGRGEAHHTGFTDDRRYLWAGRLDDNKIFIFDLIDPANPKLIKTITDFADRTGYVGPHTFYALPGRMLIQALSNTKTHDGQTGLAVYSNAGELVSLHPMPVTDGGDGYGYDIGINPAKNVLLTSSFTGWNNYMMDLGKMVKDPEAMKRFGNTMAIWDLKSMKAEKILNVPGAPLEIRWSLKPEHNWAYTATALTSKLWLIKQDDKGEWIAKETGTIGDPSKIPLPVDISITADAKGLWVNTFLDGTTRFYDISEPEHPKEVFSKKMGNQVNMVSQSYDGKRVYFTTSLIANWDKKGAENDQWLKAYDWDGKELVEKFTVDFNELKLGRAHHMKFSSKTNAAELGTNQSFPTRQ | Function: Catalyzes the oxidation of methanethiol. Can also degrade ethanethiol, but not methanol, methylamine or dimethylsulfide.
Catalytic Activity: H2O + methanethiol + O2 = formaldehyde + H(+) + H2O2 + hydrogen sulfide
Sequence Mass (Da): 48307
Sequence Length: 435
Pathway: Organosulfur degradation.
Subcellular Location: Periplasm
EC: 1.8.3.4
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P9WGK9 | MIFGSRRRIRGRRGRSGPMTRGLSALSRAVAVAWRRSLQLRVVALTLGLSLAVILALGFVLTSQVTNRVLDIKVRAAIDQIERARTTVSGIVNGEETRSLDSSLQLARNTLTSKTDPASGAGLAGAFDAVLMVPGDGPRAASTAGPVDQVPNALRGFVKAGQAAYQYATVQTEGFSGPALIIGTPTLSRVANLELYLIFPLASEQATITLVRGTMATGGLVLLVLLAGIALLVSRQVVVPVRSASRIAERFAEGHLSERMPVRGEDDMARLAVSFNDMAESLSRQIAQLEEFGNLQRRFTSDVSHELRTPLTTVRMAADLIYDHSADLDPTLRRSTELMVSELDRFETLLNDLLEISRHDAGVAELSVEAVDLRTTVNNALGNVGHLAEEAGIELLVDLPAEQVIAEVDARRVERILRNLIANAIDHAEHKPVRIRMAADEDTVAVTVRDYGVGLRPGEEKLVFSRFWRSDPSRVRRSGGTGLGLAISVEDARLHQGRLEAWGEPGEGACFRLTLPMVRGHKVTTSPLPMKPIPQPVLQPVAQPNPQPMPPEYKERQRPREHAEWSG | Cofactor: Autophosphorylates in the presence of Mg(2+) and/or Ca(2+), but only Mg(2+) ions promote phosphotransfer to MtrA.
Function: Member of the two-component regulatory system MtrA/MtrB. Probably functions as a membrane-associated protein kinase that phosphorylates MtrA in response to environmental signals. Autophosphorylates and transfers phosphate to MtrA in vitro. Overexpression of MtrA alone decreases bacterial virulence in mouse infection; co-expression of MtrA and MtrB restores normal bacterial growth, suggesting that bacterial growth in macrophages requires an optimal ratio of MtrB to MtrA. Probably plays a role in cell division.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
PTM: The C-terminal domain (residues 234-567) autophosphorylates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61637
Sequence Length: 567
Subcellular Location: Cell membrane
EC: 2.7.13.3
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Q58259 | MSHGGGGHAAELYPEEQIFAVGIALSLVGCYLANFLSPYGLGMLIGGLLASAACVAGANTVRKVAAYGLGTGVPSIGMVSLGMGTLAAVAGVLIPDYFNLPYLVAPIITLIVSAVIGYIVGRLTVNPVGMKIPIMVRSMTFLSIAGAMALLGFTVAYVGSLEPQKYIDYALNNGMMALAFIAAGMAILHPFNACLGPNESHKRTLTLAVACGFITWFVFSVVKLDIVSIIVSIILWAIVYVKFVKMSFKDACAVLHVPEIPKKEE | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27804
Sequence Length: 265
Pathway: One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 2/2.
Subcellular Location: Cell membrane
EC: 2.1.1.86
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O32865 | MILRTLLISAVAPGGEEEEVEVAVAISPLKLMTAGLICGILGTAFAWVHPLIPALAVIPVVVWGADAVRRVAGYGLGTGVPSIGFMGLGGGSVAAILAAALSGNTVPAWAAAIIGTVIGAVVGALLGVLDRRVIKMKIPVMERCSTEIVASGTLALICLMAAVAGDFTWSAVYSKVIATGLIAVLWAICAISLLHPFNACLGPSETQERTLWLGAECGSLCTVVAGLATANPVVLLAGAAAWLITFWKFWELTKRDAADVVWTGIVPKGE | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27666
Sequence Length: 270
Pathway: One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 2/2.
Subcellular Location: Cell membrane
EC: 2.1.1.86
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O59638 | MSAGGAGGEAKGAYPQQTLMALGIVGGLVGIYLGHFMPPAYSFFGGIGAICATVWGADAVRRVASYGLGTGVPSIGMLALGMGILAALFGLALGGIAGPILAVVVAAIIGGVIGALANKVIGMGIPIMEQAMIEISCAGTLVILGLSVVIAGSFDYAAIIENVIANGYIALIFIIGGMGILHPFNACLGPDESQDRTLILAVEKAAIALIITGFASSLHEGLMTAGINILVGLVIWYVAFSKYYALIKRDAYAVVGTGLLPSAEELQ | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26942
Sequence Length: 267
Pathway: One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 2/2.
Subcellular Location: Cell membrane
EC: 2.1.1.86
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P80185 | MSVAAGGPAGAAIPESRLMALGILGGLAGIYASAVNPVIGPVLASLGAVCAIVWGADAIRRVASYGLGTGVPSIGYMSVSIGIVGVVAGLASVFVVPAIAVPVVALILAMILGVVVAVLGKKIVKMKIPILEKCTAEISGAAALSVLGFSAAIAGSYTLQTMLTSVITTGFIGLLFILNTMAIQHPFNACLGPNENQTRTLKLAASTGFISMAIVGLLGIGLNPSWWLVSLIGALCWIVAFRAFVSASFEEAASVKWSGLWPKEEEH | Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27117
Sequence Length: 267
Pathway: One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 2/2.
Subcellular Location: Cell membrane
EC: 2.1.1.86
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P43505 | MAFYASKAMRAAALAAAVALALSSCGKGGDAAQGGQPAGREAPAPVVGVVTVHPQTVALTVELPGRLESLRTADVRAQVGGIIQKRLFQEGSYVRAGQPLYQIDSSTYEAGLESARAQLATAQATLAKADADLARYKPLVSADAISKQEYDAAVTAKRSAEASVKAAQAAIKSAGINLNRSRITAPISGFIGQSKVSEGTLLNAGDTTVLATIRQTNPMYVNVTQSASEVMKLRRQIAEGKLLAADGAIAVGIKFDDGTVYPEKGRLLFADPTVDESTGQITLRAAVSNDQNILMPGLYVRVLMDQVAADNAFIVPQQAVTRGAKDTVMIVNAQGGMEPREVTVAQQQGTNWIVTSGLKDGDKVVVEGISIAGMTGAKKVTPKEWAPSENQAAAPQAGVQTASEAKPASEAK | Function: Cell membrane lipoprotein, involved in cell membrane permeability to hydrophobic compounds such as antibiotics, dyes and detergents.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42774
Sequence Length: 412
Subcellular Location: Cell inner membrane
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Q17440 | MPRVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQEEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFLKFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREKFNADFIATGHYATTNFGDFQQNAKDSDEIRLFSGKDPLKDQTFFLCTVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFQEVAKKPESMGICFIGKKKRFSDFLDEYIEPKPGRILLKNGSEIGNHHGIHQFTIGKRINGKYLEARSHLGFFVSHIHSDTGDIIACEGSHHPDLYASRFLINHPKWIRTFDPFNRISSNNFLCRIQRTHPPIPCVAEKQEQFLSVIPRLALRATAPGQMCVFYNTKNECLGGGEIMNIQETL | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 42795
Sequence Length: 375
Subcellular Location: Mitochondrion
EC: 2.8.1.14
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Q54I63 | MINNINRIKKTYNTFLNVNKLRYSTSIISSNILENDNNNIDDFEQVLKSTKVRMPTSALLLPKKPKVCIGMSGGVDSTITAKLLKLQGFDVTGVFIKSWDEVEDTGRCQGERDWKDALEASNFLDIPMYKADFVKDYWNRVFVDFLKDYKNGLTPNPDVWCNREIKFDLFFDFAKENFGVDYIATGHYSNLYYGEENVGDNNNNNLQLHRAIDKNKDQTFFLCMTKGERLKQAIFPIGGFTKENIVSFAKTIPNFSKITSKKSSRGICFIGKRPLPDFLSQYMTLKPGDFFDISTNSFIKGKKHKGSVCYTMGQKANIDSLSERYFIVRSDIERNIVYVCPESQFDQFSLYYEFNTHSFNWINEIPTEVKSEQGFKGRGICRHRGDVVNLTIKDTGKTSPIDGSVIYSVNLDQPLRSVASGQILCLFDRNTDRCFGGGVINSSPLYNPTQF | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 51498
