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 hypo... |
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 hypo... |
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 hypo... |
B1WQH2 | MNTIYPVIWSNNKVLLIDQTSLPSRYTLVEISRYEDMAKAIKTMIVRGAPAIGVAAAYGMYLGARDIQTQDRETFLKHLDKIAQILRQTRPTAVNLFWAISRMLKTAYETLGTVEEIKKILLETAQKIQEEDLQTCQAIGHNSLSILPTNPEKLTILTHCNAGALATAGYGTALGVIRSVWTAGRLNRVFADETRPRLQGAKLTAWECVQEKIPVTVISDNMAAHCMQKGLIDMVVVGADRIAANGDTANKIGTYGLAVIAKMHQVPFYVAAPLSTVDFSLETGDLIPIEERDPSELYQIGNTVIYPDGVDYYNPAFDVT... | 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-met... |
P0CN40 | MVAAAPSNKERLPDMMTSIRLDQSGRVEIIDQLLLPHSVVWMPVSTPEEAFDAIKTMRIRGAPAIASLAALTLRSYLSSSSSPVSSSSSSSDVISWVGQTIDYLQSSRPTAVNLGEAMDRIRAALKDSEAQNQTAGDIIQRVKKICGDVHDEDLERNMKMGRLGAEWLWKKRGGGKKGLKVMTVCNTGSLATSGYGTAIGVITALFQEDHLDTAYYAQTTPYHQGSRLTSLELTTLQIPACMICDTMLGSLFQHEDIDGVIVGADRVVKNGDTANKIGTYQAAVLAQRHNVPFMVVAPVTTIDLSLPTGAEIHIEHRPAA... | 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-met... |
A9JRE2 | MTLEAIRYRSGSLQILNQLLLPRETVYDEIRSVRDGYEAIKSMKVRGAPAIAIVGCLSLAVELRAGAGAEDLVSFVRDSLCHLTSARPTAVNMGRAARELMEFTENESMEKNTEQLRDSVIGWIEEMLERDVNDNKKIGNYGAQHILSGVPRDSVTILTHCNTGSLATAGYGTALGVVRSLHMLGRLKRLYCTETRPYNQGARLTAYEAVAEGFPATLITDSMAALAMREKSITAVVVGADRVVANGDTANKVGTYQLAIAAKHHGIPFYVAAPSTSCDLSLESGRDIVIEERPAEELTSINGVPVAAPGIDVWNPAFDV... | 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-met... |
Q47AR7 | MNIDGIPTRTLRAHPDRRAIDIIDQTRLPHALHWVRVATLEEAAHAIRAMQVRGAPLIGATAAYGLAIALDFEASDRRLAEAVALLGATRPTAVNLHWALARMENILRPLAPEARCDAAWAEAAAIAEEDVAQNAAIGQHGLKLWNDLIVADGQTLNIMTHCNAGWLATVDWGTALSPVYAAHDAGVPVHVWVSETRPRNQGLLTAWELEQHGVPHTLIADNAAGLLMRNGKVDAVIVGADRIAANGDVANKVGTYLKALACADNGIPFYVAAPRSTLDFACPEGASIPIEERDGDEFRLVHGLDSRGVPSALRQLPAGE... | 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-met... |
B8J4S7 | MDDHIRFDHQTFELHLLDQRLLPAQEADFVCRSVEDVVYALQTMVVRGAPAIGVTAAWGCVLALREAQGPDWAARLEQGMERIAAARPTAVNLRWAVERMRGVWLAAGGEAGDPAPLLTAFAHAAQTMQDEDVAVCKTLGRHGAACIEDGDCVLTHCNAGALATAGYGTALGVIRAAVEAGKKVSVIADETRPFLQGARLTAWELERDGIPVTVACDNACALLMSRGLVQRVVVGADRIAANGDTANKIGTYGVALLARHFHIPFYVAAPLSTIDPATPDGAGIPIEERPELEVTHMGETRLCPENVPVLNFAFDVTPAE... | 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-met... |
A8ZYA5 | MTATDPAPTRPIWLADDKKRVQIIDQRMLPHNLVIVDLTTVDQVIEAIGEMMVRGAPLIGVTGAFGVFIAVQNALERGDFEAQVRKECLRIKEARPTAVNLAWGVDRVCAAVFSKTLPADCLAAALAEASAIAEEEVDNCRRIGVHGVGLIETISRQKGGKTVNVLTHCNAGWLACVEHGTATAPIYKAFEKRIDIHVWVDETRPLNQGARLTAWELGQRGVAHTVITDNAGGHLMQHGMVDMVIVGTDRSTYTGDVANKVGTYLKALAARDNNIPFYVALPSSTFDWEMTDGLAQIPIEERNPDEVRCVEGLCPDGRVE... | 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-met... |
