ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q60367 | MIGIIGGTGIAEILKGDKEEIINTKYGKARVIIDKENEVVLLFRHGVRHNIPPHKINYRANIYALKKLGVERILAINSVGSLKEDLKPGMFFVPNDFIEFTKKREETFYDEGKVVHIDMTDPYCPELRNILKSILDKNNFSYGEGVYVCTEGPRFETKKEIAIYKNWGDVVGMTGYPEVVLARELEMCYVSLCNITNYACGISKNILTVDEVLEKIKEMENKILKVVEDFINYGFGERKCICKDALKHAVIG | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
Catalytic Activity: phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Mass (Da): 28664
Sequence Length: 252
Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.44
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O27633 | MIGIIGGTGIYEMAEYGRLERRGSLITPYGKTPEISVFKLHGRRVAFIPRHSPGHDKPPHMVNYRANIWALKELGVRQIIATNAVGSLKRSIGPGDFVVPHDFLDFTRSRPSTFYDEKTVHVDMTEPYCRNIRSALSGSSGVVDGGVYVCTEGPRFETPAEIRMFQTLGGTVVGMTGLPEAVLARELEMCYASICLVSNYAASISPSKLTIDEVFEIMDEKKNDLIDIIDAAIRDLKTEQSCPCQHALRGADVNNHEEELYEGFNDICKPEKEEQHHDGP | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
Catalytic Activity: phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Mass (Da): 31100
Sequence Length: 280
Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.44
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Q9HZK1 | MSVYAIIGGTGLTQLEGLTLSESLPIETPYGAPSAPLQRGRYAGREVLFLARHGHPHRFPPHQVNYRANLWALKQAGAEAVIAVNAVGGIHAAMGTGHLCVPHQLIDYTSGREHTYFAGDIEHVTHIDFSHPYDEPLRQRLIEALRALGLAHSSHGVYACTQGPRLETVAEIARLERDGNDIVGMTGMPEAALARELDLPYACLALVVNPAAGKSAGIITMAEIEQALHDGIGKVREVLARVLAG | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine. Involved in quorum sensing.
Catalytic Activity: phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Mass (Da): 26266
Sequence Length: 245
Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.44
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B1WQH2 | MNTIYPVIWSNNKVLLIDQTSLPSRYTLVEISRYEDMAKAIKTMIVRGAPAIGVAAAYGMYLGARDIQTQDRETFLKHLDKIAQILRQTRPTAVNLFWAISRMLKTAYETLGTVEEIKKILLETAQKIQEEDLQTCQAIGHNSLSILPTNPEKLTILTHCNAGALATAGYGTALGVIRSVWTAGRLNRVFADETRPRLQGAKLTAWECVQEKIPVTVISDNMAAHCMQKGLIDMVVVGADRIAANGDTANKIGTYGLAVIAKMHQVPFYVAAPLSTVDFSLETGDLIPIEERDPSELYQIGNTVIYPDGVDYYNPAFDVTPADLITGIITEQKTVNPKELITLKG | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 37939
Sequence Length: 345
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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P0CN40 | MVAAAPSNKERLPDMMTSIRLDQSGRVEIIDQLLLPHSVVWMPVSTPEEAFDAIKTMRIRGAPAIASLAALTLRSYLSSSSSPVSSSSSSSDVISWVGQTIDYLQSSRPTAVNLGEAMDRIRAALKDSEAQNQTAGDIIQRVKKICGDVHDEDLERNMKMGRLGAEWLWKKRGGGKKGLKVMTVCNTGSLATSGYGTAIGVITALFQEDHLDTAYYAQTTPYHQGSRLTSLELTTLQIPACMICDTMLGSLFQHEDIDGVIVGADRVVKNGDTANKIGTYQAAVLAQRHNVPFMVVAPVTTIDLSLPTGAEIHIEHRPAAEATQVRGLDTETGKLSVVRITPEGVGEGDKPWQRVYNPSFDVTPAELISAVVTEKGVAERKEGEKSIDVASIC | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 42378
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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A9JRE2 | MTLEAIRYRSGSLQILNQLLLPRETVYDEIRSVRDGYEAIKSMKVRGAPAIAIVGCLSLAVELRAGAGAEDLVSFVRDSLCHLTSARPTAVNMGRAARELMEFTENESMEKNTEQLRDSVIGWIEEMLERDVNDNKKIGNYGAQHILSGVPRDSVTILTHCNTGSLATAGYGTALGVVRSLHMLGRLKRLYCTETRPYNQGARLTAYEAVAEGFPATLITDSMAALAMREKSITAVVVGADRVVANGDTANKVGTYQLAIAAKHHGIPFYVAAPSTSCDLSLESGRDIVIEERPAEELTSINGVPVAAPGIDVWNPAFDVTPHQLITGGIITELGVFLPSELQAALTGRLTAL | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 37980
Sequence Length: 353
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Subcellular Location: Cytoplasm
EC: 5.3.1.23
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Q47AR7 | MNIDGIPTRTLRAHPDRRAIDIIDQTRLPHALHWVRVATLEEAAHAIRAMQVRGAPLIGATAAYGLAIALDFEASDRRLAEAVALLGATRPTAVNLHWALARMENILRPLAPEARCDAAWAEAAAIAEEDVAQNAAIGQHGLKLWNDLIVADGQTLNIMTHCNAGWLATVDWGTALSPVYAAHDAGVPVHVWVSETRPRNQGLLTAWELEQHGVPHTLIADNAAGLLMRNGKVDAVIVGADRIAANGDVANKVGTYLKALACADNGIPFYVAAPRSTLDFACPEGASIPIEERDGDEFRLVHGLDSRGVPSALRQLPAGEDVANPAFDVTPNWLVKAIITERGVCPASRDGLLALYPEEARG | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 38703
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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B8J4S7 | MDDHIRFDHQTFELHLLDQRLLPAQEADFVCRSVEDVVYALQTMVVRGAPAIGVTAAWGCVLALREAQGPDWAARLEQGMERIAAARPTAVNLRWAVERMRGVWLAAGGEAGDPAPLLTAFAHAAQTMQDEDVAVCKTLGRHGAACIEDGDCVLTHCNAGALATAGYGTALGVIRAAVEAGKKVSVIADETRPFLQGARLTAWELERDGIPVTVACDNACALLMSRGLVQRVVVGADRIAANGDTANKIGTYGVALLARHFHIPFYVAAPLSTIDPATPDGAGIPIEERPELEVTHMGETRLCPENVPVLNFAFDVTPAEYISGIITEKGVLYPPYGLSIWAALNDLSTGRSAGISAGPLRDEDDAPDAEPDWSRERS | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 40338
Sequence Length: 378
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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A8ZYA5 | MTATDPAPTRPIWLADDKKRVQIIDQRMLPHNLVIVDLTTVDQVIEAIGEMMVRGAPLIGVTGAFGVFIAVQNALERGDFEAQVRKECLRIKEARPTAVNLAWGVDRVCAAVFSKTLPADCLAAALAEASAIAEEEVDNCRRIGVHGVGLIETISRQKGGKTVNVLTHCNAGWLACVEHGTATAPIYKAFEKRIDIHVWVDETRPLNQGARLTAWELGQRGVAHTVITDNAGGHLMQHGMVDMVIVGTDRSTYTGDVANKVGTYLKALAARDNNIPFYVALPSSTFDWEMTDGLAQIPIEERNPDEVRCVEGLCPDGRVEKVRIVPENSRAANYAFDVTPARLVTGFITERGVCGAGRDQVLALFPEKR | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 40202
Sequence Length: 369
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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Q4ZQ92 | MRDRLLAAEKVKAIDWRDDALYLLDQRVLPFEEVWHRYTTAEGVAEAIRTMVVRGAPAIGISAAYGAVLAARARIAQGADWYPALEEDMQLLADSRPTAVNLFWALNRMRDRLMRVKDGDDPLAALEAEAVAIHLSDREANLTMAQLGADLIRKHQGNLQTVLTHCNTGALATGGFGTALGVIRAAHLEGMIERVYADETRPWLQGSRLTAWELANEGIPVTLNADSAAAHLMRTKGITWVIVGADRITANGDVANKIGTYQLAVAAMHHGVRFMVVAPSSTIDMEMASGDDIVIEERDGRELLEVGGQRVGAEVEAFNPVFDVTPADLIDAIVTEKGIVERPDTARMAQLMSRKHLH | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 39087
Sequence Length: 358
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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Q9UZ16 | MEVRYKPEELTKLPRSVEYKERTVYMINQRLLPREFKVEAFRTVESVAEAIKNMTVRGAPAIGAAAAFGLALYAETSKAKSKDEFMDGFYKAYETLKNTRPTAVNLFWALNRIKKLVEEHLEDPLDEIKSLIVNEAQKIADEDVEANLRMGHYGAEVLPEGNLLTHCNAGSLATVHLGTVGAVVRVMHKDGSLKLLWLDETRPVLQGARLSAWEYSYDGLNVKLIADNAAAFVMQQGLVDAIIVGADRIVANGDFANKIGTYMLAVLAREHGIPFFAVAPLSSIDMSLKSGKEIPIEERSPEEVLTCGGCRIAPDVPVYNPAFDVTPHKYVTGIITDKRVVWPPFKRNLKKLFGEQ | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 39549
Sequence Length: 356
EC: 5.3.1.23
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Q7UF90 | MNEAETIRYHAAHNGRPAELDLLDQTKLPGTLTRLVCTTIDQTHDAIQRLVVRGAPAIGIAAAYGVTLTPVDAESNSSLPEAQARYRQTIDYLATSRPTAVNLFWALDRMRAIVDDFSGPVAELRERLVTEAIRIHDDDRQMCRSIGCHGATLLADCKSVMTHCNAGSLATSMWGTALAPMYHLHESGHSLEVFADETRPLLQGARLTAWELHQAGIPVTVCTDSMSGSLMRQGRVDAVIVGADRIAANGDVANKIGTYPLAVLAKYHNIPFYVAAPTNTFDSELESGDLIPIEQRSADEVSYPCGTDSPRQTPEGVAVVNPAFDVTPAELVTALITEKGVISEPDTAKVRAHLGL | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 38390
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
EC: 5.3.1.23
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A4W7Z4 | MTDNLQLTHLVDACRWIGAKGWAPATGGNMSIRQNDAFCWLSESGKDKGSLTIDDFLQVDIASNRAPSGRKPSAETGLHTLIYRLFPEANAVLHVHTVNATVLSRLVKETELRISGFEMQKSLTGQSTHLDTVTIPVFDNDQDIDALASRIAHYAQERPFNYGFLLRGHGLTCWGRDVAEARRHLEGLEFLFECEMRLRQLEKI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 22910
Sequence Length: 204
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
EC: 4.2.1.109
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A9H8G1 | MISTDPWAGAVQDIIAAGRRMDRFGWVPATAGNISRRLPDGRIAITRSGGHKGHLTADGVIEVTADGRAVRAGDRPSAETLLHCHVYEASPDVGAVLHGHSVASTVLSMMEQGDAILLSGYEVLKVFEGQQTHDTTVRLPVFDNDQDIARLSGVVAPYLGRMPAGYVIRGHGVYVWGGTMDVALARLEGLEFLLACELERRKVAR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 22053
Sequence Length: 205
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
EC: 4.2.1.109
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Q0BPT9 | MTGTVTSVRQPPEWAAVTIVAAGQRMDARGWVPATAGNISVRLPDDTIAITSSGNHKGFLKTSDIMVVDQAGKPLTPGLKPSAETLLHCQIYRLDNQAGAVVHGHSVAATVLSMAPGKNDAPPDFIRLEGYEVLKAFGVKTHQITLDLPILDNDQDMERLASIAEPILLRGAPLGYLIRGHGVYVWGGDMAAALARLEGLEFLLACELERRRLR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 23025
Sequence Length: 214
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
EC: 4.2.1.109
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Q2SKZ2 | MFDLHKFSLRAQEIIEAGGFLYGAGWSPATSSNYSARIDDANIAITVSGKHKGRLQAQDIMVVDLQGRAVASQMKSSAETLLHTVIYDLKPNVGAVLHTHSVTATVLSRALRPNTEIVFEDYELQKAFRGVYTHEGRCVVPIFDNTQDIEALSALSVEYLKEHSDCPGYLIRGHGMYTWGETMAECLRHVEAMEFLLACELEMMRIKS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 23183
Sequence Length: 208
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
EC: 4.2.1.109
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Q96GX9 | MSGCDAREGDCCSRRCGAQDKEHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPSPSKKLKKSQCTPLFMNAYTMRGAGAVIHTHSKAAVMATLLFPGREFKITHQEMIKGIKKCTSGGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGLDPSQLPVGENGIV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death.