Sequence Length: 451
Subcellular Location: Mitochondrion
EC: 2.8.1.14
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Q9W5B6 | MIRNVVVGVSGGVDSAVSAHLLAEQGFKVLGVFMRNWDEADEVGRCSGEADLKDAEWACRQLGVELRQVNYVREYWTAVFSQFLDDYQMGLTPNPDILCNRHIKFDLFHKHALENLGYDAVATGHYARNSLGNYLEGIASNNDARLLIPADTFKDQTFFLAGISRKALQRTMFPLGDFQKSQVKDLAKKIGFQRLAKKKESTGICFVGKRNFKDFIQEYITSKRGPFLDIDSGAVVGHHEGIHQWTVGQRCRLSSFLQPYFVARKEAASNTIYVASGHNHPALLSTHIAVDPPNWLCSKSQQILSDTGSLRCRFRFQHTKPLVDCQLSISPSNTFLVELDAPLRAITPGQYAVFYDDTACLGSARILSANPLKKKNAQTQQAQAANLVS | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 43350
Sequence Length: 389
Subcellular Location: Mitochondrion
EC: 2.8.1.14
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O75648 | MQALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGADAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPALYRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQRRAGMATESPSDSPEDGPGLSPLL | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 47745
Sequence Length: 421
Subcellular Location: Mitochondrion
EC: 2.8.1.14
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Q9DAT5 | MSALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDNLGADAVATGHYARTSLEDEEVFEQKHTKKPDGLFRNRFEVRNPVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLHHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIEDNTVLGTHKGWFLYTLGQRAKISGLREPWYVVEKDGTKGDVLVAPRVDHPALYRDLLRTNRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKILRLGPSAYTLQKGKNRTRVAPEASSDSPGLHPTS | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 47240
Sequence Length: 417
Subcellular Location: Mitochondrion
EC: 2.8.1.14
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Q5RB73 | MQAVRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGADAIATGHYARTSLEDEEVFEQKHIKKPEGLFRNRFEVRNAVKLLQAADSFKGQTFFLSQVFSQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPALYRDLLRTSRVHWIAEEPPAVLVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQCGAEVATESPTDSPEDGPGLSPLL | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 47764
Sequence Length: 422
Subcellular Location: Mitochondrion
EC: 2.8.1.14
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O13947 | MRVSLFLQKQIIECSKAFQPHSTRLQWPKSQDKVFVAMSGGVDSSFSAYLLKSQGYNVEGVFMRNWLDEDSAPSGCPAERDWATVQKVCKKLNISCRRFNFEKEYWNLVFEPSLDLYENGLTPNPDVSCNRQVKFGALFDALKKHCENNVKGDWWLASGHYAKSVVNIETNESHMCIPTDKRKDQTLFLCTIRKEALEKTIFPLHNWTKENVKKQASSAGFKEIAEKQESQGLCFVSPNVGRKFRKFLQRYLNFSDRPIKVIAGKNVVGEFSGNHGIWSLTVGERCGLSLPQAQSEYFGRWYVWKKDIKNNALYICRGTNNELLMSKCIYLKDWKWCGTKLQNLEKSALSCFVRVRHQQPLQPAKVTWRNPESVKIHFQDKQRAVTPGQVIAVYVNDVCLGGGMVDTVEPEKDFD | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 47627
Sequence Length: 415
Subcellular Location: Mitochondrion
EC: 2.8.1.14
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Q12093 | MLARYLNLIGRRSASPYRPQRLPAKFDNVIVAMSSGVDSSVAAALFAGEFPNTRGVYMQNWSESQSLDDPGKEPCYERDWRDVNRVAKHLNIRVDKVNFEQDYWIDVFEPMLRGYSEGSTPNPDIGCNKFVKFGKLREWLDEKYGTGNYWLVTGHYARVMQEMNGKGLFHLLRSIYRPKDQSYYLSQINSTVLSSLLLPIGHLTKPEVRDLAKYAGLPTAEKPDSQGICFVNNSQHGKFKNFLKHYLPSSPGDIITVDPQSGAKTTWGRHDGLWSYTIGQKVGISMPQADPNYQGTWFVSEKLRDTNEILIVRGRDNPALYSDTMRIENFSSLGPREDTINAFQNTGALTLQFRSLQVPVQIKSCKLNRSADNLDITIHLASKQRAITPGQSCCLYIDDRVLGSGPISHVNNNDTHA | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 47049
Sequence Length: 417
Subcellular Location: Mitochondrion
EC: 2.8.1.14
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Q8N3F0 | MDFQQLADVAEKWCSNTPFELIATEETERRMDFYADPGVSFYVLCPDNGCGDNFHVWSESEDCLPFLQLAQDYISSCGKKTLHEVLEKVFKSFRPLLGLPDADDDAFEEYSADVEEEEPEADHPQMGVSQQ | Function: Promotes megakaryocyte differentiation by enhancing ERK and JNK signaling as well as up-regulating RUNX1 and FLI1 expression . Represses NF-kappa-B transcriptional activity by inhibiting phosphorylation of RELA at 'Ser-536' . May be involved in early neuronal development (By similarity).
PTM: Phosphorylation at Tyr-34 is essential for its ability to promote megakaryocyte differentiation.
Sequence Mass (Da): 14925
Sequence Length: 131
Subcellular Location: Cytoplasm
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Q8CGA4 | MDFQQLADVAEKWCSSTPFELIAAEETERRMDFYADPGVSFYVLCPDNGCGDSFHVWSESEDCLPFLQLAQDYISSCGKKTLHEVLEKVFKSFRPLLGLPDADDDAFEEYSADVEEEEPEADHPQMGVSQQ | Function: Promotes megakaryocyte differentiation by enhancing ERK and JNK signaling as well as up-regulating RUNX1 and FLI1 expression . Represses NF-kappa-B transcriptional activity by inhibiting phosphorylation of RELA at 'Ser- 536' (By similarity). May be involved in early neuronal development (By similarity).
PTM: Phosphorylation at Tyr-34 is essential for its ability to promote megakaryocyte differentiation.
Sequence Mass (Da): 14841
Sequence Length: 131
Subcellular Location: Cytoplasm
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Q75GT2 | MSGGVQEQFEIKFRLPDGTDIGPKRYPAASTVATLKESIVAQWPKDKEKGPRTVNDLKLINAGKILENNKTLSECKSPICDFSGLTTMHVVVRAPTSDKQSNKIVAKKPKDFRCGCSIM | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13080
Sequence Length: 119
Subcellular Location: Cell membrane
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Q03162 | MRDSNHRSLTSNKPIVTITSTVYDRRALDINSSIPLINSLNYLTYLTSNSSKVRETVANDGALERLVSILRSCHLSLFELLDLDLENFNEHENIKDLWKEKRLALCAWKWTLTFQCLVLTGTRGTEQIRKKVVMSGVLSVLVTVLDNYLLYHKNYDFIKDQTMTFDFKGITTETMYKFMRKDENETYQQYIEFITGQDKLKLSTDKNFLNERLVAPSMTIPTDFSDIWGRFADLASNFEPDQERHDDDIDIDSEVESENFDAHKNFFSQPDINRPTISTPREFFLGRIVPKQDDVIWSLQLLAFVSKYTYMKSTLQNVELVESLSFRSMAYKIKQRISEENDLEEQERDVTVKLSSLYPYLSKNPENNSKVKALDTSKMDPFFKELEELSNRCQQEEQNEICNNHCPVLNLFERYRVPKPSDDNAYGKDKERINLRKKISDNFERRWSYDKMKKELTNIVYKNKVLTNVVNIFPLVEKYTVSAENTHDVIYWSSVIMRNSCRKNEILGVRQCANFSCGKWEDFPRQFAKCRRCKRTKYCSRKCQLKAWGYHRYWCHEVGSSHMRSTNTTTGVNTPNEPSSLNATATTAADVSNSTSTFTPNISTTVPDEISNRDENSIPE | Function: Involved in the determination of the onset of polarized growth. Required for the ubiquitin-dependent degradation of RPN4. Cooperates with UBR2 to transfer ubiquitin from RAD6 to RPN4.
Sequence Mass (Da): 72251
Sequence Length: 620
Domain: The MYND-type zinc finger is essential for the ubiquitin-dependent degradation of RPN4.
Subcellular Location: Cytoplasm
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Q8LCS8 | MAEVKDQLEIKFRLNDGSDIGPKLFPDATTVATLKETVVAQWPRDKENGPKTVKDVKLISAGRILENNKTVGDCRSPVGNFSGAVTTMHVIIQHQVTEKEKKKKKPKGDLKQNKCVCLCFGARC | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
PTM: Acylated protein. Probably modified with palmitate .