Q4ZQ92 | MRDRLLAAEKVKAIDWRDDALYLLDQRVLPFEEVWHRYTTAEGVAEAIRTMVVRGAPAIGISAAYGAVLAARARIAQGADWYPALEEDMQLLADSRPTAVNLFWALNRMRDRLMRVKDGDDPLAALEAEAVAIHLSDREANLTMAQLGADLIRKHQGNLQTVLTHCNTGALATGGFGTALGVIRAAHLEGMIERVYADETRPWLQGSRLTAWELANEGIPVTLNADSAAAHLMRTKGITWVIVGADRITANGDVANKIGTYQLAVAAMHHGVRFMVVAPSSTIDMEMASGDDIVIEERDGRELLEVGGQRVGAEVEAFNP... | 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-met... |
Q9UZ16 | MEVRYKPEELTKLPRSVEYKERTVYMINQRLLPREFKVEAFRTVESVAEAIKNMTVRGAPAIGAAAAFGLALYAETSKAKSKDEFMDGFYKAYETLKNTRPTAVNLFWALNRIKKLVEEHLEDPLDEIKSLIVNEAQKIADEDVEANLRMGHYGAEVLPEGNLLTHCNAGSLATVHLGTVGAVVRVMHKDGSLKLLWLDETRPVLQGARLSAWEYSYDGLNVKLIADNAAAFVMQQGLVDAIIVGADRIVANGDFANKIGTYMLAVLAREHGIPFFAVAPLSSIDMSLKSGKEIPIEERSPEEVLTCGGCRIAPDVPVYN... | 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
|
Q7UF90 | MNEAETIRYHAAHNGRPAELDLLDQTKLPGTLTRLVCTTIDQTHDAIQRLVVRGAPAIGIAAAYGVTLTPVDAESNSSLPEAQARYRQTIDYLATSRPTAVNLFWALDRMRAIVDDFSGPVAELRERLVTEAIRIHDDDRQMCRSIGCHGATLLADCKSVMTHCNAGSLATSMWGTALAPMYHLHESGHSLEVFADETRPLLQGARLTAWELHQAGIPVTVCTDSMSGSLMRQGRVDAVIVGADRIAANGDVANKIGTYPLAVLAKYHNIPFYVAAPTNTFDSELESGDLIPIEQRSADEVSYPCGTDSPRQTPEGVAVV... | 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-met... |
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
Se... |
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
Se... |
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
Se... |
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
Se... |
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 in... |
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
Se... |
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 ... |
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-methylthiobuty... |
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 ... |
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 ... |
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-methylthiobuty... |
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 ... |
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 ... |
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-ade... |
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-aden... |
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-aden... |
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-aden... |
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-aden... |
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): ... |
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): ... |
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): ... |
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): ... |
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): ... |
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): ... |
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): ... |
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... |
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-tetrahy... |