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 27125
Sequence Length: 242
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Subcellular Location: Cytoplasm
EC: 4.2.1.109
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C4R7D9 | MSSCFCSKSQETEKRGAVSEDQLVISDDSTHPANLICELCKVFYNNGWVTGTGGGISIREGSKIYIAPSGVQKERMVPDNMFVMDLESENYLRTPLTLKPSACTPLFLSAYKMRDAGACIHTHSQAAVMVTLLYDKVFEISSIEQIKAIPKVTEKGNLMYSDRLVIPIIENTEREEDLTDSLQQAIEEYPGTTAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELALKMHQLGIPTVKQN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 26874
Sequence Length: 240
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Subcellular Location: Cytoplasm
EC: 4.2.1.109
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Q4WDE1 | MKAYWYDNKPGDQREPHDSGRPVTVDYLASIGVQYYHFPSLESVNELAKERGYKNRDEIVVSPQAMGDVYEEKVKMFFNEHLHEDEEIRYIRDGEGYFDVRGQEDEWVRIKLAKDDLIILPAGIYHRFTTDDKNYVKAMRLFQEEPKWTPLNRGPDVDENSHRQSYLRTIQNKTVA | 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. 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.
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)
Sequence Mass (Da): 20848
Sequence Length: 176
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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O31669 | MATIRIHDEANTTIENQEEVASFLDSQEVIYEQWDITRLPEHLSEKYDLTEEEKQQILDTFETEIKDISTRRGYKAQDVISLSDSNPKLDELLENFKREHHHTDDEVRFIVSGHGIFVIQGQDGTFFDVRLNPGDLISVPENIRHYFTLQEDRKVVAVRIFVTTEGWVPIYEKDSVNQ | Cofactor: Binds 1 Fe(2+) cation per monomer.
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. 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.
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+)
Sequence Mass (Da): 20824
Sequence Length: 178
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.
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Q3ZBL1 | MVEAWYMDEAADDPRLPHRAEPARPVGLEQLRRLGVLYWKLDADKYENDPELEKIRKERNYSWVDIITISKDKLPNYEEKIKMFFEEHLHLDEEIRYILDGSGYFDVRDQEDRWIRISMEKGDMITLPAGIYHRFTLDEKNYVKAMRLFVGDPVWTPYNRPSDHLEARTQYLEFLAQSA | 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. 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. Also down-regulates cell migration mediated by MMP14.
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21487
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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C3ZAH2 | MVRAWYMDDSDADQRAPHMTDPPQPVELDQLKNIGVLYWQLSGNEDDETLAGIRKDRGYSYNDLIEITPEKLPNYEQKIKTFFEEHLHLDEEIRYCVGGSGYFDVRDKGDKWIRIEMEKGDLIVLPAGIYHRFTLDEKNYIKAMRLFVGEPVWTPYNRPADDKDARKEYLKTMGLAA | 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. 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.
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)
Sequence Mass (Da): 20723
Sequence Length: 177
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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A5EES7 | MTQLIVYEAGNPSHVLLQTSDFDVIAGKVAALGARIERWEARHPIAPGASNEEVLSAYGHEIDRLKRERGYTNGDVVRIKPGNPNWPELRGKFLQEHVHVEDEVRFFVEGTGAFYLHLDDKVYQLVGEAGDLLSVPHGVKHWFDGGPEADFTCIRLFTNQEGWVAHFTGDAISDAFPKYEIAA | Cofactor: Binds 1 Fe(2+) cation per monomer.
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. 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.
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+)
Sequence Mass (Da): 20442
Sequence Length: 183
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.
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Q59WJ5 | MVEFYFHDNKDTLENFTEDHNSGEPVSFDQLAEIGVIYKYITTQEELDALATEREYKNRDVVTLNLPAFNNDIDAYNAKMQQFYKEHYHEDEEIRYIAEGEGYFDVRDKQDRWIRAKLSPYDLLILPAGIYHRFTLTNAAKHVKAVRLFKDEPKWEAINRDTGKNTEARELYAKTIAV | 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. 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.
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)
Sequence Mass (Da): 21008
Sequence Length: 178
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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F6W3G8 | MVRAWRILQEETDDPRDALYSDESVSLEQLAQVGVEYFKFDADTFEQNDDYLKLKNNRGYSYSDTISVSRATLPDFDAKIKSFFEEHLHTDDEIRFILDGSGYFDVRDLDGRQLRDCWIRIECVKGDLLVLPSGIYHRFTLDKKDYIKALRLFIGVPVWTPHNRPADSMKERLDYVSKYLTATT | 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. 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.
Catalytic Activity: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)
Sequence Mass (Da): 21565
Sequence Length: 184
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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O32028 | MRLAVIGAMEEEVTILRNKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELDGIQVAKGTIATGDSFMNDPKRVEEVRARFSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRIH | 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 (By similarity).
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
Sequence Mass (Da): 25265
Sequence Length: 231
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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Q1LTN6 | MIIGVIGAMEQEVMLLSKQLAKLNIWQQARCNIYSGWLHGKKVVLVQSGIGKVSAALGCTLLLTNFEATLVINIGSAGGLSPALAVGDIIVSEEVQYHDVNVTAFGYDKGQMAQYPLLFPASPSLVALTKQLTEHTNINVVCGQIISGDIFINGGQELYKLKRRFPQAIAVDMEVTAIAQICYLFAVPFVGIRVITDIADSVSHKSFKDNLITVVSHLSLLVSDIIQAL | 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): 24698
Sequence Length: 229
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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P57306 | MKIGIIGAINQETERLKKIIHFYIEKKINTYKIYIGKFKSHDVFLIKSGIGKVSASVATMILIDLYKPDTIINSGSAGSLQSFLKIGDIIIPKKTCYYDVDLTNFGYTRGQIPGYPKEFTVNEKICNFFKKNADKYQLKYIKGLILSGDTFVRENESIKILKKQFPSAIAVEMESSAIAQVCYKFNIPLIIIKSISDESDNNATVNFKENIDFVSYQLSKFVKIILENLIDM | 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. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
Sequence Mass (Da): 26344
Sequence Length: 232
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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Q89AQ7 | MKKEIKKNYRIGIIAALQQEVQILFNKLKNYKINKISNITFYIGNIHNIHVVLAKSGVGKVFSGITCALLLQKYKVKFIINIGSAGSLNKNLKPGSIIIPTNVCYHDVNLTAFGYSIGQIKNCPKTFLSNTLMLKLTEKYLFENKIKYQKKLMISGDIFIDTCEKKSLLKKRFPKAIAVDMEAAAIAHVCYQFNIPILIIKSISDSSDINAADNFKYFINLASKNSSLVTINVLQTLFKNTKNILFDNNNRC | 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. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
Sequence Mass (Da): 28426
Sequence Length: 252
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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Q6AQW7 | MKVGIIAAMEEELTLLVDRLDNCEEVQLGHCKYYTGQINGVEVGLMRCGIGKVNAAIGTTLMIDKLKPKCLINTGVAGGFINEMNVGDIVISSSVRHHDADATAFGYELGQIPDMPSEFQADRRLVEMATKVNLKSKARIFEGPVFSGDSFIHTTEQVENILKNFPQIMAVEMEGASIAQTSHLFNIPFVLIRSISDKVRETKSADTYTQSMEESAKNSVQVVFEMVEQLKEGM | 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): 25783
Sequence Length: 234
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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Q819E7 | MSIQVFCDFDGTITNNDNIMSIMEKFAPPEAEEVKNKILSQELSIQEGVSQLFQLIPTNLHDDIIQFLIETAEIRSGFHEFIQFVKENNISFYVISGGMDFFVYPLLQGIIPKEQIYCNETDFSAEFITVKWPHSCDDHCQIHCGLCKSSLIRKLSDTDDFHIVIGDSITDLQAAKQADKVFARDFLITKCEENHIAYTPFETFQDVQAELKLLLEVKA | Function: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25042
Sequence Length: 219
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
EC: 3.1.3.87
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O31667 | MTTRKPFIICDFDGTITMNDNIINIMKTFAPPEWMALKDGVLSKTLSIKEGVGRMFGLLPSSLKEEITSFVLEDAKIREGFREFVAFINEHEIPFYVISGGMDFFVYPLLEGIVEKDRIYCNHASFDNDYIHIDWPHSCKGTCSNQCGCCKPSVIHELSEPNQYIIMIGDSVTDVEAAKLSDLCFARDYLLNECREQNLNHLPYQDFYEIRKEIENVKEVQEWLQNKNAGESSLK | Function: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 27002
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 4/6.