Location Topology: Lipid-anchor
Sequence Mass (Da): 13709
Sequence Length: 124
Subcellular Location: Cell membrane
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Q67UI2 | MASGGGGGGGMEAVEVRFRLDDGSDIGPSMHDQATTVTALKEFVLARWPQGKEIAPRTVNDVTIINAGQVLENNRTLAESRNLAAESPEGPITMHVVVRRSRPERRVKQPPKARPPERIGCGCTIL | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13554
Sequence Length: 126
Subcellular Location: Cell membrane
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Q9SW27 | MPEEESIDIKFRLYDGSDIGPFRYSAASTVDFLKQRVVSDWPKGKTVVPKGINEVKLISSGKILENNKTVGQCKTPFGDIAGGVIVMHVVVQPSLAKSKTEKKVDKAPKAVICTCTIL | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12836
Sequence Length: 118
Subcellular Location: Cell membrane
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Q6Z8K4 | MAGGKEPIEVKFRLFDGTDIGPSKYDPSTTVSALKEFILARWPQDKEITPKTVNDLKLINAGRILENNRTLAESRVPVGEVPGGVITMHVVVRPPQPDKNSEKQLANSPKQNRCGCTIL | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13079
Sequence Length: 119
Subcellular Location: Cell membrane
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Q9LSD8 | MPEEDLVELKFRLYDGSDVGPFQYSPTATVSMLKERIVSEWPKDKKIVPKSASDIKLINAGKILENGKTVAQCKAPFDDLPKSVITMHVVVQLSPTKARPEKKIEKEEAPQRSFCSCTIM | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13452
Sequence Length: 120
Subcellular Location: Cell membrane
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Q7XRU4 | MAEKEEGKVAAEGGAEAEADEEVEVKFRLFDGSDIGPLRCNAVATTVAALKDRVVADWPKDKTIVPKTANDVKLISGGKILENDKNIAQCRAPFGDLPSTAITMHVVVQPSSAKSKPDKKTNKLPKTTRCSCTIL | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 14437
Sequence Length: 135
Subcellular Location: Cell membrane
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Q9SH14 | MGDEDLIELKFRLADGTDIGPSKYSQFMTVASLKEKIIAQWPKDKENAPKMINEVKLINGGKILENNKTLSEARSLITIGELPGIVTTMHVVLRPPLFEKKKEKLQNDPPRKSHCVCCIL | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13487
Sequence Length: 120
Subcellular Location: Cell membrane
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Q8GWJ6 | MAGEEDWIELKFRLADGTDIGPSKYNQSMTVSSLKEKLISQWPKDKENTPKTVNDMKLINAGKILENNRTLAESRLPVCELPGMIITMHIVLRLPTLDKKSEKLQNDPPMKNRCVCTIL | Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13510
Sequence Length: 119
Subcellular Location: Cell membrane
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Q9H3R2 | MKAIIHLTLLALLSVNTATNQGNSADAVTTTETATSGPTVAAADTTETNFPETASTTANTPSFPTATSPAPPIISTHSSSTIPTPAPPIISTHSSSTIPIPTAADSESTTNVNSLATSDIITASSPNDGLITMVPSETQSNNEMSPTTEDNQSSGPPTGTALLETSTLNSTGPSNPCQDDPCADNSLCVKLHNTSFCLCLEGYYYNSSTCKKGKVFPGKISVTVSETFDPEEKHSMAYQDLHSEITSLFKDVFGTSVYGQTVILTVSTSLSPRSEMRADDKFVNVTIVTILAETTSDNEKTVTEKINKAIRSSSSNFLNYDLTLRCDYYGCNQTADDCLNGLACDCKSDLQRPNPQSPFCVASSLKCPDACNAQHKQCLIKKSGGAPECACVPGYQEDANGNCQKCAFGYSGLDCKDKFQLILTIVGTIAGIVILSMIIALIVTARSNNKTKHIEEENLIDEDFQNLKLRSTGFTNLGAEGSVFPKVRITASRDSQMQNPYSRHSSMPRPDY | Function: Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling.
PTM: Cleaved into two subunits, alpha and beta, probably between the first EGF domain and the SEA domain. Beta subunit contains the cytoplasmic tail and alpha subunit the extracellular tail. The homooligomerization into dimers is dependent on intrachain disulfide bonds.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 54604
Sequence Length: 512
Subcellular Location: Cell membrane
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P19467 | MKGFLLLSLSLLLVTVGSSSQASSTTSSSGGTSPPTTVQSQSPGSSSQASTTTSSSGGASPPTTVQSQSPGSSSQASTTTSSSGGASPPTTVQSQSPGSSSQASTTTSSSGGASPPTTVQSQSPGSSSQASTTTSSSGGASPPTTVQSQSPGSSSQASTTTSSSGGASPPTTVQSQSPGSSSQVSTTTSSSGGASPPTTVQSQSPGSSSQPGPTQPSGGASSSTVPSGGSTGPSDLCNPNPCKGTASCVKLHSKHFCLCLEGYYYNSSLSSCVKGTTFPGDISMSVSETANLEDENSVGYQELYNSVTDFFETTFNKTDYGQTVIIKVSTAPSRSARSAMRDATKDVSVSVVNIFGADTKETEKSVSSAIETAIKTSGNVKDYVSINLCDHYGCVGNDSSKCQDILQCTCKPGLDRLNPQVPFCVAVTCSQPCNAEEKEQCLKMDNGVMDCVCMPGYQRANGNRKCEECPFGYSGMNCKDQFQLILTIVGTIAGALILILLIAFIVSARSKNKKKDGEEQRLIEDDFHNLRLRQTGFSNLGADNSIFPKVRTGVPSQTPNPYANQRSMPRPDY | Function: Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling.
PTM: Cleaved into two subunits, alpha and beta, probably between the first EGF domain and the SEA domain. Beta subunit contains the cytoplasmic tail and alpha subunit the extracellular tail. The homooligomerization into dimers is dependent on intrachain disulfide bonds (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58701
Sequence Length: 573
Subcellular Location: Cell membrane
|
P97881 | MSQSSGGTSTPTTTATQPTSTSTQTPGTTQLLSTTSTPTTTATQPTSTSTQTPGTTQLPSTTSTPTTTATQPTXTSTQTPGTTQLPGTTSTPTTTATQPTSTSFQTPGTTQLPSSTSTPTTTATQPTSTASQTPGTTQPPGGASSPTTTVTQPTGSSSQTPGTTQPPGGASTPTTTVTQPTGSSSQTSGTTQPPGGASSSTVTSSSSTGSNDPCNSNPCKSPASCVKLYDSYFCLCLEGYYYNNSSSCVKGTTFPGEIGMSVNETTDLEDKNSVNYQTLHSSVVKFFENTFKKTDYGQTVILKVSKDSLMSSRSVMRAATQTVYVSVVNMFGENTKEDEESVASVIKEAVKTDNNVERYFQQDRCDYYGCVKSGSNVCRNGLQCTCKPGLERLNPQVPFCVAPTCSEPCSAEKKQLCLKKDNGAMECGCMAGYRKANGKCEECPFGYSGMDCKDQFQLILTIVGTIAGAFILILLIVFIVSMRSKNKKKSGEEQNLIEDDFHNLRMRPTGFSNFGADTSIFPKVKTGVPSQTSNPYANHRSMPRPDY | Function: Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling.
PTM: Cleaved into two subunits, alpha and beta, probably between the first EGF domain and the SEA domain. Beta subunit contains the cytoplasmic tail and alpha subunit the extracellular tail. The homooligomerization into dimers is dependent on intrachain disulfide bonds (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 57652
Sequence Length: 547
Subcellular Location: Cell membrane
|
Q8MI01 | MLTSAKILLISILSSLLLFGSHGEEGQKTNTTESTAEDLKTMENQSVPLESKANLTSDKENRETSNPKASNFSFEDPSNKTHETGFYSNLSTDNSSRSPSLMPTLSPRSPSTHSFVSKLPWNSSIADNSLLPASAPPNTTVPVSSENFTLSSINDTMKAPDNSSITVSNLPSGPNTTSVTPMVTEGWPTTTRESMEGFTVYQETTLHPTLKFTNNSKIFPNTSDPQEENRNTGVVFGAILGAILGASLLSLVGYLLCGKRKTDSFSHRRLYDDRNEPVLRLDNAPEPYDMSFGNSSYYNPTANDSSTSAGGENAHDSIPMDDIPPLRTSV | PTM: Highly glycosylated (N- and O-linked carbohydrates).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35715
Sequence Length: 330
Subcellular Location: Cell membrane
|
Q8N387 | MLALAKILLISTLFYSLLSGSHGKENQDINTTQNIAEVFKTMENKPISLESEANLNSDKENITTSNLKASHSPPLNLPNNSHGITDFSSNSSAEHSLGSLKPTSTISTSPPLIHSFVSKVPWNAPIADEDLLPISAHPNATPALSSENFTWSLVNDTVKTPDNSSITVSILSSEPTSPSVTPLIVEPSGWLTTNSDSFTGFTPYQEKTTLQPTLKFTNNSKLFPNTSDPQKENRNTGIVFGAILGAILGVSLLTLVGYLLCGKRKTDSFSHRRLYDDRNEPVLRLDNAPEPYDVSFGNSSYYNPTLNDSAMPESEENARDGIPMDDIPPLRTSV | Function: May play a role in the cell adhesion to the extracellular matrix.