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-tetrahy... |
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-tetrahy... |
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-tetrahy... |
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-tetrahy... |
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
... |
P0AAD2 | MATLTTTQTSPSLLGGVVIIGGTIIGAGMFSLPVVMSGAWFFWSMAALIFTWFCMLHSGLMILEANLNYRIGSSFDTITKDLLGKGWNVVNGISIAFVLYILTYAYISASGSILHHTFAEMSLNVPARAAGFGFALLVAFVVWLSTKAVSRMTAIVLGAKVITFFLTFGSLLGHVQPATLFNVAESNASYAPYLLMTLPFCLASFGYHGNVPSLMKYYGKDPKTIVKCLVYGTLMALALYTIWLLATMGNIPRPEFIGIAEKGGNIDVLVQALSGVLNSRSLDLLLVVFSNFAVASSFLGVTLGLFDYLADLFGFDDSAV... | 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 | MIQQKSPSLLGGAMIIAGTAIGAGMLANPTSTAGVWFIGSILALIYTWFCMTTSGLMILEANLHYPTGSSFDTIVKDLLGKSWNTINGLSVAFVLYILTYAYITSGGGITQNLLNQAFSSAESAVDIGRTSGSLIFCLILAAFVWLSTKAVDRFTTVLIVGMVVAFFLSTTGLLSSVKTAVLFNTVAESEQTYLPYLLTALPVCLVSFGFHGNVPSLVKYYDRDGRRVMKSIFIGTGLALVIYILWQLAVQGNLPRTEFAPVIEKGGDVSALLEALHKYIEVEYLSVALNFFAYMAISTSFLGVTLGLFDYIADLFKFDD... | 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
|
P9WHH2 | METYDIAIIGTGSGNSILDERYASKRAAICEQGTFGGTCLNVGCIPTKMFVYAAEVAKTIRGASRYGIDAHIDRVRWDDVVSRVFGRIDPIALSGEDYRRCAPNIDVYRTHTRFGPVQADGRYLLRTDAGEEFTAEQVVIAAGSRPVIPPAILASGVDYHTSDTVMRIAELPEHIVIVGSGFIAAEFAHVFSALGVRVTLVIRGSCLLRHCDDTICERFTRIASTKWELRTHRNVVDGQQRGSGVALRLDDGCTINADLLLVATGRVSNADLLDAEQAGVDVEDGRVIVDEYQRTSARGVFALGDVSSPYLLKHVANHEA... | 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 | MDSQYETKKNDPNAIMPYPESNDEHVGEVRGLGGGIMDKEPEAQEGHAKFHRLGWKRLTVVLIVEAIALGSLSLPGAFATLGMVPGVILSVGMGLICIYTAHVIGQTKLKHPEIAHYADVGRVMFGRWGYEIISFMFVLQLIFIVGSHVLTGTIMWGTITDNGNGTCSLVFGIVSAIILFLLAIPPSFAEVAILGYIDFVSICAAILITMIATGIRSSHQEGGLAAVPWSCWPKEDLSLAEGFIAVSNIVFAYSFAMCQFSFMDEMHTPSDYKKSIVALGLIEIFIYTVTGGVVYAFVGPEVQSPALLSAGPLLAKVAFG... | 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 | MSSSPAQTPSRRPSLLGGSMIIAGTAVGAGMFSLPIAMSGIWFGWSVAVFLLTWFCMLLSGMMILEANLNYPVGSSFSTITRDLLGQGWNVVNGLSIAFVLYILTYAYISGGGSIIGYTLSSGLGVTLPEKLAGLLFALAVALVVWWSTRAVDRITTLMLGGMIITFGLSISGLLGRIQPAILFNSGEPDAVYWPYLLATLPFCLTSFGYHGNVPSLMKYYGKDPQRISRSLWIGTLIALAIYLLWQASTLGTIPREQFKGIIAGGSNVGTLVEYLHRITASDSLNALLTTFSNLAVASSFLGVTLGLFDYLADLCRFDD... | 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 | MAVSSIASIFAAEKSYSIPPVCQLLVSPVLNPLYDAKAESQIDAWCAEFLKLQPGSEKAVFVQESRLGLLAAYVYPTIPYEKIVPVGKFFASFFLADDILDSPEISSSDMRNVATAYKMVLKGRFDEATLPVKNPELLRQMKMLSEVLEELSLHVVDESGRFVDAMTRVLDMFEIESSWLRKQIIPNLDTYLWLREITSGVAPCFALIDGLLQLRLEERGVLDHPLIRKVEEIGTHHIALHNDLMSLRKEWATGNYLNAVPILASNRKCGLNEAIGKVASMLKDLEKDFARTKHEIISSGLAMKQGVMDYVNGIEVWMAG... | 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 = (+)-germac... |