EC: 3.1.3.87
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C0ZL41 | MSKKLVLFCDFDGTITEKDNIVAIVRKFAPPEWEALTEQILSQKISVQEGVGKLFQLLPSSLRQDIIDFIVHEATIRPGFAEFVSYCREEGIELLITSGGIDFFLEPILAPFDLADVPIYCNGSDFSGERITITWPNACDEHCTNGCGMCKTTIIRRYDPATHFRIVIGDSITDLAGAKIADYVIARSFLADKAEELQLPHSTFATFHDVIRILQQVQQEVV | Function: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 24846
Sequence Length: 222
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
EC: 3.1.3.87
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C4KZ51 | MSTHVICDFDGTITEEDNIIALMRRFAPPEWVELKDSVLNQTLSIREGVGQMFSLLPSNQQERYREFLQSTITLRAGFVEFLQETQSHGFRFDVVSGGMDFFVHPILEGHVAPEHIFCNHVDFSGETARVTWPHACDVHCLNDCGCCKPTIARQIVSPTDTLIVIGDSVTDFEIAKRADVVYARGQLISLCEAEGIRHVPFETFYDISAYMKGVNV | Function: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 24319
Sequence Length: 216
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
EC: 3.1.3.87
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Q5L1E1 | MTKQLVLFCDFDGTITENDNIIAIMKQFAPPEWEALKDDILAERISVQEGVGKMFSLLPSSLKGEIIDFLRRTTRLRAGFREFVAFTKERGIPLYIVSGGIDFFVYPLLEGLIEPERIFCNGSDFSGETIRITWPHACDGECQNGCGCCKPSLLRKLARPDGYHVVIGDSITDLAVAKQADYVMARDFLLQKCQELGLPHAPFATFFDVIDALQRMEVIV | Function: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 24690
Sequence Length: 220
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
EC: 3.1.3.87
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B1HYT5 | MKPIIFCDFDGTITETDNIFSLMTEFVPQESEKIAKAMMEQTISFKDGLSAMFHLLSTEQKDEVIQYLMDTAVIREGFEDFVRYAQNHDIPFYIVSGGVDFFIEPLVEKYGPFSGIYCNKADFSGEQIKLIYSNSCDEECAKYSTQGCGCCKPSVMRKVAKEEHFKIVIGDSLSDFEAAKQADIVLARDHLIQRCEELHVSYKPFITFHDCLKIVQELMETNHAVPTT | Function: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25970
Sequence Length: 228
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
EC: 3.1.3.87
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B0JX47 | MSKIVFCDFDGTITAVETFAGMLKEFAPDLSAQIMPQMYARTLTLRRGVRQLLESIPSQKYADILAYAESKPIRPGLAEFLAFLQEQSIPFIIISGGIQGMIETVLKREGLLDKVTAIYGVNLHTQGEYLQVHSDWENETELVAKALIMAKYSGVETIAIGDSVTDITMARRADLVFARDRLIDYLQAENQPYIPWDNFFEIREYLLLRD | Function: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 23806
Sequence Length: 210
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
EC: 3.1.3.87
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P24581 | MFKIIDLFAGIGGIRLGFEQAFDDVRCVFSSEIDKYAVQTYQANHGGETVCGDITQTDVADIPDHDILSAGFPCQPFSQAGLKKGFADTRGTLFFDIERILLAKKPQAFLLENVKQLKGHDKGRTLQVILAHLQQAGYKVYTEVLKARDFGIPQNRERIYLVGFLNHDVDFRFPQPIGQATAVGDILEAYPDEKYTISDKLWQGYQRRKAENRAAGKGFGYGLFNAESAYTNTISARYYKDGSEILIEQPGKNPRKITPPEAARLQGFPDSFQIPVSDAQAYRQFGNSVCVPVIRAIAEQMKAALSAVSDRKV | Function: A methylase, recognizes the double-stranded sequence 5'-CCNGG-3' and methylates C-2 on both strands. May be the equivalent of dcm in this bacteria, or it may protect the DNA from cleavage by the putative NlaXP endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34843
Sequence Length: 313
EC: 2.1.1.37
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Q2FRN2 | MANKKSPASGWPIVQGDFHTGDPNSPVAVVTMGSHLDEGAICSAGAAIAGSCKTENLGLEKVIANVISNPNIRFVITCGTEVKGHLSGQSLIALHQNGVDGGKIVGSKGAIPFIENLSADNIKRFQEQVELVDIMESEDLGAISAKIKELTARDPGAFDAEAMIVEIKEEGGGAAEEGGEVRPMSAEVALIHARMKTIQRTITDIGFYDKYAAGVYGGKVEGLMIGLIVSFVIIGLLLVGHGVS | Cofactor: Binds 1 5-hydroxybenzimidazolylcobamide group.
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: Single-pass membrane protein
Sequence Mass (Da): 25425
Sequence Length: 244
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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Q58261 | MANKREPAPGWPIVSGEYVVGNPESCVGVVTLGSHGLEQACIDAGAAIAGPCHTENLGIEKVVANYISNPNIRFMILCGSEVQGHITGQCFKALWENGIGDDGGIIGAKGAIPFLENVNKEAVERFRRQIVEVVDLIDCEDIGKITQAIKECLSKDPGAIDEDPFIIELEGGKGGGEEEEGVIKPITPEMAIIESRMRLIGNEMCYNGLLAKWQAGYYNGKIQGIATGLFLMLLIMGILMF | Cofactor: Binds 1 5-hydroxybenzimidazolylcobamide group.
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: Single-pass membrane protein
Sequence Mass (Da): 25880
Sequence Length: 241
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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O32867 | MPEKAEPAEGWPVVEGDYVVGDPEAPVHVVTLGSHIEEDILKAAGEDKVAIAGPCKTENIGIEKVIANVIANPNIRFGVLCGAEVTGHLTGQCFKAMYENGVDPDSGEIIGAEGAIPYLENIPEEAVERYRDQIVELVDLIDVEDVDEIVKAIEECVEKDPGAYEEGPMTISLEEEEEEELAEVAGMPVSAETVTVEYRINDVRVGVKSIGAMQRYMAGYLSGRTMGLLIGIISGMIFLFLPMVVLGGV | Cofactor: Binds 1 5-hydroxybenzimidazolylcobamide group.
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: Single-pass membrane protein
Sequence Mass (Da): 26762
Sequence Length: 249
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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O59640 | MADKREPAPGWPILKGEYEVGDVKNSVLVITCGSHLPGKPILDAGAACTGSCKTENLGIEKVVAHIISNPNIRYLLVTGSEVKGHITGQSMMSLHANGVKENRIAGALGAIPYVENLNAAAVARFQEQVQVVNLLDTEDMGAITSKVRELASKDPGAFDADPLVVEISEEGEEEEEGGVVRPVSGEIAVLRSRLKAIEARMMDIGNLNKFHSGVHAGKVEGAMIGLTITISLLGLLLLGR | Cofactor: Binds 1 5-hydroxybenzimidazolylcobamide group.
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: Single-pass membrane protein
Sequence Mass (Da): 25366
Sequence Length: 240
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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Q2NI29 | MADKKEVIQNWPLETGDYAVGNVESPVAVVSLGSNMNDELVAAGAAISGPLHTENLGIEKVVANIISNSNIRYVLICGSEVQGHITGKTVEALYENGIDEEKKSIIGSPGAIPFVENLPVEAVERFQKQVSIVSMINNEDVSEISSKIDECISNDPGAYDEDAMIVEFNETPEEEFEVDEVTFSDDSAVDLASIVLLEVENRISMMNNEIKQIASLEKISSGYYAGKIEGIVIGFILTLVFLIIIIQGL | Cofactor: Binds 1 5-hydroxybenzimidazolylcobamide group.
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: Single-pass membrane protein
Sequence Mass (Da): 26969
Sequence Length: 249
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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A0QTK2 | MDTMRQRILVVDDDPSLAEMLTIVLRGEGFDTAVIGDGSQALTAVRELRPDLVLLDLMLPGMNGIDVCRVLRADSGVPIVMLTAKTDTVDVVLGLESGADDYVMKPFKPKELVARVRARLRRNEDEPAEMLSIGDVEIDVPAHKVTRQGEQISLTPLEFDLLVALARKPRQVFTRDVLLEQVWGYRHPADTRLVNVHVQRLRAKVEKDPENPQVVLTVRGVGYKAGPP | Function: Member of the two-component regulatory system MtrA/MtrB, responding to environmental signals (Probable). Controls expression of a number of genes including dnaA, ripA, fbpB and probably itself. Probably plays a role in cell division.
PTM: Phosphorylated by MtrB.
Sequence Mass (Da): 25318
Sequence Length: 228
Subcellular Location: Cytoplasm
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P0AAD2 | MATLTTTQTSPSLLGGVVIIGGTIIGAGMFSLPVVMSGAWFFWSMAALIFTWFCMLHSGLMILEANLNYRIGSSFDTITKDLLGKGWNVVNGISIAFVLYILTYAYISASGSILHHTFAEMSLNVPARAAGFGFALLVAFVVWLSTKAVSRMTAIVLGAKVITFFLTFGSLLGHVQPATLFNVAESNASYAPYLLMTLPFCLASFGYHGNVPSLMKYYGKDPKTIVKCLVYGTLMALALYTIWLLATMGNIPRPEFIGIAEKGGNIDVLVQALSGVLNSRSLDLLLVVFSNFAVASSFLGVTLGLFDYLADLFGFDDSAVGRLKTALLTFAPPVVGGLLFPNGFLYAIGYAGLAATIWAAIVPALLARASRKRFGSPKFRVWGGKPMIALILVFGVGNALVHILSSFNLLPVYQ | Function: Involved in the transport of tryptophan into the cell.
Catalytic Activity: H(+)(in) + L-tryptophan(in) = H(+)(out) + L-tryptophan(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44333
Sequence Length: 414
Subcellular Location: Cell inner membrane
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P44614 | MIQQKSPSLLGGAMIIAGTAIGAGMLANPTSTAGVWFIGSILALIYTWFCMTTSGLMILEANLHYPTGSSFDTIVKDLLGKSWNTINGLSVAFVLYILTYAYITSGGGITQNLLNQAFSSAESAVDIGRTSGSLIFCLILAAFVWLSTKAVDRFTTVLIVGMVVAFFLSTTGLLSSVKTAVLFNTVAESEQTYLPYLLTALPVCLVSFGFHGNVPSLVKYYDRDGRRVMKSIFIGTGLALVIYILWQLAVQGNLPRTEFAPVIEKGGDVSALLEALHKYIEVEYLSVALNFFAYMAISTSFLGVTLGLFDYIADLFKFDDSLLGRTKTTLVTFLPPLLLSLQFPYGFVIAIGYAGLAATIWAAIVPALLAKASRQKFPQASYKVYGGNFMIGFVILFGILNIVAQIGANLGWFASFTG | Function: Involved in the transport of tryptophan into the cell.
Catalytic Activity: H(+)(in) + L-tryptophan(in) = H(+)(out) + L-tryptophan(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45018
Sequence Length: 418
Subcellular Location: Cell inner membrane
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P9WHH2 | METYDIAIIGTGSGNSILDERYASKRAAICEQGTFGGTCLNVGCIPTKMFVYAAEVAKTIRGASRYGIDAHIDRVRWDDVVSRVFGRIDPIALSGEDYRRCAPNIDVYRTHTRFGPVQADGRYLLRTDAGEEFTAEQVVIAAGSRPVIPPAILASGVDYHTSDTVMRIAELPEHIVIVGSGFIAAEFAHVFSALGVRVTLVIRGSCLLRHCDDTICERFTRIASTKWELRTHRNVVDGQQRGSGVALRLDDGCTINADLLLVATGRVSNADLLDAEQAGVDVEDGRVIVDEYQRTSARGVFALGDVSSPYLLKHVANHEARVVQHNLLCDWEDTQSMIVTDHRYVPAAVFTDPQIAAVGLTENQAVAKGLDISVKIQDYGDVAYGWAMEDTSGIVKLITERGSGRLLGAHIMGYQASSLIQPLIQAMSFGLTAAEMARGQYWIHPALPEVVENALLGLR | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the NAD(P)H-dependent reduction of mycothione (the oxidized disulfide form of mycothiol) to mycothiol.