PTM: Highly glycosylated (N- and O-linked carbohydrates).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 36294
Sequence Length: 334
Subcellular Location: Cell membrane
|
Q8C6Z1 | MLTLAKIALISSLFISLPFARPQKQNPRRNVTQHTIEDVKIMRNNSIHLERSINVTSENGSDISNLMVTTPSPLNLSTTFRTTNSTRTWLMTSSSESSRPSSTYSVPPLVQGFVSKLPLNSSTADANPLQVSEHSNSTNSPSPENFTWSLDNDTMNSPEDISTTVRPFPPPPKTTPVTPFTAEPTEWLPTNNDNFAGFTPYQEKTTLQPTLKFTNNSKLFPNTSDTPKENKNTGIVFGAILGAILGASLLSLVGYLLCGQRKTDSFSHRRLYDDRNEPVLRLDNAPEPYDVNFGNSSYYNPAVSDSSMPEGGESLQDGIPMDAIPPLRPSI | PTM: Highly glycosylated (N- and O-linked carbohydrates).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 36383
Sequence Length: 331
Subcellular Location: Membrane
|
P19670 | MEKLNIAGGDSLNGTVHISGAKNSAVALIPATILANSEVTIEGLPEISDIETLRDLLKEIGGNVHFENGEMVVDPTSMISMPLPNGKVKKLRASYYLMGAMLGRFKQAVIGLPGGCHLGPRPIDQHIKGFEALGAEVTNEQGAIYLRAERLRGARIYLDVVSVGATINIMLAAVLAEGKTIIENAAKEPEIIDVATLLTSMGAKIKGAGTNVIRIDGVKELHGCKHTIIPDRIEAGTFMIAGAAMGKEVIIDNVIPTHLESLTAKLREMGYHIETSDDQLLIVGGQKNLKPVDVKTLVYPGFPTDLQQPMTALLTRAKGTSVVTDTIYSARFKHIDELRRMGANMKVEGRSAIITGPVELQGAKVKASDLRAGACLVVAGLMADGVTEITGLEHIDRGYSSLEKKLEGLGATIWRERMTDEEIEQLQNS | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 46000
Sequence Length: 429
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
|
Q8XH79 | MNRLIINGGKALKGSIEINGAKNAAVAILPAAILASKGECIIDNVPDIADVHCLERIIRSLGCNVEKLDNNTLKINAEEIKTVEACGNDVRKMRASYYFIGALLARFKEAKVELPGGCPIGVRPIDQHIKGFEALGAKVSIEHGAVNIMAEKLIGTNIFFDVVSVGATINLMIAATLAEGTTVLENAAREPHVVDVANFLNAMGANVKGAGTDVIRIKGVKELKGCNYSVVPDQIEAGTFMIAAAATRGDVTIQNVIPKHLESISAKLLEMGAKVEEGDDSVRVYVDGDLKGVNLKTAPYPGFPTDVQQPMCTLLSTAKGRSIIVETIWENRHKHVDELKKMGATIKVEGRSAIIDGVDRLTGAVVKATDLRAGAAMVIAGLISDGVTEITSIEHIDRGYPHIEEKFRMLGADIVRK | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 44533
Sequence Length: 417
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
|
P45025 | MDKFRVYGQSRLSGSVNISGAKNAALPILFAAILATEPVKLTNVPELKDIETTLKILRQLGVVVDRDATGAVLLDASNINHFTAPYELVKTMRASIWALAPLVARFHQGQVSLPGGCSIGARPVDLHISGLEKLGADIVLEEGYVKAQVSDRLVGTRIVIEKVSVGATLSIMMAATLAKGTTVIENAAREPEIVDTADFLNKMGAKITGAGSAHITIEGVERLTGCEHSVVPDRIETGTFLIAAAISGGCVVCQNTKADTLDAVIDKLREAGAQVDVTENSITLDMLGNRPKAVNIRTAPHPGFPTDMQAQFTLLNMVAEGTSIITETIFENRFMHIPELIRMGGKAEIEGNTAVCHGVEQLSGTEVIATDLRASISLVLAGCIATGETIVDRIYHIDRGYEHIEDKLRGLGAKIERFSGSDEA | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 45187
Sequence Length: 424
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
|
P56189 | MDFLEIVGQVPLKGEVEISGAKNSALPILAATLLSRQEVKIKSLPQVVDIKAMALLLQNLGASLEWLNPNTLQIGAKSLNHTEATYDLVRKMRASILVLGPLLARFKECLVSLPGGCAIGARPVDLHLKAMQQLGAKITIEQGYIHAKAPKGLKGNDILFDKISVTGTENALMAASLAKGITRIINAAKEPEIAQLCAFLQSGGVEIHGIGSSELKIRGVENDALNLKDIQIIPDRIEAGTYLCVGAITNSQLKINHIIPNHLQAITDKLIEIGFSLDIQENSIEIHPAKKRQAFEITTKEYPGFPTDMQAQFMALATQCLGTSVIEETLFENRFMHASELQRLGANISLKTNVATISGSTELTGSDVMATDLRASSALVLAALVAKGVSRVHRIYHLDRGYERLEDKINALGAKVARLKEK | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 45657
Sequence Length: 422
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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A1WR98 | MDRLLIRGGRRLHGEVPVSGAKNAALPQLCAALLSAEPVTLLNMPRLQDVSTMLRLLHHMGVGVERSDDGPLRIDAGALHTPEAPYELVKTMRASVLVLGPLLARRGAAKVSLPGGCAIGSRPVDQHIKGLTAMGADIVVEHGDMIARLSAGRRRLKGAHIATDMITVTGTENFLMAATLAEGETVLENAAQEPEIADLAEMLIAMGAQIEGHGSSRIRIQGVDRLHGCSHRVVADRIEAGTFLCAVAATGGDVLLRHGRADHLDAVIEKLRAAGADVQALADGIRVQSPGGAKLKAQGFRTTEYPGFPTDMQAQFMALDCIAQGTATVTETIFENRFMHVDELLRLGARIQVDGKVAVIEGQPRLSGATVMATDLRASACLVIAGLVAEGQTAVERIYHLDRGYDCMEAKLHGIGADIERVPA | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 44934
Sequence Length: 424
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q5GRP6 | MHKILVRSNYKPLVGQIKINGSKNAILPIMAASLLSSSSVVLHNVPDLIDVHLMSELLEGLGAKVNFMHNKDHKANHTLETDCSNINNYAIQYETASKLRASFLMLGPMLSRFGKARTAFPGGCNIGKRPVDMHIKALEEMGAKIEIDGYNIIATVKGKLQGRKITLEKISVGATENIIMAATLAEGVTTINNAATEPEILDLIEFLKKIGADIKINNTKVIITGVKKLNGCIHKIISDRIEAGTYALAAIITNGKLVLEGINLSDIRCIANELEAIGAMVELYDGSIVISRKNGSIKSTNVATDPYPNFPSDMQPQLMSAMCIADGISVIEENIFENRFSHADELRKLGANISIKKNKAAINGIKSLSGANLYATDLRSTAALVLASLVASGETTINNSHHLWRGYEAMHEKLNSCGADISISP | Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 45870
Sequence Length: 425
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q890Y6 | MNHYKDFISNLIENLGSENVKTNELMKNHTSFKVGGPVDILVTPESYEQVQYVIKHSRGNNIPYFIMGNGSNLLVRDGGIRGLVIKFCKLNRIKIEDDKIIAQSGVLLSKVSNMAAKNNLEGLEFASGIPGSIGGALTMNAGAYNGEISQVIDSALVLDKSGEILNLSKEELELGYRTSSILKNGYVVLEAILKLSLGDSKNIYDRIKELTEKRKTKQPLEYPSAGSTFKRPQGYFAAKLIEESGLKGINVGDAEVSQKHSGFIINKGNASAKDILNVINIVQDTVKSKFDVELHTEVLIIGEDKLN | 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
Sequence Mass (Da): 33618
Sequence Length: 307
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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Q47UY2 | MHSNQNYSLKSSNSFNIKASCSRIYFPSSLAELQQLPDLSAGNTSDNFYILGEGSNTLFVEAQAPIIIQPKFNGISIVEQDDHFVVTVGAAENWHDLVCFCLEQGIYGLENLALIPGSVGAAPVQNIGAYGVEFADFCQEIQWYEFASETLHSLTKQACRFAYRDSIFKQERYNKGLITQVTFNFPKAWQANLSYAGLDTLAKESTAKQVMAQVIALRSSKLPDPKELPNAGSFFKNPIVNDADFAQLQQQYPKIPHFPQKNGEIKLAAGWLIDQAGLKGFRHGDVGVHQQQALVLVNYGSELGAEIISLAKYIQQKVAKKFSVSLIPEVRMITHKGERSFSSLSDLNPIENITVIGDSNSIRGSSDD | 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
Sequence Mass (Da): 40623
Sequence Length: 368
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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Q4JSV7 | MTDSTNNAHFTSEERARHLLERLSGTGADSVSIPGTRVTSRSFAEMTTLRIGAAPAGVVECSSAEAVAQVVSFLDAHTQPLLIVGGGSNLVVGEGDEVSQLVVVLMSAGGGEGGVDKKGAAEKSAEGDVMIDRETGVVRAFAGVEWDQLVAATVEAGLGGLECLSGIPGSVGATPVQNVGAYGAEVAQVLRRVQLYDRTRGELEWVDPSALDLGYRYSNLKFTSRAVVTAVEFQLTTDGLSVPLRFGELARRLGVDADEAAAGEIRRPATDVRQAVLELRAGKGMVLDSADHDTWSAGSFFTNPIVTGEEARDAVVAAVREKCGDAEAESMPLYSVKSSGGDASGGGAGASVGEPQYKFSAAWLIERAGFAKGWHVPGNERASLSTKHTLALTNRGSATSADVVELARAVRTGVREAFGVVLEPEPIWVGVSID | 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