B6SCF3 | MSLSGVPLSAGLAPSPSNKPTNGKGQNIVRRSGNYKPALWDYDYLQSLPTLYAGEAHVEKLNKLKGEVRIMLEKTVTENPLAQLEQIDTLYRLGISYHFQDEIKALLNTIHNNNNNNNNNDDVYATALEFKLLRLYGYTVHSEVFNVFKDEIDKGFKAISLCGDYVKGMLSLYEASFYSFKGETILDEARDFSTKHLQKYVMMRHNNNSKDQSVDDDDDLVILVEYALELPMHWRMIRLEAKWFIDVYSKRRDDMNPTFLELAQIDFNLLQSTYQEDLKHVSRWWSTCKLGERLPFCRDRLVEVFLLAVALKYEAEFGYA... | 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 | MPVLPWLAAAATTPVRRSPPLPATPRALLRLPASSFPPWSNCAKSGLPPRGPFATAADTPLGGSLPEPEEERDTLLDGALRAARFRDEESRRPDPLFIDPYAAVLLSLDVASEDKDLLALHLMPSAEHYRLVTRYIDDKLQHFISNSDDLRQIVLLTDGMDTRPYRLSWPRLSVVYDVSPRRVFITASQQLRGAGAKISRNCVVLHTSSESPDLQAGLNKNGFNGNRPSLWVLQGLPLFTFKSLEDLLLVIGNLAMKGSIFIGEVPRFTQWGAATDMASEQDRLENLFFTQGFRVSFVHYEEVAKDVGLGLDSPPEIHGR... | 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 respon... |
P09795 | MIMNDIITVTEAAQLLELTPQRVRTMCKQGSIDAYQSGRTWLIKSSSVEKLMLVNSLSDAQNSYSMLASEPKNKPKALSFFSGAMGLDLGIEQAGFETLLASEIDKAARDTILSNRPNMALIGDIRDYTTEDILKLAGVSSGNEIDLIMGGPPCQAFSTAGKRLGLEDERGNVFIKYLDVALDIRPKYIVIENVRGLLSAPMKHRPHNERGEGLPPLKSEEQPGGVLHYIIRIIKSAGYSVSFNLYNSANFGVPQIRERVIIICSRDGSRVPFLQPTHSEKGEYGLPKWITLRETITNLKNITHEHVLFPEKRLKYYRLL... | 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
Seq... |
O31073 | MNHELPVISLFSGAGGLDCAIESCAEPPLVQDGSGSPLRVAVATDYEQTALDTLSANFPHTKTLCGDIQTIPTAELLEAGGLKPGDPTLVIGGPPCTPFSKSGFWIEEKRNSADPNASLLDEYVRVVRESKPEAFILENVQGLTYKTHQAQFDRLIAGLKDAGYNPTFRVLLAAEYGVPQLRRRVFVVGRRDGKAFHFPETTHSGESERDRVIDHTKIPFTSLREALAGLPDVPEAGEVVEGTYAELAAEVPPGQNYLWHTDRYGGRNEFKWRSRYWTFLLKADPDRPSTTLQAQPGPWVGPFHWENVKNANGEERARRF... | 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
Se... |
Q53609 | MHSEAREAEARRLLLQETLDAERTFLERNQWGQFATPPSLAGEIMRYTIDLHEETRINFLEPSCGSGSFFSALLRNLGDKKIEHAVGVELDPRFSKAASDLWTGQGLRVIEGDFTSPSLVSGPVASLLVANPPYVRHHHLGIDQKRDLVARCADQLGIKPSGLSGLYLYFVLLSHRLLRADAVSTWLIPSEFMDVNYGTALKEYLATRVQLVRIHQYDAAEVQFDDALVTSSVVVFRNSPPRPGHTAEFSFGGTLSEPKVTHQIPSAALTPEAKWSRYVTGVMPADINLKQTGPKLSDFFKIRRGLATGSNAFFIIPRSE... | 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-adenos... |
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-homocystein... |
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 | MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRPLKEEKNRVHIQSSQTVESSGLYTLQSILKAQLVKEDKDAQFYCELNYRLPSGNHMKESREVTVPVFYPTEKVWLEVEPVGMLKEGDRVEIRCLADGNPPPHFSISKQNPSTREAEEETTNDNGVLVLEPARKEHSGRYEC... | 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 ne... |
Q9EPF2 | MGLPRLVCAFLFAACCCCRSATGVPGEEKQPTPTPDPVEVEVGNTALLKCGPAHPSGNFSQVEWFLIHKERQIPIFRVHQGKGQSEPGEYEHRLSLHGPGATLALSQVTPHDDRMFLCKSKQPRPQDHYVQLQVYKAPEEPTIQANVLGIHVDIQELKEVATCVGRNGYPIPQVIWYKNGRPLQEEENRVHIQSSQTVESSGLYTLKSVLSARLVKEDKDAQFYCELSYRLPSGNRMKESKEVTVPVLYPAEKVWVEVEPVGLLKEGDHVKIRCLTDGNPQPHFTINKKNPSTEEMEEESTDENGLLSLEPAQKHHSGVY... | 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 ne... |