Catalytic Activity: 2 mycothiol + NADP(+) = H(+) + mycothione + NADPH
Sequence Mass (Da): 49946
Sequence Length: 459
EC: 1.8.1.15
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P38680 | MDSQYETKKNDPNAIMPYPESNDEHVGEVRGLGGGIMDKEPEAQEGHAKFHRLGWKRLTVVLIVEAIALGSLSLPGAFATLGMVPGVILSVGMGLICIYTAHVIGQTKLKHPEIAHYADVGRVMFGRWGYEIISFMFVLQLIFIVGSHVLTGTIMWGTITDNGNGTCSLVFGIVSAIILFLLAIPPSFAEVAILGYIDFVSICAAILITMIATGIRSSHQEGGLAAVPWSCWPKEDLSLAEGFIAVSNIVFAYSFAMCQFSFMDEMHTPSDYKKSIVALGLIEIFIYTVTGGVVYAFVGPEVQSPALLSAGPLLAKVAFGIALPVIFISGSINTVVVSRYLIERIWPNNVIRYVNTPAGWMVWLGFDFGITLIAWVIAEAIPFFSDLLAICSALFISGFSFYFPALMYFKITRNDAKSQGKKYFLDALNMLCFVIGMGILGIGTYAAIQDIMDRYDHGKVSKPYSCAPLA | Function: Required for the transport of neutral aliphatic and aromatic amino acids via the N system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51162
Sequence Length: 470
Subcellular Location: Membrane
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Q02DS7 | MSSSPAQTPSRRPSLLGGSMIIAGTAVGAGMFSLPIAMSGIWFGWSVAVFLLTWFCMLLSGMMILEANLNYPVGSSFSTITRDLLGQGWNVVNGLSIAFVLYILTYAYISGGGSIIGYTLSSGLGVTLPEKLAGLLFALAVALVVWWSTRAVDRITTLMLGGMIITFGLSISGLLGRIQPAILFNSGEPDAVYWPYLLATLPFCLTSFGYHGNVPSLMKYYGKDPQRISRSLWIGTLIALAIYLLWQASTLGTIPREQFKGIIAGGSNVGTLVEYLHRITASDSLNALLTTFSNLAVASSFLGVTLGLFDYLADLCRFDDSHFGRFKTALLTFVPPTIGGLLFPNGFIYAIGFAGLAAAFWAVIVPALMARASRKRFGSPLFRAWGGTPAIVLVLLFGVANAVAHILASLHWLPEYR | Function: Involved in the transport of tryptophan into the cell.
Catalytic Activity: H(+)(in) + L-tryptophan(in) = H(+)(out) + L-tryptophan(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44742
Sequence Length: 417
Subcellular Location: Cell inner membrane
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D8RLD3 | MAVSSIASIFAAEKSYSIPPVCQLLVSPVLNPLYDAKAESQIDAWCAEFLKLQPGSEKAVFVQESRLGLLAAYVYPTIPYEKIVPVGKFFASFFLADDILDSPEISSSDMRNVATAYKMVLKGRFDEATLPVKNPELLRQMKMLSEVLEELSLHVVDESGRFVDAMTRVLDMFEIESSWLRKQIIPNLDTYLWLREITSGVAPCFALIDGLLQLRLEERGVLDHPLIRKVEEIGTHHIALHNDLMSLRKEWATGNYLNAVPILASNRKCGLNEAIGKVASMLKDLEKDFARTKHEIISSGLAMKQGVMDYVNGIEVWMAGNVEWGWTSARYHGIGWIPPPEKSGTFQL | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Sesquiterpene synthase converting farnesyl diphosphate to eight sesquiterpenes, with (+)-germacrene D and an unidentified oxygenated sesquiterpene as the major products. Has no diterpene synthase activity.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate
Sequence Mass (Da): 38990
Sequence Length: 348
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.77
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B6SCF3 | MSLSGVPLSAGLAPSPSNKPTNGKGQNIVRRSGNYKPALWDYDYLQSLPTLYAGEAHVEKLNKLKGEVRIMLEKTVTENPLAQLEQIDTLYRLGISYHFQDEIKALLNTIHNNNNNNNNNDDVYATALEFKLLRLYGYTVHSEVFNVFKDEIDKGFKAISLCGDYVKGMLSLYEASFYSFKGETILDEARDFSTKHLQKYVMMRHNNNSKDQSVDDDDDLVILVEYALELPMHWRMIRLEAKWFIDVYSKRRDDMNPTFLELAQIDFNLLQSTYQEDLKHVSRWWSTCKLGERLPFCRDRLVEVFLLAVALKYEAEFGYARRLLTKIGVLVTLMDDIYDVYGTLDELKLLEDAIERWNINELDQLPEYMNIFFVAMYNVVNGIAYDVLKENEILIVKYLKRAWMDACKSYMVEAKWYYSGYTPSLEEYLENGLISITIPLDLIFLYCLTTSPITEDSMEYLLQYPTILGLSGTLFRLVDDLATSSDELKRGDNPKSIQCYMHESGVCENDSREYIKNLISETWKQMNEVRVAKSPLFSQAFIESAVDFVRGAMLLYQKGDGFGTKHDGDAKDKLVSLFFNPIPTP | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Sequence Mass (Da): 67511
Sequence Length: 585
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Subcellular Location: Plastid
EC: 4.2.3.-
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Q6YSY5 | MPVLPWLAAAATTPVRRSPPLPATPRALLRLPASSFPPWSNCAKSGLPPRGPFATAADTPLGGSLPEPEEERDTLLDGALRAARFRDEESRRPDPLFIDPYAAVLLSLDVASEDKDLLALHLMPSAEHYRLVTRYIDDKLQHFISNSDDLRQIVLLTDGMDTRPYRLSWPRLSVVYDVSPRRVFITASQQLRGAGAKISRNCVVLHTSSESPDLQAGLNKNGFNGNRPSLWVLQGLPLFTFKSLEDLLLVIGNLAMKGSIFIGEVPRFTQWGAATDMASEQDRLENLFFTQGFRVSFVHYEEVAKDVGLGLDSPPEIHGRAIFIAEQLRFSDAQMESFRMHFERIEDDADEDGFEEL | Function: Involved in melatonin biosynthesis . Can function as acetylserotonin O-methyltransferase . Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine) . Involved in the regulation of jasmonate- and brassinosteroid-mediated plant growth and defense responses .
Catalytic Activity: N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39828
Sequence Length: 357
Pathway: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.
Subcellular Location: Plastid
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P09795 | MIMNDIITVTEAAQLLELTPQRVRTMCKQGSIDAYQSGRTWLIKSSSVEKLMLVNSLSDAQNSYSMLASEPKNKPKALSFFSGAMGLDLGIEQAGFETLLASEIDKAARDTILSNRPNMALIGDIRDYTTEDILKLAGVSSGNEIDLIMGGPPCQAFSTAGKRLGLEDERGNVFIKYLDVALDIRPKYIVIENVRGLLSAPMKHRPHNERGEGLPPLKSEEQPGGVLHYIIRIIKSAGYSVSFNLYNSANFGVPQIRERVIIICSRDGSRVPFLQPTHSEKGEYGLPKWITLRETITNLKNITHEHVLFPEKRLKYYRLLKEGQYWKHLPEDLQKEALGKSFFLGGGKTGFLRRVAWDRPSPTLVTHPAMPATDLAHPDELRPLSVQEYKVIQQFPEEWVIKGKLLDKYRQLGNAVPIGLGLAVGKNILDHMNGRKIESFPNFRYSRYKNTSDLDIFGELV | Function: A methylase that recognizes the double-stranded sequence 5'-GGWCC-3', methylates C-4 on both strands, and protects the DNA from cleavage by the SinI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51767
Sequence Length: 461
EC: 2.1.1.37
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O31073 | MNHELPVISLFSGAGGLDCAIESCAEPPLVQDGSGSPLRVAVATDYEQTALDTLSANFPHTKTLCGDIQTIPTAELLEAGGLKPGDPTLVIGGPPCTPFSKSGFWIEEKRNSADPNASLLDEYVRVVRESKPEAFILENVQGLTYKTHQAQFDRLIAGLKDAGYNPTFRVLLAAEYGVPQLRRRVFVVGRRDGKAFHFPETTHSGESERDRVIDHTKIPFTSLREALAGLPDVPEAGEVVEGTYAELAAEVPPGQNYLWHTDRYGGRNEFKWRSRYWTFLLKADPDRPSTTLQAQPGPWVGPFHWENVKNANGEERARRFRVAEMKRIMTFPDEFVFTGVKREVQRQIGNPVPVELGKVVVRALMEQLGYLDSRGTTIPSQAGHEQLELI | Function: A beta methylase recognizes the double-stranded sequence 5'-GAGCTC-3', methylates C-4 on both strands, and protects the DNA from cleavage by the SacI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43293
Sequence Length: 390
EC: 2.1.1.37
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Q53609 | MHSEAREAEARRLLLQETLDAERTFLERNQWGQFATPPSLAGEIMRYTIDLHEETRINFLEPSCGSGSFFSALLRNLGDKKIEHAVGVELDPRFSKAASDLWTGQGLRVIEGDFTSPSLVSGPVASLLVANPPYVRHHHLGIDQKRDLVARCADQLGIKPSGLSGLYLYFVLLSHRLLRADAVSTWLIPSEFMDVNYGTALKEYLATRVQLVRIHQYDAAEVQFDDALVTSSVVVFRNSPPRPGHTAEFSFGGTLSEPKVTHQIPSAALTPEAKWSRYVTGVMPADINLKQTGPKLSDFFKIRRGLATGSNAFFIIPRSEAERLGIKRNFLRPILPSPRKLKGDAITADASGWPDIPEQLALLDCPLPIEDLLLENPALAAYLSTADEKIRGGYLVSKRSPWYKQEQREPAPILLTYMGRGKDDQHPLRFIRNDSDAVATNMYLMLYPTALLQRYLAGDPERIKQVHKALLAITAADLRGGGRVYGGGLHKMEPKELAALPADGIATLDPVLREDISMVSVPPRKRTGRPQMPGPSASEVRAWARANGVCVPDRGRLRPEVWDAWRQAHAGEASPLNIDAGDQVALW | Function: A gamma subtype methylase that recognizes the double-stranded sequence 5'-GTCGAC-3', methylates A-5 on both strands, and protects the DNA from cleavage by the SalI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 64975
Sequence Length: 587
EC: 2.1.1.72
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O52692 | MSGRDFGYVIQSSAALWNRLSTFSQRGKALDTRLADIKKALGKPYYETSDVLLYHGDSLELLKSMPQQIFDLTVTSPPYNIGKEYEGVLSIEEYISWCETWMSRVHRATSAGGAFWLNVGYVPVPNQGKAVPIPYLLWDKSPFYMIQEVVWNYGAGVASRKSFSPRNEKFLWYVRDPLNYYFDLDSVRDPNVKYPNQKKNGKLKCNPLGKNPTDVWQFPKVTSGAKRSSVERTAHPAQFPSAVIERVIKACSPSDGVILDPFLGSGTTSLTARKQGRCSVGIEIREDYLDIAVGRLEAEAQSLF | Function: A methylase that recognizes the double-stranded sequence 5'-AGTACT-3', methylates C-5 on both strands, and protects the DNA from cleavage by the ScaI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34187