Sequence Mass (Da): 45174
Sequence Length: 434
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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Q6A6J8 | MSTTVIGPYEDDDPTEACSTIHHEVIGTTTCLSGGEDVPLAPLTTLKVGGPARHLVIATTHDELLATVRDCDRRGEPCLVLGGGSNVLVGDNGFDGTVVRVATSGLSAEVSSCGGALVTVAAGQVWDDFVVHAIEQEWIGPEFLSGIPGLVGSTPIQNVGAYGVEVGEFIARVRTWDRVDDTQRTFTADQCDFGYRSSRFKAEPDRYVVLDVTMQFNLGTRSLPVRYAELARRLGVEPGERVDTSQVRETVLAVRAGKGMVLNPNDHDTWSAGSFFTNPLVSPDQVPEGAPAFAQSDGRVKTSAAWLIDHAGYGKGFKVAEDAPASLSTKHVLALTNRGGASSGDFTTLARTVIDGVRDVYGITLVPEPRLIGCTI | 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
Sequence Mass (Da): 39916
Sequence Length: 376
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
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A8ZXW1 | MDQGFRQWLTTVFRDRVKWDEPMSRHTTLGVGGPADALVAPETVSELRELIGRCRAQNIAFMVLAGGSNLLVRDRGIRGIVIDMKKYWQTIERHSDRGSGARLTVGAGLTLAALCRYAADNGLAGMTFAVGIPGTVGGAVAMNAGTAEGWMGDVVEAVEMVTGDGRRIRKEKQDLVFSYRRFAVRNDDTATPGPPVITGVDLGLGFDDSEALKAAAEERRRRRTATQPAGFRSAGCFFKNPEAGDPAGKLIDRAGLKGLAVGGAVVSEAHGNFLVNRGNATAGDLLALMETVQRRVADRFGVTLEPEVTIVGQ | 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
Sequence Mass (Da): 33428
Sequence Length: 313
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q6AJ55 | MKEEKKRALSRLVLTPVQWERSLALHTSFAIGGPARALVQVVNEEELAEVVQFLRAEDIAWRVIGRGTNLVVADEGYIGVIILLKGDFATISICPPTGKTVAATVGAGISLSRLCKSCQERGLSGLEFMYGIPGTLGGAVIMNAGAWGGEISDVLLGVSLLSADGIVDISSAEMNFSHRAWQDYEERWPNAVILSARFLLRPVGQEVVKSHCDSVMAKRRLAQPIKQPNAGSFFKNPVGESAGRLIDSCGLKGLTFGKVMVSPEHANFVVNTGGGTSADIRNLMKEVQGTVFRETGISLQPEVHFI | 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
Sequence Mass (Da): 32890
Sequence Length: 306
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
A4J2B3 | MIYTSLAGELQSLVKGSIQINEPMRKHTTWKIGGKADLFLNPSDKEDIRQAVEFAREKAIPITVIGNGSNLLVKDGGIRGLVIKVGRGMAKITIEGTSIKAGAGALLPELAVFACKNSLGGFGFAAGIPGSLGGAIVMNAGAMNGCVSDVLQSIVVLNERNQFEVLTKDHLNFAYRTSNLQSRGLICVETCWQGYAKDQWLIEQETKEYLAKRKAAQPQGFPNAGSVFKNPEGDFAGRLIEGCGGKGLRVGDAEVSSKHANWILNLGRATAQDVLILIDHLKQMVQERFGVLLQLEVKVLGED | 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
Sequence Mass (Da): 32593
Sequence Length: 303
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q1GRY1 | MSATATLPAVRGKLTPQAPLAPLVWFKSGGAADWLFEPKDVDDLADFLRDLDPAIPVMALGLGSNLIVRDGGFPGVVVRLGKAFAKVEPIDATTLRCGGGASGILVSSTARDAGIAGMEFLRSIPGTVGGFVRMNGGAYGGEVKDILVDCDVVLRSGERKTLALADLGYTYRHSELPEGAVVVGATFRGRPGASAAIQAEMDRISASREASQPLRSRTGGSTFKNPAGHKAWQLVDAAGCRGLMVGGAQVSEKHTNFLINTGDATSADIEALGEEVRRRVKDKSGIELQWEIQRVGKAE | 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
Sequence Mass (Da): 31358
Sequence Length: 299
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
P40778 | MTVYHFVGIKGTGMSPLAQILHDNGYTVQGSDIEKFIFTQTALEKRNITILPFSAENIKPGMTVIAGNAFPDTHPEIEKAMSEGIPVIRYHKFLGDYMKKFTSVAVTGAHGKTSTTGLLAHVIQNAKPTSFLIGDGTGQGNENSEYFVFEACEYRRHFLSYQPDYAIMTNIDFDHPDYFSSIDDVFDAFQEMALQVNKGIIACGDDEHLPKIHANVPVVYYGTGEENDFQARNIVKSTEGTTFDVFVRNTFYDTFYIPAYGHHNVLNSLAVIALCHYEEIDSSIIKHALKSFGGVKRRFNEKQLGDQVLIDDYAHHPTEIKVTIEAARQKYPDREIVAVFQPHTFTRTQQFLDEFAESLSGADCVYLCDIFGSARENAGKLTIGDLQGKIHNAKLIEEDDTSVLKAHDKAVLIFMGAGDIQKYMRAYENVMA | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 48365
Sequence Length: 432
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
Q7NI67 | MNMSLDPLVTGEVSHFVGIGGIGMSGLALVLRSQGKRVSGSDLKPNLQTQRLEASGISVFYGHRAENLQGVTRLVYSSAIQPDNPELLAARRGGVAVRHRAQVLAQLAEGYRMIGVSGTHGKTTTSSLIAVMLYHCGLDPTVVVGGEVDELGGNARLGSGPHLVAEVDESDGSLVLFSPEVAVVTNIEGDHLDHYANLEQIVEAFQQYANQARVVVGCLDCQAVRDRMPLTVSYSLDGHPQADYTADRVSFTAQGTTARVLERGEVLGELSLKLLGRHNLANALAAVAVGRYLGLSFEQIAAGLREFRGAHRRFERIGERDDIVFVDDYAHHPSEVRATLAAARLQGRRVVAVFQPHRYSRSQLLLDEFGTAFGDADAVVVTEIYAAGEANTLGVSGELVARRIAAHHPDVHFEATSDSLKRHLEAHLRPGDLALFLGAGNLNRIIPELLQRAEPPALAL | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 49482
Sequence Length: 460
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
P45066 | MKHSHEEIRKIIPEMRRVQQIHFIGIGGAGMSGIAEILLNEGYQISGSDIADGVVTQRLAQAGAKIYIGHAEEHIEGASVVVVSSAIKDDNPELVTSKQKRIPVIQRAQMLAEIMRFRHGIAVAGTHGKTTTTAMISMIYTQAKLDPTFVNGGLVKSAGKNAHLGASRYLIAEADESDASFLHLQPMVSVVTNMEPDHMDTYEGDFEKMKATYVKFLHNLPFYGLAVMCADDPVLMELVPKVGRQVITYGFSEQADYRIEDYEQTGFQGHYTVICPNNERINVLLNVPGKHNALNATAALAVAKEEGIANEAILEALADFQGAGRRFDQLGEFIRPNGKVRLVDDYGHHPTEVGVTIKAAREGWGDKRIVMIFQPHRYSRTRDLFDDFVQVLSQVDALIMLDVYAAGEAPIVGADSKSLCRSIRNLGKVDPILVSDTSQLGDVLDQIIQDGDLILAQGAGSVSKISRGLAESWKN | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 51994
Sequence Length: 475
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
Q2S527 | MAELRTQPALGRIRQVHMVGIGGIGMSSIAEVLLNRGYDVTGSDLERSDVTERLEAEGATIHEGHAAEQVGTADVVVYSSAVDPDENPETREAERRRISLIPRAEMLGELIRMKFGVGVAGTHGKTTTTSMAGLVVAEGGFDPTVIVGGKVTAFGSNAITGEGDVLVIEADEYDRTFLRLTPSLAVITSIEEDHLDVYEDLAAIQASFTQYANSVPFFGAAILCLDDPNVQAIVGDVERRVVTYGTTRQAEVRGENVRREGMTTRFDVVVRGERLGTIELHVPGMHNVRNALAAVAVGQELEISFERVRDGLGTFTGVRRRFEKKGEVGGITVLDDYAHHPTEIEATLDAAHQGFPDRRVVAVFQPHMYSRTQNFMDEFACSFFNADMLVLTDVYGAREAPIEGVTGGRLAERAEQFGHRAVHYVPEKTDLPGRLQELVGPGDVVLMLGAGDIWRASEAFVELLENDGGTAIERD | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 51609
Sequence Length: 475
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
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A4X9R5 | MSGKSAAKFSPAGRLTAEDLGAIHLIGAGGVGMSGLARLFLTRGISVSGSELREWPSLAGLRALGGTIHMSHEVANLDGVDTVVYSSAIPSDHLELVEARRRGLRVLHRSEALATAMTGRRTVAVAGTHGKTTTTSMVTMVLQQAGVDPSFVIGGEISEVGSGAHHGTGDYFVVEADESDRSFLIYRPFVSIITNIEADHLNTYGDLANLEAAFADFARLTDPDGFIITCADDVGGRRLAETLRAEGRRVYTYGISTDADLRLTEMASSTRGIRYLAEIDGRSLGEFRLPVPGRHMGLNSASAVLAEYLLDLPLEAAQSALAAFPGVRRRFERKGVADDVLVYDEYAYHPTPIALALRTLREVAGDGGLIVVFQPYRLYRTRDLQAEIAEALAIADELVLLEVFGPGELREPGEGSAALIEAVPLPVDRKVFVDSWDAAPVEVARRAKPGDVVVTMGAPPSSLMGDQLLDALSRRGAAGPAGTVPGGDVGGATTIGGTIPDIPGGSTPDASAAG | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 54025
Sequence Length: 514
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