Q8WML4 | MTPDIQAPFLSLLLLFPVLTVANVPTLTTSDSINPRRTTPVSTTQSSPTSSPTKETSWSTTTTLLTASSPAPSPAASPGHDGASTPTSSPAPSPAASPGHDGASTPTSSPAPSPAASPGHDGASTPTSSPAPSPAASPGHDGASTPTSSPAPSPAASPGHNGTSSPTGSPAPSPAASPGHDGASTPTSSPAPSPAASPGHNGTSSPTGSPAPSPAASPGHDGASTPTSSPAPSPAASPGHNGTSSPTGSPAPSPTASPGHDSAPSLTSSPAPSPTASPGQHGASSPTSSDTSSMTTRSMSSSMVTSAHKGTSSRATMTPV... | 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 ra... |
Q29435 | MTPGTQSLFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSMPSSTEKKVVSMTSSVLSSHSPGSGSSTTQGQDVSLAPATEPASGSAATWGQDVTSVPVTRPAPGSTTSPAQDVTSAPDTRPALGSTAPPVHGVTSAPDTRPTLGSTAPPVHGVTSAPDTRPTLGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLTSHSTKTDASSTHHSTVSPLTSSNHSTSPQLSIGVSFFFLSFHISNLQFNSSLEDPSTNYYQELQRDISELILQIYKQGDFLGVSNIKFRPGSVV... | 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 m... |
Q60528 | MTPGIRAPFLLTLLLALVTDPNSVALSQDTSSSSTLNTTPVHSGSSAPATSSAVDSATTPGHSGSSAPPTSSAVNSATTPGHSGSSAPPTSSAVNSATTPVHSGSSAPVTSSAVNSATTPVHSGSSAPPTSSAVNSATTPVHSGSSAPVTSSAVNSATTPVHSGSSAPVTSSAVDSATTPVHSGSSAPPTSSAVNSATTPVHSGSSAPVTSSAVNSATTPVHSGSSAPVTSSAVNSATTPVHSGSSAPPTSSVVNSATTPVHSGSSAPPTSSAVNLATTPVHSGSSTPATNSTTDSATTPVPPGSSMQTTEAISGSANTP... | 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 m... |
Q02496 | MTPGIRAPFFLLLLLASLKGFLALPSEENSVTSSQDTSSSLASTTTPVHSSNSDPATRPPGDSTSSPVQSSTSSPATRAPEDSTSTAVLSGTSSPATTAPVNSASSPVAHGDTSSPATSLSKDSNSSPVVHSGTSSAATTAPVDSTSSPVVHGGTSSPATSPPGDSTSSPDHSSTSSPATRAPEDSTSTAVLSGTSSPATTAPVDSTSSPVAHDDTSSPATSLSEDSASSPVAHGGTSSPATSPLRDSTSSPVHSSASIQNIKTTSDLASTPDHNGTSVTTTSSALGSATSPDHSGTSTTTNSSESVLATTPVYSSMPFS... | 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 membr... |
Q05049 | APTTAAAVAATGKDTTAAAEGSAAAEKTAAAGEVSAPPTAAVAATGEDATTAAATAAAETTAAAGEAPTTTTAPATTAAGKAPTTAAATAPTTAAAGAPTTATGKAPATAAAPVPTTAASKAPTTAAAATHSTAAAAAPTTAASAAKSKERSTSSSSEEEHCHVKPSKREMCGSKGITKKQCKKKNCCFDPKGHGGIHCFHRKPKGHSHEEHTTTTTKAPTTIQIATTTTTPTTTTTTTKATPTTTTTTKATPTTTTTTKATTTTTTPTTTTTTTKATTTPTTTTTTTPTTTTTKATTTTTTTSGECKMEPSKREDCGYS... | 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 | MRQNLKKVAQIKVDESKKLFPYVFRVKTSCGNCAKRSKPKLIYLLIFSLISSCFVFAPQLLCFPYPSALFLIDSSIKEIENRVSESNIESPKTSQKEESISCDRTGYRSDICFMKGDIRTHSPSSSIFLYTSNDLTTDQVLQEKIKPYTRKWETSIMETIPELKLVTKDMKLFGDKRKCEVIHEVPAVLFSTGGYTGNLYHEFNDGLIPLYITSKRFNKKVVFVIAEYHKWWEMKYGDVLSQLSDYSLIDFNKDKRTHCFKEAIVGLRIHGELTVDPSQMQDDGTTINEFRNVLDRAYRPRINRLDRLEEQRFHARLAQR... | 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 s... |
Q5SSG8 | MKMQKGNVLLMFGLLLHLEAATNSNETSTSANTGSSVISSGASTATNSGSSVTSSGVSTATISGSSVTSNGVSIVTNSEFHTTSSGISTATNSEFSTVSSGISIATNSESSTTSSGASTATNSESSTPSSGASTATNSDSSTTSSGASTATNSDSSTTSSEASTATNSESSTTSSGASTATNSESSTVSSRASTATNSESSTTSSGASTATNSESRTTSNGAGTATNSESSTTSSGASTATNSESSTPSSGAGTATNSESSTTSSGAGTATNSESSTVSSGISTVTNSESSTPSSGANTATNSESSTTSSGANTATNSDS... | 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.