Sequence Length: 304
EC: 2.1.1.113
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O64471 | MEGDQETNVYTLVARKPSFDLPTACPNCLPAYIYLKLAQLPFELAFNSTFPDSDELPYFESDTYVAYNNEDGGVIEKLKKDGIVNLDSQLQSLSDYLSLKALIVSWLEEALTYEIWVGTEGISTSKIYYSDLPWVISKVLFYKQTYLAKNRLGITKENAEQREKQIYKRASEAYEALSTRLGEQKFLFEDRPSSLDAFLLSHILFIIQALPVTSVLRCKLLEHSNLVRYAEKLKSEFLEASSSSPSPPLHSFPSSFPRKSSKPKSKPKVEKTEEEKKFKKRARFFLAAQFLAVVIYVSVMGGGSSDELEYEDEDD | Function: Involved in transport of proteins into the mitochondrion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35854
Sequence Length: 315
Subcellular Location: Mitochondrion inner membrane
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P43121 | MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRPLKEEKNRVHIQSSQTVESSGLYTLQSILKAQLVKEDKDAQFYCELNYRLPSGNHMKESREVTVPVFYPTEKVWLEVEPVGMLKEGDRVEIRCLADGNPPPHFSISKQNPSTREAEEETTNDNGVLVLEPARKEHSGRYECQGLDLDTMISLLSEPQELLVNYVSDVRVSPAAPERQEGSSLTLTCEAESSQDLEFQWLREETGQVLERGPVLQLHDLKREAGGGYRCVASVPSIPGLNRTQLVNVAIFGPPWMAFKERKVWVKENMVLNLSCEASGHPRPTISWNVNGTASEQDQDPQRVLSTLNVLVTPELLETGVECTASNDLGKNTSILFLELVNLTTLTPDSNTTTGLSTSTASPHTRANSTSTERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITLPPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH | Function: Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 71607
Sequence Length: 646
Subcellular Location: Membrane
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Q9EPF2 | MGLPRLVCAFLFAACCCCRSATGVPGEEKQPTPTPDPVEVEVGNTALLKCGPAHPSGNFSQVEWFLIHKERQIPIFRVHQGKGQSEPGEYEHRLSLHGPGATLALSQVTPHDDRMFLCKSKQPRPQDHYVQLQVYKAPEEPTIQANVLGIHVDIQELKEVATCVGRNGYPIPQVIWYKNGRPLQEEENRVHIQSSQTVESSGLYTLKSVLSARLVKEDKDAQFYCELSYRLPSGNRMKESKEVTVPVLYPAEKVWVEVEPVGLLKEGDHVKIRCLTDGNPQPHFTINKKNPSTEEMEEESTDENGLLSLEPAQKHHSGVYQCQSLDLETTVMLSSDPLELLVNYVSDVQVDPTAPEVQEGDSLTLTCKAESNQDLEFEWLRDKTGQLLGKGPILQLNNVKREAGGRYLCVASVPSVPGLNRTRRVSVGIFGSPWMAAKERKVWAQENAMLNLSCEASGHPQPTISWNINGSATEWNPDPQTVVSTLNVLVTPELLETGAECTASNSLGSNTTVIILKLVTLTTLTPDSSQTTGLSTPTVSPHSRANSTSTEKKLPQQESKGVVIVAVIVCTLVLAVLGATLYYFYKKGKLPCGRSGKQEITLPPTRKSEFVVEVKSDKLPEEMALLQGSNGDKRAPGDQGEKYIDLRH | Function: Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 71327
Sequence Length: 648
Subcellular Location: Cell membrane
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Q8WML4 | MTPDIQAPFLSLLLLFPVLTVANVPTLTTSDSINPRRTTPVSTTQSSPTSSPTKETSWSTTTTLLTASSPAPSPAASPGHDGASTPTSSPAPSPAASPGHDGASTPTSSPAPSPAASPGHDGASTPTSSPAPSPAASPGHDGASTPTSSPAPSPAASPGHNGTSSPTGSPAPSPAASPGHDGASTPTSSPAPSPAASPGHNGTSSPTGSPAPSPAASPGHDGASTPTSSPAPSPAASPGHNGTSSPTGSPAPSPTASPGHDSAPSLTSSPAPSPTASPGQHGASSPTSSDTSSMTTRSMSSSMVTSAHKGTSSRATMTPVSKGTPSSVPSSETAPTAASHITRTAASSPSIALSTSSNPKTSQQLSVRVSLYFLSFRITNLQFNSSLENPQTSYYQELQRSIWGLILQIYKQRDFLGLSEIKFRPGSVVVELTLAFREGTTAEWVKAQFSQLEAHAASYNLTISGVSVYSAPFPSSAQAGSGVPGWGIALLVLVCVLVALAIIYLIALVVCQCGRKKCEQLDVFPTLDAYHPMSEYSTYHTHGRYVPPGSTKRSPYEEVSAGNGGSNLSYTNLAATSANL | Function: The alpha subunit has cell adhesive properties. May provide a protective layer on epithelial cells against bacterial and enzyme attack (By similarity).
PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic acid). O-linked glycosylation consists mainly of GalNAc, galactose, and sialic acid. The ratio from pools of milk from different dairy breeds is GalNAc: GlcNAc:galactose:mannose:sialic acid is 14:1:10:1:15.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58092
Sequence Length: 580
Subcellular Location: Apical cell membrane
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Q29435 | MTPGTQSLFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSMPSSTEKKVVSMTSSVLSSHSPGSGSSTTQGQDVSLAPATEPASGSAATWGQDVTSVPVTRPAPGSTTSPAQDVTSAPDTRPALGSTAPPVHGVTSAPDTRPTLGSTAPPVHGVTSAPDTRPTLGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLTSHSTKTDASSTHHSTVSPLTSSNHSTSPQLSIGVSFFFLSFHISNLQFNSSLEDPSTNYYQELQRDISELILQIYKQGDFLGVSNIKFRPGSVVVQSTLAFREGTTNVHDVEAQFNQHKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDAYHPMSEYPTYHTHGRYVPPSSTNRSPYEKVSEGNGGSSLSYTNPAVAATSANL | Function: The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack (By similarity).
PTM: Probably both N- and O-glycosylated (in repeat region).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 49372
Sequence Length: 475
Subcellular Location: Apical cell membrane
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Q60528 | MTPGIRAPFLLTLLLALVTDPNSVALSQDTSSSSTLNTTPVHSGSSAPATSSAVDSATTPGHSGSSAPPTSSAVNSATTPGHSGSSAPPTSSAVNSATTPVHSGSSAPVTSSAVNSATTPVHSGSSAPPTSSAVNSATTPVHSGSSAPVTSSAVNSATTPVHSGSSAPVTSSAVDSATTPVHSGSSAPPTSSAVNSATTPVHSGSSAPVTSSAVNSATTPVHSGSSAPVTSSAVNSATTPVHSGSSAPPTSSVVNSATTPVHSGSSAPPTSSAVNLATTPVHSGSSTPATNSTTDSATTPVPPGSSMQTTEAISGSANTPIHNGSLVPTTSSALVPTTSAAHSGASAMTNSSESDLATTPIDSGTSISTTKAPATTPVHNGSLVPTTSSVLGSATTLIHNDTSTMATTTPVGNGTQSSVPSRHPVTPTPPAVSSNSTIALSTYYSTALSPAFSSHAAPQVSVGVSFFLLSFHIWNHQFNSSLEDPSSNYYQELKRNVSGLFLQVFSRAFLGISTIEFRSGSVVVDSTVIFREGAVNASEVKSQLLQHEQEAEEYNLAISKINVGEMQFPSSAQSWPGVPGWGIALLVLVCILVALAIVYLIALAVCQCRRKNYGQLDIFPIQDSYHPMSEYPTYHTHGRYVPPGSTKRSPYEEVSAGNGSSLSYTNPVVATTSANL | Function: The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack (By similarity).
PTM: Probably both N- and O-glycosylated (in repeat region).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 67617
Sequence Length: 676
Subcellular Location: Apical cell membrane
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Q02496 | MTPGIRAPFFLLLLLASLKGFLALPSEENSVTSSQDTSSSLASTTTPVHSSNSDPATRPPGDSTSSPVQSSTSSPATRAPEDSTSTAVLSGTSSPATTAPVNSASSPVAHGDTSSPATSLSKDSNSSPVVHSGTSSAATTAPVDSTSSPVVHGGTSSPATSPPGDSTSSPDHSSTSSPATRAPEDSTSTAVLSGTSSPATTAPVDSTSSPVAHDDTSSPATSLSEDSASSPVAHGGTSSPATSPLRDSTSSPVHSSASIQNIKTTSDLASTPDHNGTSVTTTSSALGSATSPDHSGTSTTTNSSESVLATTPVYSSMPFSTTKVTSGSAIIPDHNGSSVLPTSSVLGSATSLVYNTSAIATTPVSNGTQPSVPSQYPVSPTMATTSSHSTIASSSYYSTVPFSTFSSNSSPQLSVGVSFFFLSFYIQNHPFNSSLEDPSSNYYQELKRNISGLFLQIFNGDFLGISSIKFRSGSVVVESTVVFREGTFSASDVKSQLIQHKKEADDYNLTISEVKVNEMQFPPSAQSRPGVPGWGIALLVLVCILVALAIVYFLALAVCQCRRKSYGQLDIFPTQDTYHPMSEYPTYHTHGRYVPPGSTKRSPYEEVSAGNGSSSLSYTNPAVVTTSANL | Function: The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack.
PTM: Probably both N- and extensively O-glycosylated (in repeat region).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 64539
Sequence Length: 630
Subcellular Location: Apical cell membrane
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Q05049 | APTTAAAVAATGKDTTAAAEGSAAAEKTAAAGEVSAPPTAAVAATGEDATTAAATAAAETTAAAGEAPTTTTAPATTAAGKAPTTAAATAPTTAAAGAPTTATGKAPATAAAPVPTTAASKAPTTAAAATHSTAAAAAPTTAASAAKSKERSTSSSSEEEHCHVKPSKREMCGSKGITKKQCKKKNCCFDPKGHGGIHCFHRKPKGHSHEEHTTTTTKAPTTIQIATTTTTPTTTTTTTKATPTTTTTTKATPTTTTTTKATTTTTTPTTTTTTTKATTTPTTTTTTTPTTTTTKATTTTTTTSGECKMEPSKREDCGYSGITESQCRTKGCCFDSSIPQTKWCFYTLSQVADCKVEPSQRVDCGFRGITADQCRQKNCCFDSSISGTKWCFYSTSQVAATKTTTTPTTTTTPTTTTTTKATTTTPTTTTTTPTTTTTTTTTTKATTTTPTTTTPTTTTTKATTTTPTTTTTTPTTTTTKATTTTPTTTTTTPTTTTTKATTTTPTTTTTTTTTTKATTTTTSGECKMEPSKRADCGYPGITESQCRSKGCCFDSSIPQTKWCFYSLPQVADCKVAPSSRVDCGFGGITADQCRQRNCCFDSSISGTKWCFYSTSQGNAMCSGPPTKRRDCGYPGISSSVCINRGCCWDNSVMNVPWCFYRT | Function: Could be involved in defense against microbial infections. Protects the epithelia from external environment.
PTM: Extensively O-glycosylated.