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Q6G2Q3 | MISIAFYKGKKVALFGLGKSGLATAQALISGGADVVAWDDNPSGVQAAHRENIPARNLQYENWSEFVALILAPGVPLTYPQPHWVVDKARQANIEIIGDIELFVRARNHFLQQYGFCDEDVPFIAITGTNGKSTTTALLAHLLEQMGYDVQMGGNIGTAILTLKPFVKKRIYVIECSSFQIDLAPSLQPTIGLLLNLTPDHIDRHGSFAHYVNAKKNLVTGASQAFISVDDAACQVLYRQLLHEGHHVEAVSKEHFVENGFYADGTQLFSVCQGRRHMLADLASMAALRGSHNAQNALMALATLQALKITDPHMNKHLASYQGLAHRMQQVRKMGSVLFINDSKATNAEASAPALAAFNNIFWIVGGQAKEAGIVSLRGFFHKIRKAYLIGAAAEEFAGVIGSSFPFSMSLTLENAVHEAAVDAMRCKAKEVVVLFSPACASYDQFKNYEVRGEAFISFVMQLKET | 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
Sequence Mass (Da): 50883
Sequence Length: 466
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q6MIF8 | MYKEYSDLKDKRILVVGLGKTGVSLAHFLTKHGAQVTVTDHKSKPELSVQLEQLGELPIKFELGGHSPKTFIAQDLVILSPGVPSNLKIFDYARSQGIKITGEFEFSAGFIKEPIIGLTGTNGKTTVAKITEAILTESGVKTWVGGANEKPLVDYLRLDDKAQVVIAEVSSFMLEHCDTFNPGNIVFTNLAENHLDRYRSMEEYVNAKRRIFKNTNQATTSILNADDNAVVELARDPAVQRGRIFYFSRKPALEPQIMNIGGAVNIGDEIRVRTGPEIESFNIKGMKMRGKHSVENIMAAILASREHGATREAVQKVINTFTGLPHRIEYVRKVGGVMFYNDSKATNVHAVLRALDTFDENVILIAGGKDTNLNYEPLRTSVKRKVKTLILVGEAKERINRDLGDFSETFLIGTFEEAVLIAYQKSRIGDVVLLSPGCSSFDMFDSFEERGDYFKEIVRKFH | 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
Sequence Mass (Da): 51466
Sequence Length: 462
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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B7GQ76 | MQVADKTVVIAGLGVSGTSLAEVLRERGAHVIGVDERKPEADLRSFDDVDWDHVDYVMSSPVFNPRTPFVLEAQRRGIPVMSEVEFAWQLRVNNERTGTPAPWIGITGTNGKTSTTEMTSEMLTACGLDAPTAGNIASGDMSMSLSRCATNPQHDVLCVELSSFQLHFTDSLALDCAAITNIADDHLDWHGGRENYAADKSKVFHNAKHAIVYNAQDAKVSELAAEAQTAEGCRKVGFTLEAPQAGQIGIEDGWIVDRSGVAGGAVGEPVRLAAITDFTHLAEPDGSLYPHLVADALTALALVLGLGADRDTALKALTSFKPGGHRIETVAEAVVEGGSVRFVDDSKATNGHAARASLSSFPAKSVIWIAGGLAKGSRFEDLVKDQAHTIKAAVIIGKDQQPMIEAFASQAPDIPVTIIDPEDNDTVMDRAVEACGTYAAAGDIVLMAPACASMDQFKSYADRGNRFAAAAKTWSEVHGLH | 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
Sequence Mass (Da): 51034
Sequence Length: 481
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q493Q3 | MRNYRGSKVVIIGLGITGLSCVNFFLDRGVIPKVIDTRIYPPGIKKIPHVVQCYLGAFNDIWLLSATLIVVSPGVRLDHPVLIEALKLGIEIIGDIELFTREATAPIIAITGSNGKSTVTQLVSRMARIAGWHVGVAGNIGVPVLSLLNKSYQLYILEISSFQLDTTYSLRAIAAAILNVSEDHMDHYPGGLKQYWFSKQRIYKNAKICVMNALDFLTIPIYHEYDYCISFGENEDSADYYLKYYKGHTWIVAYNEYVLNCSEMRINNRINYINALSALALSDIIKIPRSVSLKVLCQFSGLAHRCQLIYKNHGVSWINDSKATNVSATKEAINNLKLCGTLHLILGGDGKLADFSSLKHLIKQHEIHLYCFGKDGLLLTTLGFSDVILTNTMIQAMRIINRRIKAKDIVLLSPACSSLDQFKSFEMRGLIFTCFAREFR | 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
Sequence Mass (Da): 49313
Sequence Length: 440
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q0SMS3 | MRLDEIKNLNFLVMGLGLNGGGVALSRFLLKHGAKLVITDLKSEAELALSIDSLRDFDDQIRYVLGKHDVNDFKKADIVVKNPSVRPNNKYLKLAKRVETDISLFLIFNKNPIIAVTGTKGKSTLVSLLYQALKKKYPRVKLGGNIGVSPLSFFDQLDGKSPLILELSSWQLQSLENFNPILSIITNVYNDHQNYYSNFDDYIIDKSKIFVNQTSGIVIIQDKAYYKYFSKFESKAKVILFSEFNPCNLDQDIFYSNKGEVYFNDNLIGSFFESQVVFMIPKLIAFFVAYYLNIDLNHMFQILKNFKGIEHRLEFVKLVRNVMFYNDTASTIPDSTVLSVKSLKTNDNCINLIVGGTDKNLDFSSFSKIINLVKAWILIKGSATVKIINVLEKSSIQYFVFDSLRGAVNYAFEISSPGDIVLFSPASASFELFNNEFDRGLQFKKLVDMLG | 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
Sequence Mass (Da): 51147
Sequence Length: 451
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q7VUQ1 | MNTTETSRAAAPLVLILGLGETGVAAARWYARQGSPLRVTDSRAQPGGLAALQAALADATVEYRLGCGEQFPPDLLDGVAQIVLSPGLVPHESPTRELLEQARERNVEVVGEIELFARALAGLAESREYRPRVLAITGTNGKTTVTALTRQLIEAGGMSARAAGNISPAALAALMDALDQDDLPQVWVLELSSFQLETTRTLAPDAAVVLNVTQDHLDWHGDMQAYAQAKARILKPARLAIVNRDDPLAVAMVESLQALNVRSFGRDVPALVGDMGLELGQGVAWLTACESNDFDEPAPAPRRKKDAPPPTRAGGRMSRLMPVDALRIRGVHNALNALAAMQLARSLDLGWGPMLRTLRDYAGEPHRAELVRSIGDVDYINDSKGTNVGATVAALEGLGQQVVLIAGGQGKGQDFSPLVPVVRRHARAVVLIGVDGAAIGKVLEPTGVPCAAAADMREAVRRAAELAQPGDAVLLSPACASFDMFRNYPHRGEVFAAEVRELALDRGEVA | 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
Sequence Mass (Da): 54070
Sequence Length: 510
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q8F7V4 | MKFPESLKGLKILVLGGGISGNSALNFLISEKAQPILCDQNQPERTVVPFFPDNIPPQSLPEVSLVIKSPGILPTHPILSYAADKKIPVVSEIDLGRYFFKGKIIGITGTDGKSTTTSLIAHLLKESFPDLKEGGNLGIPFTSFCKESISLAVLELSSYQLEDSSPLHLDVSVFLNLASDHLERHKTMENYFQAKLKIADLSNSNHTLIVSEKIKERILNSISYQCKLLSFGKTSDSNAFLDENSLKIKTSKFVYDISKFYLPGTHNRENLAASILAAEEIGGKPESIQTRIPLFRGLPHRFQIAGEKLGISFINDSKSTNLHSMLAGMATWKNIDQTCLILGGRPKQEDLKPLYNFLIRGIGCVVLFGEARATWESGIKNIIGEKLYCVENLNDTFEIFKKGNIFPVPGLNKDIIIRLSDSISISSFVFSPACASFDQYKNFEERGNHFLSLVNDFLDQIDS | 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
Sequence Mass (Da): 51298
Sequence Length: 463
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q03W34 | MQATDFKNKKVMVFGWARSGKAAAQLLTKLGSKVTVVNGGEFDAQDATYRSLLAADVTLIGTDNAETLDSTYDYLIKNPGINYDHPLVQKAEKLNIPILTEVEIALSTFNGRLIAVTGSNGKTTTTSLIRDMLKADGQNVITAGNIGVPVSEVVFDLTREDTLLLELSSFQLLGLPDIQPDIALVTNIFSNHLDYHKTRANYVAAKFRITRHQNANQYLVLNADGQDTEKFKNETEAQVLEFSRTKQHFPVAFSNGNLTLTDEIVMPTKDIKLVGPHNQENILAAVTVANLAGVSKPAIREVLKTFSGVAHRLQYLFTAGDVKYYNDSKATDIEATQTALDSFDCPTIWIGGGLERGDDLERLLPNLKNVKAVIAVGETQQKIVTLAREAGKPVIAVTDVEHAAPVAVQLASPGDVVLLSPAQASWDQYSSFEERGDNFVASLKETLNS | 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
Sequence Mass (Da): 48892
Sequence Length: 449
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q8Y5M1 | MKKIEMYHHKKVLVLGLARSGVSAATIMHKLGAFVTVNDQKPFSENPEAQGLLEQGIKVICGSHPIELLDEGFELVIKNPGIPYNNPMIEKALKLKIPVITEVELAYQISEAPIVGITGTNGKTTTTTIIHHMLNTHKENSSLLAGNIGFPASAVAENATSDQYISMELSSFQLMGVETFKPHISVITNIYEAHLDYHTDRSEYVQAKWHIQKNQIADDFLVINWDQEELKNLTKQTKAQVIPFSTTQRLGQGSYVQNGNIMFNDEVIGERDNILLPGEHNLENVLASVAVAKTLGVTNEEIMHVLETFKGVEHRTQFVVEWQGRKFYNDSKATNILATQSALKGFKNPVVLLAGGLDRGNSFDELLPFFKNVKTLIVFGETADKIGRVGKIAGIEVHYVDNVEAAVPVAYRESAPGDIILLSPACASWDQYRTFEVRGNAYMDAIGELIEEVEK | 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
Sequence Mass (Da): 50431
Sequence Length: 455