L... |
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 impor... |
Q969V5 | MESGGRPSLCQFILLGTTSVVTAALYSVYRQKARVSQELKGAKKVHLGEDLKSILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLTLQEHKMVWNRTTHLWNDCSKIIHQRTNTVPFDLVPHEDGVDVAVRVLKPLDSVDLGLETVYEKFHPSIQSFTDVIGHYISGERPKGIQETEEMLKVGATLTGVGELVLDNNSVRLQPPKQGMQYYLSSQDFDSLLQRQESSVRLWKVLALVFGFATCATLFFILRKQYLQRQERLRLKQMQEEFQEHEAQLLSRAKPEDRESLKSACVVCLSSFKSCVFLECGHV... | 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 polyubiqui... |
Q8VCM5 | MESGSRPSLGQVILLGTSSMVTAVLYSIYRQKAQVAQELKGAKKIHLGEDLKGILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLSLQEHKMVWNRTTHLWNDYSKIIHQRTNTVPFDLVPHEDGVAVSVRVLKPLDSVDLGLETVYEKFHPSVQSFTDAIGHYISGERPKGIQETEEMLKVGATLTGIGELVLDNNAVRLQPPKQGMQYYLSSQDFDSLLHRQESSVRLWKILVLVFGFATCATLFFILRKQYLHRQERLRQQQLQEEFLEHEAQLLSQASPEDRESLKSACVVCLSNFKSCVFLECGHV... | 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' involv... |
Q08750 | MGFVDFFETYMVGSRVQFKQLDISDWLSLTPRLLILFGYFYLHSFFTAINQFLQFINTNSFCLRLHLLYDRFWSHVPIIGEYKIRLLSRALTYSKLKIIPTLDKVLEAIEIWFQLHLVEMTFEKKKNVQIFITEGSDDLNFFKDSKFQTTLMICNHRSVNDYTLINYLFLKSCPTKFYTKWEFLQKLRKGEDLAEWPQLKFLGWGKMFNFPRLDLLKNIFFKDETLALSSNELRDILERQNNQAITIFPEVNIMSLELSIIQRKLHQDFPFVINFYNLLYPRFKNFTTLMAAFSSIKNIKRKKNRNNIIKEARYLFHREL... | 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 | MSEGRTFLSQLNVFNKENYQFSSSTTKKEVSNSTVDADNGASDFEAGQQFATELDQGEKQLGILSCIGLICNRMLGTGVFAVSSTIYTLCGSVGLALIMWAVGAIIAISGLYVYMEFGTAIPKNGGEKNYLEAIFRKPKFFITCMYAAYIFFLGWAAGNSINTAIMFLTAADTEVTKWNQRGIGVAVVFFAFLINSLNVKIGLYLQNILGIFKIGIVLFISITGWVALGGGLKDGYQSHNFRNAFEGTETATAYGIVNALYSVIWSFVGYSNVNYALGEVKNPVRTLKIAGPTSMVFLAIIYIFVNIAYFAVVPKDKLIS... | 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 | MEPLLFNSGKANPSQDVFIDVEVGDITTKYGSTNTGSFSSMDTVEAQAIKAETARFMEVPQGRHLGVFSTVVLFVSRIMGSGIFAVPSVILLNTGGNKLIYFAIWVFSAAIAFAGLYLFLEFGSWIPKSGGRKNFLERSFERPRLLISVVFSCYSVLTGYALTGSIVFGKYVLSAFGVTDDSWSKYVSISFIIFAVLIHGVSVRHGVFIQNALGGLKLIMIVLMCFAGLYTLFFYKSTGQVAWDLPVTQVEKDSLLSVSSIATAFISSFFCFSGWDTVHTVTSEIKNPVKTLKVSGPLSLIICFVCYTMMNVAYLKVLTY... | 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 | MQVTVNERDAVQSVATAHPAANGESHGHGMDKLVIEGGHRLSGEIVVSGAKNAALPILCAGLLTGDPVDLDNVPNLKDVRTTLKVLNQMGVKSETDGCRVQLDASRVDNLVAPYELVKTMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDQHIKGLQAMGAEISIEHGFIEARAKRLKGARIVTDMITVTGTENLLMAATLADGETVIENAAREPEVSDLAHLLVAMGAKIDGIGTDRLVIQGVERLHGARHSVIPDRIEAGTFLCAVAAAGGDVRLTGVRPHILDAVIDKLREAGVSIEEGDSWLRVKMDRRPSAV... | 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 biosynthe... |