Sequence Mass (Da): 67775
Sequence Length: 662
Subcellular Location: Secreted
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Q9SS43 | MRQNLKKVAQIKVDESKKLFPYVFRVKTSCGNCAKRSKPKLIYLLIFSLISSCFVFAPQLLCFPYPSALFLIDSSIKEIENRVSESNIESPKTSQKEESISCDRTGYRSDICFMKGDIRTHSPSSSIFLYTSNDLTTDQVLQEKIKPYTRKWETSIMETIPELKLVTKDMKLFGDKRKCEVIHEVPAVLFSTGGYTGNLYHEFNDGLIPLYITSKRFNKKVVFVIAEYHKWWEMKYGDVLSQLSDYSLIDFNKDKRTHCFKEAIVGLRIHGELTVDPSQMQDDGTTINEFRNVLDRAYRPRINRLDRLEEQRFHARLAQRRKAKRPKLALFSRTGSRGITNEDLMVKMAQRIGFDIEVLRPDRTTELAKIYRVLNSSKVMVGVHGAAMTHFLFMKPGSIFIQIIPLGTDWAAETYYGEPAKKLGLDYNGYKILPRESSLYEKYDKDDPILKDPNSITKKGWQFTKGIYLNDQKVRLDLHRFKKLLIDAYAKSIR | Function: Glycosyletransferase required for the proper composition and structural properties of released seed coat mucilage . Required for the production of highly branched xylan polymers in seed coat mucilage . Facilitates the addition of xylose residues directly to the xylan backbone . Xylan with xylose side chains seems to be necessary for pectin attachment to the seed surface . Essential for xylan synthesis in seed coat epidermal (SCE) cells .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 57287
Sequence Length: 494
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
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Q5SSG8 | MKMQKGNVLLMFGLLLHLEAATNSNETSTSANTGSSVISSGASTATNSGSSVTSSGVSTATISGSSVTSNGVSIVTNSEFHTTSSGISTATNSEFSTVSSGISIATNSESSTTSSGASTATNSESSTPSSGASTATNSDSSTTSSGASTATNSDSSTTSSEASTATNSESSTTSSGASTATNSESSTVSSRASTATNSESSTTSSGASTATNSESRTTSNGAGTATNSESSTTSSGASTATNSESSTPSSGAGTATNSESSTTSSGAGTATNSESSTVSSGISTVTNSESSTPSSGANTATNSESSTTSSGANTATNSDSSTTSSGASTATNSESSTTSSGASTATNSESSTTSSGASTATNSGSSTTSSGTSTATNSESSTVSSGASTATTSESSTTSSGASTATNSESSTVSSGASTATNSESSTTSSGANTATNSGSSVTSAGSGTAALTGMHTTSHSASTAVSEAKPGGSLVPWEIFLITLVSVVAAVGLFAGLFFCVRNSLSLRNTFNTAVYHPHGLNHGLGPGPGGNHGAPHRPRWSPNWFWRRPVSSIAMEMSGRNSGP | PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 54228
Sequence Length: 566
Subcellular Location: Cell membrane
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Q2YDH0 | MSGLSRPLLLAVGCLAALCVITAAGNTTLAPNVTTASSPPPTTTTVPVSPTTLSPLPVTTPAPDICGSRNSCVSCVDGNATCFWIECKGKSYCSDNSTAGDCKVVNTTGFCSVPTTTPTPTNSTAKTTTLPSTTTTSTTATTSGTTNTTLSPTIQPTRKSTFDAASFIGGIVLVLGVQAVIFFLYKFCKSKERNYHTL | Function: Sialomucin that may play a key role in hematopoiesis. May be involved in cell adhesion. Promotes myogenesis by enhancing CXCR4-dependent cell motility. Positively regulates myoblast migration and promotes myoblast fusion into myotubes (By similarity).
PTM: Highly N- and O-glycosylated; contains sialic acid.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 20347
Sequence Length: 198
Subcellular Location: Lysosome membrane
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Q04900 | MSRLSRSLLWAATCLGVLCVLSADKNTTQHPNVTTLAPISNVTSAPVTSLPLVTTPAPETCEGRNSCVSCFNVSVVNTTCFWIECKDESYCSHNSTVSDCQVGNTTDFCSVSTATPVPTANSTAKPTVQPSPSTTSKTVTTSGTTNNTVTPTSQPVRKSTFDAASFIGGIVLVLGVQAVIFFLYKFCKSKERNYHTL | Function: Sialomucin that may play a key role in hematopoiesis by facilitating the adhesion of CD34(+) cells to the stroma and by negatively regulating CD34(+)CD38(lo/-) cell proliferation. Modulates the migration of umbilical cord blood CD133+ cells and this is mediated through the CXCL12/CXCR4 axis. May play an important role in prostate cancer metastasis and the infiltration of bone marrow by cancer cells. Promotes myogenesis by enhancing CXCR4-dependent cell motility. Positively regulates myoblast migration and promotes myoblast fusion into myotubes (By similarity).
PTM: Highly N- and O-glycosylated; contains sialic acid.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 20917
Sequence Length: 197
Subcellular Location: Lysosome membrane
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Q969V5 | MESGGRPSLCQFILLGTTSVVTAALYSVYRQKARVSQELKGAKKVHLGEDLKSILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLTLQEHKMVWNRTTHLWNDCSKIIHQRTNTVPFDLVPHEDGVDVAVRVLKPLDSVDLGLETVYEKFHPSIQSFTDVIGHYISGERPKGIQETEEMLKVGATLTGVGELVLDNNSVRLQPPKQGMQYYLSSQDFDSLLQRQESSVRLWKVLALVFGFATCATLFFILRKQYLQRQERLRLKQMQEEFQEHEAQLLSRAKPEDRESLKSACVVCLSSFKSCVFLECGHVCSCTECYRALPEPKKCPICRQAITRVIPLYNS | Function: Exhibits weak E3 ubiquitin-protein ligase activity . E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates . Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteasomal degradation . Mediates polyubiquitination of cytoplasmic TP53 at 'Lys-24' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion . Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations . Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization . Likely to promote mitochondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway . May also be involved in the sumoylation of the membrane fission protein DNM1L . Inhibits cell growth . When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis . Involved in the modulation of innate immune defense against viruses by inhibiting RIGI-dependent antiviral response . Can mediate RIGI sumoylation and disrupt its polyubiquitination .
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Location Topology: Multi-pass membrane protein
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 39800
Sequence Length: 352
Domain: The zinc finger domain is required for E3 ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.2.27
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Q8VCM5 | MESGSRPSLGQVILLGTSSMVTAVLYSIYRQKAQVAQELKGAKKIHLGEDLKGILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLSLQEHKMVWNRTTHLWNDYSKIIHQRTNTVPFDLVPHEDGVAVSVRVLKPLDSVDLGLETVYEKFHPSVQSFTDAIGHYISGERPKGIQETEEMLKVGATLTGIGELVLDNNAVRLQPPKQGMQYYLSSQDFDSLLHRQESSVRLWKILVLVFGFATCATLFFILRKQYLHRQERLRQQQLQEEFLEHEAQLLSQASPEDRESLKSACVVCLSNFKSCVFLECGHVCSCRQCYLALPEPKRCPICRREITRVIPLYNS | Function: Exhibits weak E3 ubiquitin-protein ligase activity (By similarity). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity). Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteasomal degradation (By similarity). Mediates polyubiquitination of cytoplasmic TP53 at 'Lys-27' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion (By similarity). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (By similarity). Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization (By similarity). Likely to promote mitochondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway . May also be involved in the sumoylation of the membrane fission protein DNM1L (By similarity). Inhibits cell growth (By similarity). When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (By similarity). Involved in the modulation of innate immune defense against viruses by inhibiting RIGI-dependent antiviral response (By similarity). Can mediate RIGI sumoylation and disrupt its polyubiquitination (By similarity).
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Location Topology: Multi-pass membrane protein
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 39835
Sequence Length: 352
Domain: The zinc finger domain is required for E3 ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.2.27
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Q08750 | MGFVDFFETYMVGSRVQFKQLDISDWLSLTPRLLILFGYFYLHSFFTAINQFLQFINTNSFCLRLHLLYDRFWSHVPIIGEYKIRLLSRALTYSKLKIIPTLDKVLEAIEIWFQLHLVEMTFEKKKNVQIFITEGSDDLNFFKDSKFQTTLMICNHRSVNDYTLINYLFLKSCPTKFYTKWEFLQKLRKGEDLAEWPQLKFLGWGKMFNFPRLDLLKNIFFKDETLALSSNELRDILERQNNQAITIFPEVNIMSLELSIIQRKLHQDFPFVINFYNLLYPRFKNFTTLMAAFSSIKNIKRKKNRNNIIKEARYLFHRELDKLVHKSMKMESSKVSDKTTPPMIVDNSYLLTKKEEISSGKPKVVRINPYIYDVTIIYYRVKYTDSGHDHTNGDLRLHKGYQLEQISPTIFEMIQPEMESENNIKDKDPIVVMVNVKKHQIQPLLAYNDESLEKWLENRWIEKDRLIESLQKNIKIETK | Function: Involved in the organization of the outer spore wall layers and especially in the assembly of the chitosan layer.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57237
Sequence Length: 479
Subcellular Location: Membrane
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P50276 | MSEGRTFLSQLNVFNKENYQFSSSTTKKEVSNSTVDADNGASDFEAGQQFATELDQGEKQLGILSCIGLICNRMLGTGVFAVSSTIYTLCGSVGLALIMWAVGAIIAISGLYVYMEFGTAIPKNGGEKNYLEAIFRKPKFFITCMYAAYIFFLGWAAGNSINTAIMFLTAADTEVTKWNQRGIGVAVVFFAFLINSLNVKIGLYLQNILGIFKIGIVLFISITGWVALGGGLKDGYQSHNFRNAFEGTETATAYGIVNALYSVIWSFVGYSNVNYALGEVKNPVRTLKIAGPTSMVFLAIIYIFVNIAYFAVVPKDKLISSKLILAADFFDIVFGGQAKRAAAALVGLSALGNVLSVIFSQGRIIQQLGREGVLPFSNFFASSKPFNSPMVGLFQHFIVCTVTILAPPPGDAYLLVQNLISYPMNIINFAISAGLLWIYWQRRQGKIEWNPPIKAGVFVTGFFTLSNLYLIIAPYVPPSNGESVYSSMPYWIHCVIAWGIFFFGGVYYVVWAQLLPRWGHYKLVSKDVLGEDGFWRVKIAKVYDDTIGDVDTQEDGVIETNIIEHYKSEQEKSL | Function: High affinity permease for methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63221
Sequence Length: 574
Subcellular Location: Membrane
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P04939 | MKLLLPLLLLLCLELTLVCIHAEESSSMERNFNVEQISGYWFSIAEASYEREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYDGFNTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRCLEARE | Function: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females.
PTM: Glycosylated.