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q2W0H5 | MISVPLLKGKRVLVMGLGKSGTATARALLAAGAGVMAWDDGEAARKSGAEAGIPIRDPSLLPLDKADLLVWSPGIPHTHPQPHPLAEKARAANLPMVCDVELLAQALPGARMLAVTGTNGKSTTTTLLAHVLDECGLPVAAGGNLGTAALDLPELPGDGRYVLELSSYQLELTHSLKLGVAILLNVTPDHLGRHGGMAGYIAAKRRVFDFLTPGGAAVVGIDDGPCRAIVAELDRRGIRVVKISVDSVLAEGVSAPEGVLLDNAKPVCDLKTIPSLPGRHNWQNACAVYAAARAEGLSPKQIAQALATYPGLAHRQELVGEDHGIAWINDSKATNADAVEKALVCYDHVYWILGGQAKEGGIASLEKHFGRIQHAFLIGEATEAFAATLDGKVRFTRCATLDKAVAAARNLAVSDSIPGAVVLLSPACASWDQFTSFEHRGDTFRELVQAFDQGGAA | 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
Sequence Mass (Da): 47788
Sequence Length: 457
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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A1U3G0 | MSVIVSDRRTLIVGLGKTGLSCVRYLSGQGREIAVADSRLQPPGLDELKAGWPDVPVYLGDFDEALFAGFNELVVSPGISIAEPAIAGAAARGARIRGDIDLFADAADAPIIAITGSNGKTTVTTLVGEMARAAGRNVQVGGNIGTPALDLLEQGADLYVLELSSFQLETTEELGALAATVLNVSDDHMDRYPDKMAYFQAKQRIYRGCKNAIVNLDDALSTPMARDTLRFLCFGFNRVNPETFSTRDDDEGTWITWGLENLLLASELQLMGRHNISNVMAALALGYAAGLAMEPMLEVARRFRGLPHRCESVRNLDGVDYINDSKGTNVGATVAAIESLVPESGKVILIAGGDGKGADFQPLAEPVAACCRALVLIGRDAGKISRAVGASVPQHRATSLQEAVSLARQAAEPGDRVLLSPACASFDMFRDYNDRGEQFRTLVEGL | 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
Sequence Mass (Da): 47530
Sequence Length: 446
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q604V5 | MHDRLIDENPTCGFVRLGLDVRSRVIVLGLGATGLSTVRFLRCHGFECAVMDSRLAPPGLQDLREAFPDVPLFLGDFSRSALAAATHLVVSPGLSLDLAEIRESHRCGVRVFGDLDLFACCVRAPVVAITGANGKSTVTTLVGLMAKAAGVNAAVGGNLGTPMLDLLDAAAELYVLELSSFQLERSELFEADVATVLNISPDHMDRYPDLASYAEAKRRVFRGEGLMVLNQDDPLVAAMYRPGRRAVRFGLGSGDELDYSLARWEGRAWLLAKGVPLLPADEVRIKGRHNLANALAAVAIADACGFDRQAMVGVLRTFPGLDHRMQWVADIGGVAYVNDSKATNVGACIAALSGLEGKVVLIAGGDGKGADFSSLVPVAAEKLRAAVLMGRDGPLIDEVLKGVVPTIRVKTMFEAVRAARGVAQSGDTVLLAPACASLDQYEDYQERGRDFAATVRSLA | 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
Sequence Mass (Da): 48786
Sequence Length: 459
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q9WY76 | MKIGFLGFGKSNRSLLKYLLNHQEAKFFVSEAKTLDGETKKFLEEHSVEYEEGGHTEKLLDCDVVYVSPGIKPDTSMIELLSSRGVKLSTELQFFLDNVDPKKVVGITGTDGKSTATALMYHVLSGRGFKTFLGGNFGTPAVEALEGEYDYYVLEMSSFQLFWSERPYLSNFLVLNISEDHLDWHSSFKEYVDSKLKPAFLQTEGDLFVYNKHIERLRNLEGVRSRKIPFWTDENFATEKELIVRGKKYTLPGNYPYQMRENILAVSVLYMEMFNELESFLELLRDFKPLPHRMEYLGQIDGRHFYNDSKATSTHAVLGALSNFDKVVLIMCGIGKKENYSLFVEKASPKLKHLIMFGEISKELAPFVGKIPHSIVENMEEAFEKAMEVSEKGDVILLSPGGASFDMYENYAKRGEHFREIFKRHGGDEV | 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
Sequence Mass (Da): 49154
Sequence Length: 430
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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B0K8K5 | MELKGKKVLVAGLGVSGIALCKVLDSLKAKVIAYDEKEYDVLKENLEEIKSLSIDFRFGKFKKEFLEGVDLVVLSPGVPTDSDIVKTAQEKKIELLGEVEFAYRFSKAPIYAITGTNGKTTTTSLLGEMFKNTGRKVYVAGNIGYPLIYAVMEAAEGDFIVAEISSFQLETIKEFKPKISCIINITPDHLDRHKTFENYRDIKGRIFENQREDEYTVLNYDDPVTWSLKNKAKCRVFPFSRKSLLENGAYIKDGSIYISVNGNAEKIIDIEEIYIPGEHNLENALAASSVAYLSGISADVIANTLKTFKGVEHRIEFVDEINGVKFYNDSKGTNPDASIKAIQALKTPIVLIAGGYDKGSEFDEFVKAFNGKVKKLILIGQTAKKIRDTARKYSYPEDDILFAGTLEEAVKKAYESAKEGDSVLLSPACASWDMFRNFEERGRIFKKAVAELRR | 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
Sequence Mass (Da): 50721
Sequence Length: 454
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q3SMH5 | MNYDALQLSGRKVLVLGLGDTGLSCARWLSVHGADVSVADSREAPPHAARLAETLPQVALFTGPFEAAHLAAADMLVLSPGVPLSEPAVAQAVAQGVEAVGDVELFARALAVLNAQRAALPAPQAAMRVIAITGSNGKSTVTAMCGDMCRMAGLTVCVAGNIGLPVLDALHEIEQGAAPLPQVWVLELSSFQLETTSSLDATAAAVLNLSEDHMDRYPDMAAYAAAKARIFSGNGVQVLNRDDPRTLAMAIPGRHVVSFGLDRCPTDENFGLCEDELCLGGDMLMPLSVLAVPGLHNAANALAALALTRALDLPIEALLRGLMHFKGLPHRVEKVADIDGVTWYDDSKGTNVGATEAALYGMGRRKAVVILGGDGKGQDFGPLKAAVAANARAVVLIGRDAVAIEAAIEDSGVASYRADTLPDAVEQAARLAEPGDAVLLSPACASFDMFRNYVHRAEVFVDAVKKLAAQRAQV | 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
Sequence Mass (Da): 49390
Sequence Length: 474
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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O83873 | MEQARALLQGKTVTIMGLGVHGGGCAAACFCAEAGARLTVTDLRNADALTPSLKRLRAYPSIRFTLGEHRLEDFENAHVVIKNPIVKGAHNIYLSAAQRAGARIETDISLFLRLSPAPLLAVSGSKGKSSTASALCYSLRALGFPAFLGGNSTVSPLEFVRHTTPATPVVLELSSWQLADLRAVDAQDHTVHHAGLLRPEIAIMTPIMADHQNWYADMESYVADKQVLYAHQGTHDTLLCNADDGWGPRFACEAQKNGVRVFWYTAQSPETACRACTPRLMERALWRATDGTYWARFAEGDRACMLIPPQLHVPGRVLQTQVASAALAALLFAQRHSLPPSSCPPCFCAHSHSPAYANHASPPDYACPSAHSPFQEHTRRLAQALESYTGIEHRLEFFYEKGGLRFYNDSASTVPEATIAALEAFDESVVLIVGGTDKNADYQPLAQAAAKAHALYLLAGSATARLQPLLHAAQVPFYGPFTSLEVLLQDLRARQKSPGVIVFSPGAASFELFAHEFERGTTFKSQVRIIFE | 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
Sequence Mass (Da): 57848
Sequence Length: 532
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q83GN2 | MSRVEGLTSWYSDWQGLSAAILGIGVSGFAAADSLRELGVDVTVYAPEKHTRYNKLLDAIGARYVCAYLDELCEVDVDFIVVSPGISPDNPVIKRLRDRQIPILSEIELAWRVRDKVNTCPWILITGTNGKTTTALLTGSMLAKDGARVAVCGNIGTPVLDAVRNPKGFDYLVVELSSFQLSLLPMHGNGAVKGFSSACVNLDEDHLEWHGAKELYYCAKSRVYHGTTGFCVYNLDDEETKKMVEQACVARNVRAIGFGLCVPDVGQVGIVDGILCDRAFLSARKDSALEITSVEKLEKNKLSMRHIISDVLCAVALARSVETNPLSISRALDEFCLSPHRTEVVAKEMGVMWVNDSKATNPHAVIASLSNFSRVILIFGGLMKGVDVSGIFDRFYETIKAVVVIGKNQSFVGNIKCKKIVCIPDSNDPMSEAVAAADLLATPGDTVLLSPGGSSFDQFESYEHRGNCFINAVKDLVKRK | 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
Sequence Mass (Da): 52236
Sequence Length: 480
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q0AYR3 | MKLVELIKNLTIELQDGPLDREISGIAYDSRRVKPGDLFICISGLKSDGHLFAGQAIENGAVAVLAERQLDTGGKATLLTTPDTRSALALLAANYYGRPSKSIRVVAVTGTNGKTTTTDLIKAILEEAGKKTAIMGTLYAQVGEIQREMQHTTPEALEIESFMALCREEKADYIVMEVSSHALQLQRVAEIDFNVAVFTNLTQDHLDFHQNMDNYRAAKLQLFQMIKEEKQNYAIINIDDPWAEEIFQAATIPCRSYGIKKRSDYQAGELKIDLDGSSFRLHYGDNSLMINMKLIGLFSIYNALAAISFALQEGIDPGLIQSALARVEGVPGRFEKVDCGQDFAVIVDYAHTPDGLENILQTSRELGKKRLICVFGCGGDRDRSKRPLMGEIAAKYSDFCVVTSDNPRSEDPHAIIAEIIPGMDKVEKSRYAIIVDRREAIRHAIHLARTGDLVVIAGKGHENYQLVKDQVLEFDDRKVAAELLRGKVK | 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.
PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Catalytic Activity: ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 54176
Sequence Length: 489
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.13
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Q1QVG7 | MSYREVSRVLIMAGGTGGHVVPALSLARALRARGVSVEWLGSPRGIENRLVPAADIVLHRIQVAGLRGNGMAGWLLAPWRLAKAVWQARQVIAKFDPQLVVGLGGFASGPGGLAAWLMRRRLIVHEQNAVAGMTNRYLSRLADGVYAAFPGAFGAHRAEVVGNPVRDDIAALGETPRGSDALRQRPLRLLVLGGSLGAQALNTQVPQALARLPAAQRPDVRHQAGRDKETATQSVYAEAGVEAEVSAFIDDMAAAYDWADLIVCRAGALTIAELAAAAKPSILVPFPHAVDDHQTLNARQLVDAGAARLMPQTQLTAESLAETLATLLEPETLATMATSARAQARLDAVERLVAGCMEANRDSQ | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38561
Sequence Length: 364
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q7NPZ9 | MANRTVMVMAAGTGGHIVPGLAVAKELQSRGWKVVWLGTRRGMENKLVPPTGIPLERLNFHGVRGKGLLGSLKGALQLAGAFFSSAAQIFRHRPDVVLGMGGYVCLPGGVMAGLLWKPLVLVNADAGLLLSNKALLPFASKLVCGFDGSAARGPKALVTGNPVRGEIERIAAPAARFAGRSGPLKVLVVGGSLGAKVLNETLPQAMARLPAEQRPQLTHQTGEANFAAVEAAYQAAGLRQQVELLPFVDDMPKRLAECDLVICRAGAITVSELCAAGVPSVLVPLVVSTTSHQRDNAEWMAQAGAAWHLPQKELNADGLAGLLAGLDRDQLLDKAERARALARSGAAGRVADLCQQLAGE | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37605
Sequence Length: 360
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
|
A5CS51 | MTVYLLAGGGTAGHVNPLLAVADELRAREPGSTILVLGTREGLESRLVPARGYELLTIARLPFPRRPDGAAVRFAPAFARAVGQIRRMIAERGIDVVVGFGGYAAAPAYAAARRPGVPVVVHEANASPGLANRLGARVAAAVGITFPGTALGPRAEVVGMPLRREIATLDRAAVRDAARAELGLDADRPTLLVTGGSTGARSLNRTVVQVAERITATGAQILHIVGGAQEFTDPGVERYHVVGYSDRMELAIAAADLVVSRAGAGALSELTAVGVPAVYVPYPVGNGEQAVNVRGVVAAGGGIVVADADFTPDWVLAHVLPLLSDPAALARMSQAAASVGTRDGAARMADLVRDAVAARPSRPAARR | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37714
Sequence Length: 367
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.227
|
Q182Y6 | MMKVLLSGGGTGGHVYPAIAIANKIRDEHPDAEIIFVGTEKGIESEIVPKYGFELKTVTVQGFKRKIDFDNVKRVFKLFKGLEQSRKIVKKFKPDIVIGTGGYVSGPVLFNASMGKIPAIIHEQNSFPGVTNKILSKTVTKVLTSFEDSHKRFPEAAEDKLVFTGNPVRKEILLSRKNIARKNLSISDEKRMVLCYGGSGGSRKINDAMRLVIKNMVNEDIAFIFATGKSYYDEFMGSISDINLKPYQKVVPYLEDMANALAASDLVIGSAGAISLAEITALGKPSIIIPKAYTAENHQEYNAKSIEKQGAGIAILEKNLTPESLNTAVFKLLGDRELLVDMANASKTIGKPEAIDLIYDEIMKVYNSTQKSTSKKTKKEKVIKEVKEIKKETTPSIEGQAKVIGIKKR | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45006
Sequence Length: 409
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.227
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A0L5N1 | MNNTPRRLLIAGGGTGGHLFPALAVAERWRERYGLHSVHFIGGQRGLENRLVPNAGFTLETLAVGQLKGKGLPHKLRTLGGLLPAVWQARGMVQRFDPHVVLGVGGYASAPAMVAARSLGIPMALHEQNARAGLTNRLLSHLAQQVLVSFNGVCAQFPGRACQLTGNPVRQALAAVPPLQIPTLFTPQRPLRILVFGGSQGASIFTQRVPEALLPLAQHGAPIQVTQQVQEADADALQRRYQEGGIEAITTPFIEDMATAYAQADLVICRSGATSVAELAATGRPSIMVPYPYAADDHQAANAQALVSIQGGWMRRQEQFHSAWLEAFITSLCMQPAQLQRAGEIARSYARPNADMQIVTLLASMVKMKR | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39832
Sequence Length: 370
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q2W0H3 | MSTQKPLIALAAGGTGGHVFPAEALASVLLDRGYRLALITDKRGAAYGGTLGKLETFRISAGGIAGRGKLSALRSALELGLGLIQARSILGRIRPAAVIGFGGYASVPGMGAAALAGIPTAIHEQNAVLGRANRLLAGHVRRIATSFAEVSHVEPKLAPKLVHTGMPVRAAILASRDASYAGITAEGPIELLVLGGSQGARILSEVIPAALARLPEALRTRIRIAQQCRPEDLEGVRRAYDGTGIDATLDSFFADVPERLARAHLVIARAGASTVAELTTLGRPAILVPYPFAVDDHQTANAHAAEDCGGAWLMQQDSFTADSLAARLDSLFTHPEALVRTAVCARNVGRPDAAEALADLVVGLIPNESGA | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38403
Sequence Length: 371
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
|
Q0AMW7 | MTPRRCLIAAGGTGGHMFPARAAAEALIARGWQVRLVTDARGLRHATDFPAVAVDEIHAASPSTKNPLKLARAALELTQGFAQARSIVGKWKPDVIAGFGGYPAFPALAVARSMGIAFAIHEQNAVLGRVNRVFAAKAGFVASGFERLDRLPAKAKKRHILTGNPLRAPILAARDAGYPAIDADGRLNILVLGGSLGARILSETVPQALAMVPEKLRSRLDVVQQTREESLPMARETYQAAGIAAQCEPFFEDVGSLYAASHLVIGRAGASTVSEVAGVGRPAIFCPLAIAADDHQSANVDGLVQAVACDVVHEGEFTAQKIAALIETRLSNPDDLASRAQSARALGRPDAADALARAVDGLVTGALV | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38460
Sequence Length: 368
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
|
C6BYG6 | MKRIVLTTGGTGGHVFPALAVAHEIKNRFPQCEILFIGGKGPEREMVERAGISFKGLPAKGVLGGGIKKVFSSLWIVSAMIMALKEIASFKPDAVIGFGGYAGFCPVLAAWLLGVPTAIHEQNSVPGVTNRILGKVVKRVFASFEDRNGSFPAAKTVVVGNPVRKEIIDSGNCADTKTVLVFGGSQGAAAINDAVIDGLAKLKEAGISLRHQTGKADFEKVRKGYEQNGMDTGKVSPFIHNMGEAYAEASLVVCRAGASTVFEVAAAGKPAIFIPFPHATHDHQTGNARSLADLGAAELIPQAELGGNRLADEIIKLIADQDRLKGMGSKALSFARTDAASAIAEGVGDIIRMKTVRGAA | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37687
Sequence Length: 360
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
|
Q1GZ01 | MSKTLLIMAAGTGGHVMPGLAIAKTMQSRGWNVHWLGTTHGMENRLVPPSGLPMTLLKFSGMRGKGWKHTLLGMFRLVGATWRAWRLMRELQPQAVLGMGGYVTVPGGWAARLAGVPLAIVNADAALLMSNRALVKHAKRVLFGFDGGAATLGGMAFKARVTGNPVRAEIVEIASPEQRFADRQGPLRVLVVGGSLGAQVLNATLPKALALLPAEQRPIVTHQSGAQHIDALREAYAAVGVQAHVVPFIDDMASAYADADVLVCRAGAITVSELAVAGVASILVPLVVSTTSHQRDNARWMAEHGAAIHLPQQEMTPQRLALLLQELTRTRLLAMAHAARELGRPMAAETIANELESIALPVQGGKHS | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39080
Sequence Length: 368
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
|
B1ZGP4 | MTVFTPLVLVCAGGTGGHLFPAQSLAYALKARGIRVALATDARVDSIAGDFPAEEIVTIASATPSGRSMLRRAGAVLTLGRGFGQAARAVRRLNPAAVVGFGGYPTVPPMLAAQLLRVPTILHEQNAVMGRANGFLAKGAQVIATGFKEVRGVPEKATARRIHTGNPIRPSVLAVAETPYPALDEGSPLRLLVFGGSQGARVMSEIVPAAIEKLPQDLRARLHLVQQARPEDLTATQNRYLAMGLGGIEAAPFFKDLPGRMAAAHLVVARSGASTVSELAAIGRPAILVPLPGALDQDQAANAATLAQIGAALSIPQSAFTPDRLAAELVDLFEAPRKLTQAAAAAKTARILDAADRLATLVAETAAATS | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38248
Sequence Length: 370
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
|
Q2RK79 | MRVIITGGGTGGHVYPALAIARGLKEARPGVELLYIGTARGLEADVVPRAGLTLATITVQGLVRRQVWKNIPALVKTGRGLGEAWQQVRRFRPDVVVGTGGYVSGPVCLAAALQGVPVILHEQNAFPGVTNRLLAILARCVCLTFPEAASRFPRRAKLVTTGLPVRPEIIQADRDSCRQHFGLRPEQLFLVTVGGSQGARSINGAMLPILKELAGCQDVSLLQVTGRRDYEAYLQQVRTQGIDLAKYGNITIEPYVYNLEQALAAADLVIGRAGASFLAEVLARGLPSVLVPYPHAAANHQEYNARAVARQGAAVVVLDRELKGGRLYQVVFELLRSREKLKAMAAAAASLGRPGALEAIIQVILKTVESG | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39696
Sequence Length: 371
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.227
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Q1JG11 | MPKKILFTGGGTVGHVTLNLILIPKFIKDGWEVHYIGDKNGIEHTEIEKSGLDVTFHAIATGKLRRYFSWQNLADVFKVALGLLQSLFIVAKLRPQALFSKGGFVSVPPVVAAKLLGKPVFIHESDRSMGLANKIAYKFATTMYTTFEQEDQLSKVKHLGAVTKVFKDANQMPESTQLEAVKEYFSRDLKTLLFIGGSAGAHVFNQFISDHPELKQRYNIINITGDPHLNELSSHLYRVDYVTDLYQPLIAMADLVVTRGGSNTLFELLAMAKLHLIVPLGKEASRGDQLENATYFEKRGYAKQLQEPDLTLHNFDQAMADLFEHQADYEATMLATKEIQSPDFFYDLLRADISSAIKEK | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40401
Sequence Length: 360
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.227
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B9DY32 | MDSEDRPIGFFDSGVGGISVLKEAVKILSNENFVYFGDSKMAPYGVRTVEEVKKLTFNAVEFLLKKNIKALVVACNTATSAAIIDLRKAYSKYMPIVGIEPALKPAVECNRKGNIIIMATPMTLAESKFNNLMKRYSNSNILPLPCSGLVELIEEGKTEGEEIERYLEEKLIPLKGNGIAAVVLGCTHYPFIKKSISKVLNQDVLILDGSKGTVRQLKRQLIKYHIESNKSKIGKIKIFNSMNSQYIIKLSYKLLKE | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 28641
Sequence Length: 257
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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