Q3JMZ4 | MQVTVNEHDAVERVATATPAGNREAHAHGTDKLAIEGGRRLAGEIAVSGAKNAALPILCAGLLSAEPVRLDNVPDLKDVRTTLALLGQMGMREETDGARVVLDASRVDNPVAPYELVKTMRASILVLGPLLARFGYAKVSLPGGCAIGARPVDQHIKGLQAMGAEIHIEHGYIEARAKRLSGARIVTDMITVTGTENLLMAATLADGETVIENAAREPEVTDLAHLLVAMGAKIDGIGTDRLVIQGVERLHGATHAVIPDRIEAGTFLCAVAAAGGDVTLTGMRAHILDAVIDKLREAGATIDEGVDTLRVRMDGRPSAV... | 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 biosynthe... |
Q9PP65 | MTYLEIEGTNHLSGNVTISGAKNAALPLIVSSILAKNEVKINNVPNVADIKTLISLLENLGAKVNFQNNSALLNTNTLNQTIAKYDIVRKMRASILTLGPLLARFGHCEVSLPGGCAIGQRPIDLHLLALEKMGANIQIKQGYVVASGNLKGNEILFDKITVTGSENIIMAAALAKGKTKLLNVAKEPEVVQLCEVLKDAGLEIKGIGTDELEIYGSDGELLEFKEFSVIPDRIEAGTYLCAGAITNSKITLDKVNATHLSAVLAKLHQMGFETLITEDSITLLPAKEIKPVEIMTSEYPGFPTDMQAQFMALALKANGT... | 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 biosynthe... |
Q7U5R6 | MTVASTVSQEILNHCLAIEGQRRLQGVLKVSGAKNSALVLMTASLLTEELVELINVPNLTDIAGMGRILSALGVQVEHSGNGVALNAGNLTSHEPPYELVNSLRASFFCIGSLLGRLGHARVPLPGGCRIGARPVVEHIRGLKALGAHVSVEHGIVSACVKGSKKRLTGAPIVLDCPSVGATETLLMAAVLATGTTTIENAAHEPEVQDLANLLIQMGADISGAGGPVITIHGVERLAGVSNYPVIPDRIEAGTFLIAAAITRSPLRVEPVIPEHLSAVLQKLRDCGCQLEIDQTGISITPGDIQAVDITTQPFPGFPTD... | 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 biosynthe... |
Q6MEP6 | MDVLKITGGIPLKGQVKAAGAKNAMTKLLVASLLSDKKCTFYNVPNIGDVEVTVSLCQEIGMEVRWDRAAGIMEVITKELKTSYIPQRFSGSNRIPILMIGALLGRTDQDIIVPTAGGCPIGQRPVDFHIQALEQLGAVIEYRGMKREGAYFAHAHNGLKGTLITLPYPSVGATENTILAGITARGVTVIKNAAIEPEIVELILFLQKLGAIITIDVDRTIRIQGTRRFYEVEHTVIPDRIEAASWGMAAISSKGKVFVEGAQHLNMITFLNKLREVGGGFDVRSNGIEFFYDGPLQGGLHLETDVHPGFMTDWQQPFVV... | 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 biosynthe... |
P57821 | MQKFRVYGQSRLRGSVNISGAKNAALPILFAAILAQEPVKLTNVPELKDIETTLKILRKLGVVVERDAEGAVHLDASKIDHFVAPYELVKTMRASIWALAPLVARFHRGQVSLPGGCSIGARPVDLHISGLERLGASIILEDGYVKAYVDHCLVGTRIVMEKVSVGATLSIMMAATLAKGKTIIENAAREPEITDTALFLNKMGAKIVGAGTDTITVEGVERLGGCEHSIVPDRIETGTFLVAAAISGGRIECKNTKADTLDAVIDKLREAGAQVDVTENSITLDMLGNRPRAVNIRTAPYPGFPTDMQAQFTLLNMVAC... | 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 biosynthe... |