Sequence Mass (Da): 21465
Sequence Length: 184
Subcellular Location: Secreted
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P38734 | MEPLLFNSGKANPSQDVFIDVEVGDITTKYGSTNTGSFSSMDTVEAQAIKAETARFMEVPQGRHLGVFSTVVLFVSRIMGSGIFAVPSVILLNTGGNKLIYFAIWVFSAAIAFAGLYLFLEFGSWIPKSGGRKNFLERSFERPRLLISVVFSCYSVLTGYALTGSIVFGKYVLSAFGVTDDSWSKYVSISFIIFAVLIHGVSVRHGVFIQNALGGLKLIMIVLMCFAGLYTLFFYKSTGQVAWDLPVTQVEKDSLLSVSSIATAFISSFFCFSGWDTVHTVTSEIKNPVKTLKVSGPLSLIICFVCYTMMNVAYLKVLTYEEIVSAGPLVGSVLFTKLFGPRVGGKFIAFSIAISAASNILVVIYSISRVNQEIFKEGYLPFSIHMSKNWPFDAPLPSISLCGFITIAWILILPKEGESFNYLVSMDGYGNQFFLLLVAIGLFIWRFKHKNEVPEIRASTFGVLAIITLSLYMLMAPFFADPSLNRVGFLPPYQIMSLLVIVACFFFWLVKFVLLPKFFHYKLLPKITYLHDGLIVTEWVKKPCLC | Function: Very low affinity permease for methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60620
Sequence Length: 546
Subcellular Location: Membrane
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Q39K93 | MQVTVNERDAVQSVATAHPAANGESHGHGMDKLVIEGGHRLSGEIVVSGAKNAALPILCAGLLTGDPVDLDNVPNLKDVRTTLKVLNQMGVKSETDGCRVQLDASRVDNLVAPYELVKTMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDQHIKGLQAMGAEISIEHGFIEARAKRLKGARIVTDMITVTGTENLLMAATLADGETVIENAAREPEVSDLAHLLVAMGAKIDGIGTDRLVIQGVERLHGARHSVIPDRIEAGTFLCAVAAAGGDVRLTGVRPHILDAVIDKLREAGVSIEEGDSWLRVKMDRRPSAVTIRTSEYPAFPTDMQAQFMALNTVATGTAQVVETIFENRFMHVQELNRLGANITIDGNTALVTGVDKLSGANVMATDLRASASLVIAGLRAEGETLVDRIYHLDRGYDRMEAKLTAVGANVRRLSGSQA | 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): 47666
Sequence Length: 449
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q3JMZ4 | MQVTVNEHDAVERVATATPAGNREAHAHGTDKLAIEGGRRLAGEIAVSGAKNAALPILCAGLLSAEPVRLDNVPDLKDVRTTLALLGQMGMREETDGARVVLDASRVDNPVAPYELVKTMRASILVLGPLLARFGYAKVSLPGGCAIGARPVDQHIKGLQAMGAEIHIEHGYIEARAKRLSGARIVTDMITVTGTENLLMAATLADGETVIENAAREPEVTDLAHLLVAMGAKIDGIGTDRLVIQGVERLHGATHAVIPDRIEAGTFLCAVAAAGGDVTLTGMRAHILDAVIDKLREAGATIDEGVDTLRVRMDGRPSAVAIRTSEYPAFPTDMQAQFMALNAVAQGAAQVTETIFENRFMHVQELNRLGANIAVDGNTALVTGVPKLSGASVMATDLRASASLVIAGLCAQGETLVERIYHLDRGYDRMETKLTAVGANVRRISGSEA | 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): 47283
Sequence Length: 449
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q9PP65 | MTYLEIEGTNHLSGNVTISGAKNAALPLIVSSILAKNEVKINNVPNVADIKTLISLLENLGAKVNFQNNSALLNTNTLNQTIAKYDIVRKMRASILTLGPLLARFGHCEVSLPGGCAIGQRPIDLHLLALEKMGANIQIKQGYVVASGNLKGNEILFDKITVTGSENIIMAAALAKGKTKLLNVAKEPEVVQLCEVLKDAGLEIKGIGTDELEIYGSDGELLEFKEFSVIPDRIEAGTYLCAGAITNSKITLDKVNATHLSAVLAKLHQMGFETLITEDSITLLPAKEIKPVEIMTSEYPGFPTDMQAQFMALALKANGTSIIDERLFENRFMHVSELLRMGADIKLNGHIATIVGGKELNAADVMATDLRASSALILAALAAKGTSKVHRIYHLDRGYENLEEKFKDLGAKITRLEE | 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): 45186
Sequence Length: 418
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q7U5R6 | MTVASTVSQEILNHCLAIEGQRRLQGVLKVSGAKNSALVLMTASLLTEELVELINVPNLTDIAGMGRILSALGVQVEHSGNGVALNAGNLTSHEPPYELVNSLRASFFCIGSLLGRLGHARVPLPGGCRIGARPVVEHIRGLKALGAHVSVEHGIVSACVKGSKKRLTGAPIVLDCPSVGATETLLMAAVLATGTTTIENAAHEPEVQDLANLLIQMGADISGAGGPVITIHGVERLAGVSNYPVIPDRIEAGTFLIAAAITRSPLRVEPVIPEHLSAVLQKLRDCGCQLEIDQTGISITPGDIQAVDITTQPFPGFPTDLQAPFMALMATAQGTSVISEKIYENRLQHVAELQRMGASIRVDGSTAIVEGVAQLSAAPVTGSDLRAAAAMVLAGLAANGTTKVSGLKHLYRGYDKVEAKLNAVGAQLERQQG | 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): 45071
Sequence Length: 433
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q6MEP6 | MDVLKITGGIPLKGQVKAAGAKNAMTKLLVASLLSDKKCTFYNVPNIGDVEVTVSLCQEIGMEVRWDRAAGIMEVITKELKTSYIPQRFSGSNRIPILMIGALLGRTDQDIIVPTAGGCPIGQRPVDFHIQALEQLGAVIEYRGMKREGAYFAHAHNGLKGTLITLPYPSVGATENTILAGITARGVTVIKNAAIEPEIVELILFLQKLGAIITIDVDRTIRIQGTRRFYEVEHTVIPDRIEAASWGMAAISSKGKVFVEGAQHLNMITFLNKLREVGGGFDVRSNGIEFFYDGPLQGGLHLETDVHPGFMTDWQQPFVVLLTQSSGTSVVHETVYENRFGYTDTLKEMGADITPFRQCLGGKSCRFASQSFSHSAIIKGATPLVGKEIRIPDLRAGFAYIMAALIANDTSTISGLPFIQRGYENFIGKLADLGANVSLVEEEKNVKEMPENSSKLPLFAELQVN | 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): 50688
Sequence Length: 465
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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P57821 | MQKFRVYGQSRLRGSVNISGAKNAALPILFAAILAQEPVKLTNVPELKDIETTLKILRKLGVVVERDAEGAVHLDASKIDHFVAPYELVKTMRASIWALAPLVARFHRGQVSLPGGCSIGARPVDLHISGLERLGASIILEDGYVKAYVDHCLVGTRIVMEKVSVGATLSIMMAATLAKGKTIIENAAREPEITDTALFLNKMGAKIVGAGTDTITVEGVERLGGCEHSIVPDRIETGTFLVAAAISGGRIECKNTKADTLDAVIDKLREAGAQVDVTENSITLDMLGNRPRAVNIRTAPYPGFPTDMQAQFTLLNMVACGTSIITETIFENRFMHIPELIRMGGKAEIEGNTAICHGVDHLSGAEVMATDLRASISLVLAGCIATGETIVDRIYHIDRGYERIEEKLRGLGARIERFSAQSEES | 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): 45812
Sequence Length: 425
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q4FNE4 | MKKLEVFGAAKLKGQIRISGSKNASLPILAATLLSNKKISLANLPRVKDIETMILLLKSLGSIIEDNKKELIIKNTKQTKTFAAYSLVKTMRAGILVLGPLLAKFGKAKVSLPGGCAIGTRPVDIHLQALSKLGVKYKIIQGYVHANAPKGLIGANIKFPKVSVGATENLIIAACLAKGKTTLSNCAIEPEIKDLVNFLINMGCNIKWTAKRTVRIEGVNNLKELDYSVMPDRIEAGTYLIAAALTEGNLKITGIDPKIISTEINILKKVGSKITLKKNEILIQGSKKIKNINIKTSPYPGFPTDLQAQMMVLLCKANKRSHIKEEIFENRFMHVAELNRMGAKISINGNQASIEGNIKFEAAELMATDLRASVSLILAALAAKGKSVINRIYHLDRGYEDIEKKLKKVGAKIKRIN | 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): 45469
Sequence Length: 417
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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A4SV13 | MDKLRMTGGTPLNGEVTIAGAKNAALPILCACLLTDQPVVLRNLPDLQDVRTMLKLLQEIGVVVSFPDANNPNHVILNAAVIKSSEATYEMVKTMRASILVLGPLLARMHSAKVSLPGGCAIGARPVDQHIKGLKAMGASIKIKSGYIQAETKPTTERLKGASILTDMITVTGTENLLMAATLASGTTILENAAREPEVGDLAELLVKMGAKITGIGSDRLVIEGVEKLHGAEHSVIPDRIEAGTFLCAVAAAGGEVLVKHCRPDTLDAVIVKLKEAGLKMEIGPDWIKASMQGRPKAVSFRTSEYPAFPTDMQAQLMAVNAVANGNSTITETIFENRFMHVQELNRLGADIAIEGNTAIAQGVERLSGAIVMATDLRASASLVIAGLAAQGETQVDRIYHLDRGYDRMEQKLTRLGANIERIK | 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): 45168
Sequence Length: 424
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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A1VK35 | MDKLRIKGGKSLAGSVDISGAKNAALPELCAALLTAETVTLQNVPGLQDVATMLKLIRNMGVEAERSAHAPGTVILNAGPLSSPEAPYELVKTMRASVLALGPLLARFGEATVSLPGGCAIGSRPVDQHIKGLQAMGADIIVEHGYMLARLPKGQTRLKGAAITTDMVTVTGTENFLMAATLAEGETILENAAQEPEIGDLAEMLIKMGAKIEGHGSRRIRIQGVERLHGCTHQVVADRIETGTFLCAVAAAGGDVVLNHGRADHLEVVIEKLREAGATVTAGEGFIRIQASGRMKAQSFRTTEYPGFPTDMQAQFMALNAIAQGTSTVTETIFENRFMHVNEMVRLGAKIQIEGKVCVINGVEQLSGATVMATDLRASASLVIAGLVASGETFVERIYHLDRGYDQMEAKLRGIGADIERMKA | 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): 44921
Sequence Length: 424
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q7MUW1 | MASYVIEGGNSLKGEILVQGAKNEALQIISATLLTDQEVVVRNIPDILDVNNLIDLLRNMGVKVKRPTRDTCVFQADNVNLDYIKSEQFLEKSRALRGSVLLVGPLISRFGYAIFPKPGGDKIGRRRLDTHLVGIQALGATCDYHSDMQAYELTASRLSGTYMLLDEASVTGTANILMAAVLADGITTIYNAACEPYLQQLCKMLLSMGAHIEGVGSNLLRIEGVQSLHGCEHKMLPDMIEVGSFIGMAAMTASELLIKDVSVPDLGIIPASFRRLGIAVEQQGDDLFIPKQEHYEIETFMDGSIMTIADAPWPGLTPDLLSVFLVVATQAKGSVLIHQKMFESRLFFVDKLIDMGAQIILCDPHRATIIGLDKRVPLRAATMVSPDIRAGIALLIAAMSAEGTSIIHNVEQIDRGYQSIDTRLNAIGARISRL | 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): 47248
Sequence Length: 434
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.7
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Q81WD1 | MEQLVNELIQANVGRVLVDEPLARYTTMKIGGPADILIVPKRVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGEGLDHLEVEKHRVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNILSKALILFEDGTIDWLTHGEMEFSYRTSVLQTKRPGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPTPYFAGDLIEKAGLRGYQIGGAQISEMHGNFIINTGGASAQDVLSLIALIKQTIKDKFGVEMHTEVEIIGR | 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): 33016
Sequence Length: 301
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q8NTF4 | MNDFKKVSESLETALRNEFDFRFATEVSLKEISRWRIGGPAAVFAEPSSINEICALLAFMKNRPEPVVVVGGTSNILFDSDGFGGLVIKLGENFSNFIIEGSRIRAQAGASVPQLVRAVATEGLEGIVHAGGIPGTVGGLVVMNGGTQRRGIGEHVTKVLVTDAEGSIRELNANELQFTYRNSVLKNSETTVLEVELLLKPGNAGELLAELETILDQRSQKFPEDLPNCGSTFLSDPAMYSIVGPPGKAIEDAGLKGLRRGSAEISMQHANFIVNHGDASDDDILWLISAVRKEVYSRTGFVMDCEVLYLSYSGDFRPAHEVADEQWPDIDLVRN | 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): 36371
Sequence Length: 335
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q67RL6 | MDVHGAAYATHGKGVTGIAALDIQQGVSLRDYSTMRLGGWAAYLAHVRSPAEVEEGIAWAEARHLPVIMVGGGSNIIWRDEGFAGLVLVNRIPGFELADQGGHLLLTVGAGENWDSVVARAVAAGASGIERLSLIPGTAGATPVQNVGAYGQEIADVLVSVDAYDRQERRFVRIPAAECAFGYRRSRFNQADRGRFFITALTLRLLREPPRAPFYPALGRYLEERGLTHPTVQQVRDAVIAIRRAKLPDPAHVANCGSFFRNPIIPAPQAAELLRRYPDMPHWPVPGGGVKLAAGWLIDRAGFRGVADPETGMGTWPAQALVVVNHRASSTADLLRFKQKVQDEVRRRFGVTLEQEPELLP | 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): 39241
Sequence Length: 361
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q8NTB0 | MDSSLAQEIAAIDGVELDSEVTFADLTTLRIGGKPRSAVRCQTTEALVSAIKLLDDASLPLLIVGGGSNLVVADGDLDVIAVIIETDDVSINLTDGLLTADAGAVWDDVVHLSVDAGLGGIECLSGIPGSAGATPVQNVGAYGTEVSDVLTRVQLLDRTTHQVSWVDASELDLSYRYSNLKFTNRAVVLAIELQLLTDGLSAPLRFGELGRRLAISEAEPHPRRPVRMVRDAVLELRRAKGMVVEHTDHDTWSAGSFFTNPIVDPALADAVFEKVGEPTMPRFPAGDGKEKLSAAWLIERAGFKKGHPGAGAKASLSTKHTLALTNRGDARASDLVALAKEIRDGVLETFGVTLVPEPVWIGISIDD | 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): 38886
Sequence Length: 367
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q67Q47 | MSPMAERLRSIIRDPGRIRRAEPLKRHTSVRIGGPADYLVEVADRHELSRLLRLAGEEALPVYILGSGSNLVVSDEGVRGLVLRLTGEFARIAVDGSTVRVGGGCSLPKLAHQASRRGLGGLEFACAIPGTVGAGLVMNAGAHGGDMAQVVAEATVIWGDGRMERLCPGEIGFAYRSTRLQGTSAIVAEVVMALRPADRAALEGAMRQHLNRRRATQPLQYPNAGSVFKNPPGDYAGRLIEQAGLKGERVGDAQVSEKHANFIVNLGQATARDVLTLMDRVRSTVERRFGVRLEAEVKIWGHNPWFPP | 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): 33219
Sequence Length: 308
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q6FAZ1 | MIHIQHQVQLKPFNTLNLDVVASHYIKVQSVNELIEALDYAEQQQLNALILSGGSNMLLPQSLDALVLHIDIQGLEMIDEDSESVKIKVGGGQIWHDFVLMTTQKGWYGLQNLALIPGLVGASPVQNIGAYGVEVGEFIELVHVYDRSEKSVKTISCADCKFAYRHSIFKDEPYRYIITHVTFKLFKTPNLKLSYGDLLKAVGNEQTPENLQKQVIQIRESKLPNPKEYPNVGSFFKNPVISRQDFNQLLTEFPLIPHYPQPHDRVKIAAGWLIDQAGWKGKRLGAVGMFEKQALVLVNYANATLIDVQHTYRHVQSDIQQKFKLRLEPEPVLFGSNGLILSHME | 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): 39023
Sequence Length: 345
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
A9KSS3 | MNNVILQELKNIVSTERVTCNEPLSKHTSFKIGGPADYFVITKKIEETAAVIQCCNQHNLPLLMIGKGSNLLISDAGIRGVVLKQEDNTEGFFVTQCEEGYLVTGGAGMNLSAFAMKIANESLTGFEFAAGIPGSLGGAVYMNAGAYGGEIKDCIKSARVLTKEGQILSLNREELELSYRSSIIQKKGYYVIDATFLLQKGNQEDILRKIEELNQARKDKQPLEYPSAGSTFKRPEGYFAGKLIMDAGLRGYRVGGAMVSEKHCGFVINTGDATAKDVLQLIDDVRRIVKEKFGVTLEPEVRLIGEKVNP | 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): 33882
Sequence Length: 310
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q5ZSA6 | MSITGMDSSHVTESQGTLLFNEPLAEYTTWRVGGPAARLYKPANIDDLALFLSRLPFDEPLLWLGLGSNSLIRDGGFSGTVILTQGCLKEMTLLSDNCIRVEAGVSCASMARFSARNNLSGGEFWAGIPGTMGGALRMNAGCHGGETWQSVIEVQTINRRGEIRTRKPEEFEVAYRHVAGLGDEWFISAKLQLSPGNKETSLQLIKDLLAHRAKTQPTNEYNCGSVFRNPPGDFAARLIESCGLKGVSIGGAVVSEKHANFIINHQGTATAANIEALIHLVQTKVREQTSIELIREVHIIGDANVQTR | 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): 33449
Sequence Length: 308
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q6AH30 | MTDPPALSALTTMRVGGTPERLLEPADRDALVATAREVWSTGDEWLLLGGGSNTIAADDGFEGTVLRIVTRGVERLAAEKGRIRLRVQAGEPWDALVALTVRNGWAGIEALSGIPGSTGAAPVQNIGAYGQEIESALIGVEFLDYLTGEVYTLARAELGLGYRTSALKRGMAGVVLSVDLELADHSVPGGVGASLSAPIAYAQLADALAVPLGSRVSVDELRRAVLALRASKGMVLDPADPDSVSAGSFFTNPIVSENVARALPSDAPRWSLGPPEPDTILSLGPEGVHPLDVPPFAAGPYEAKLSAAWLIENAGIRSGFALPGSGAAISSKHTLAIVNRGAATAADVAQLASFVRGRVQADFGVVLHPEPVLVGLTL | 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): 39010
Sequence Length: 378
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q8EZC5 | MSPVLSESQLRDFKHTLESSKIPFRSEVRLGILSSFKIGGVCPVIVEPEISSQVSEILHIFSKFDIPWKILGGGSNLLISDHPDNFVTLRLSGKFKEFVSLGDGKFKIGAATNTTPTFRQISQLGYTGAEFLSTIPGWTGGAVIQNAGCYGGELFDLIESVEFLRNGEMFVRKPSEIKYGYRFTEFLNQKDSIILGIEILLKEGNLEEIESSLKDKRDRRNSSQPENKKSAGSVFKNPKVFREDGKEIKAWELLDQAGLRGQIKGGAQISPEHCNFIVNLGTATASDVHYLIDLVVDRVYQTSGILLNREIEFFGDIP | 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): 35356
Sequence Length: 318
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q03VW0 | MQLENIEILENHSLAPYAYTQAGGLVDYLAIPKSIHELKVLVNWAKELGMPVQVFGRLSNLIVRNGGLRGLSILLHDLRDVVVDQNKIVASAGADLIWVTEQAFEHGLSGLEWGAGIPGSVGGAVFMNAGAYGGQVDMVVSSVTALMPDGTLQNFEKKALEFGYRKSVFQSNGGIIISATFELQPDSCTAIRTRMDENNFKRANKQPLNYPSNGSVFKRPEGYFAGKLIMDSKLQGVRRGGVEVSKKHAGFMVNIAHGTGNDYEDLIHYVQKTVYEKFGVHLETEVRIMGER | 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): 32031
Sequence Length: 292
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q2LR56 | MRIPVLHDFFIKEQLKSCVSGAVLFDEPLDRYTSMGVGGPADALVVPQSMEELVQLVRFLRKENIPFLTLGNGTNLIVRDGGCRGVVVALRGLQKLSWASDPEGKIRVQAEAGVPLASIVQLCIKESLAGLEFCTGIPGSVGGAVRMNAGAFGREMKDVVTAITVLNEHLELETLSRRELSFEYRRLNLSDEAVIVCAEFALCPGERESISAEISEILALRKSKHPLNFRNAGSIFKNPRNLPAGQLIEETGLKGTRRGDAMISEKHGNFIVNLGHARAADVVDLIEEIKGRVENCRAIQLEAEVHIVGEDG | 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): 33965
Sequence Length: 312
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q3A2G8 | MHVLAARLGEILHSPVQLGEPLSRHTSWRIGGPAEIFLSPCDTKELVASLELLAQVGMPWIALGAGTNVLVRDGGFRGAVIHTGGLQDMAFDADGRARVGGGVPVMRLIRHCVERGLAGLEDLAGLPATIGGAVVMNAGAGKQDLAGVLDGAFLAGPSGVEYWPADRLELGYRTSAVPPGRIVTAASLRFRKASPEVLETYVRQRVQQRRKAQGVGKPNAGSVFKNPPGQQAWRLIDSCELRGFAVGGAQVSEKHANFIVNRGGARAEDVLRLIAEIQKKVEKRTGIVLEPEVKVVGQA | 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): 31691
Sequence Length: 299
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
P95837 | MTGAVSLLETLQQAVPLAGFTSFRVGGLAQFYDEPASVEAIATAWQWARLADFPVTFLGAGSNLLISDRGLPGLVLNLRRLQGATFDLATGCVEVAAGEPIPRLAWAAARQGWSGLEWAVGIPGTLGGAVVMNAGAQGGCMADILQSVQVITDQGLETWSREQLQYDYRHSVLQTGHACVVSAQLQLQPGFERSQVLTTTSTNFRQRKRTQPYHLPNCGSVFRNPEPQKAGQLIEACGLKGYQIGDAQVSELHANFILNCGAARAQDILSLIRHVQGTVGDHFGVNLHPEVKLLGEFQDVI | 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): 32347
Sequence Length: 301
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
A0LNZ0 | MIDNKRGSSYLNSLPEGLSAEECDRYSAVVSLCWNVLGELQDVEFKWHEPLAYHTTFRVGGPAACLARPRSESALLALLERVRENSVPYVVLGGGSNVLVTDGPIPALVIQLIHVAAGLAFNKGRSSSRPLVVVGAGVPISRLLRFCVRNELGGLECLVGIPGSVGGAVVMNAGTAEGTIAEALEWLDALDGAGQRQLVFKADLPAGYRSMGLPEAWLILGGAFRLHVSSGRSLKREMRSLMVRRKATQPLGRPSAGCVFKNPVEAPAGALIERAGLKGFRMGNAQVSDKHANWIINLGSARARDILALISLVENEVFGKFGVRLEREIRILSPEKNSLNQMLNS | 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): 37041
Sequence Length: 345
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q0AY75 | MYSEIFDFLPPERIKINEPMKEHSSFKIGGPVDLMVLPESIEEIQRITHYCRKKDIPCFVFGLGSNILVRDKGIRGVAIKVGNNLKNISICNDTIFAEAGVRLAELSQAAADYSLSGLEFAEGIPGSLGGAVVMNAGAYGGEMKDVLKEVRAITPDGNLSSFKPEEMKLRYRGSIFQEEELIVVSALMQLHKERAEDIRARMQDFAKRRREKQPLEYPSAGSTFRRPAGFFVGPMIEEMGLKGFKVGGAEVSRKHAGFIINSGNATANEVLELIAIVKAKAKEHYGIELETEVKVVGEE | 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): 33010
Sequence Length: 299
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
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