Q4FNE4 | MKKLEVFGAAKLKGQIRISGSKNASLPILAATLLSNKKISLANLPRVKDIETMILLLKSLGSIIEDNKKELIIKNTKQTKTFAAYSLVKTMRAGILVLGPLLAKFGKAKVSLPGGCAIGTRPVDIHLQALSKLGVKYKIIQGYVHANAPKGLIGANIKFPKVSVGATENLIIAACLAKGKTTLSNCAIEPEIKDLVNFLINMGCNIKWTAKRTVRIEGVNNLKELDYSVMPDRIEAGTYLIAAALTEGNLKITGIDPKIISTEINILKKVGSKITLKKNEILIQGSKKIKNINIKTSPYPGFPTDLQAQMMVLLCKANKR... | 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 biosynthe... |
A4SV13 | MDKLRMTGGTPLNGEVTIAGAKNAALPILCACLLTDQPVVLRNLPDLQDVRTMLKLLQEIGVVVSFPDANNPNHVILNAAVIKSSEATYEMVKTMRASILVLGPLLARMHSAKVSLPGGCAIGARPVDQHIKGLKAMGASIKIKSGYIQAETKPTTERLKGASILTDMITVTGTENLLMAATLASGTTILENAAREPEVGDLAELLVKMGAKITGIGSDRLVIEGVEKLHGAEHSVIPDRIEAGTFLCAVAAAGGEVLVKHCRPDTLDAVIVKLKEAGLKMEIGPDWIKASMQGRPKAVSFRTSEYPAFPTDMQAQLMAV... | 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 biosynthe... |
A1VK35 | MDKLRIKGGKSLAGSVDISGAKNAALPELCAALLTAETVTLQNVPGLQDVATMLKLIRNMGVEAERSAHAPGTVILNAGPLSSPEAPYELVKTMRASVLALGPLLARFGEATVSLPGGCAIGSRPVDQHIKGLQAMGADIIVEHGYMLARLPKGQTRLKGAAITTDMVTVTGTENFLMAATLAEGETILENAAQEPEIGDLAEMLIKMGAKIEGHGSRRIRIQGVERLHGCTHQVVADRIETGTFLCAVAAAGGDVVLNHGRADHLEVVIEKLREAGATVTAGEGFIRIQASGRMKAQSFRTTEYPGFPTDMQAQFMALN... | 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 biosynthe... |
Q7MUW1 | MASYVIEGGNSLKGEILVQGAKNEALQIISATLLTDQEVVVRNIPDILDVNNLIDLLRNMGVKVKRPTRDTCVFQADNVNLDYIKSEQFLEKSRALRGSVLLVGPLISRFGYAIFPKPGGDKIGRRRLDTHLVGIQALGATCDYHSDMQAYELTASRLSGTYMLLDEASVTGTANILMAAVLADGITTIYNAACEPYLQQLCKMLLSMGAHIEGVGSNLLRIEGVQSLHGCEHKMLPDMIEVGSFIGMAAMTASELLIKDVSVPDLGIIPASFRRLGIAVEQQGDDLFIPKQEHYEIETFMDGSIMTIADAPWPGLTPDL... | 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 biosynthe... |
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
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Q8NTF4 | MNDFKKVSESLETALRNEFDFRFATEVSLKEISRWRIGGPAAVFAEPSSINEICALLAFMKNRPEPVVVVGGTSNILFDSDGFGGLVIKLGENFSNFIIEGSRIRAQAGASVPQLVRAVATEGLEGIVHAGGIPGTVGGLVVMNGGTQRRGIGEHVTKVLVTDAEGSIRELNANELQFTYRNSVLKNSETTVLEVELLLKPGNAGELLAELETILDQRSQKFPEDLPNCGSTFLSDPAMYSIVGPPGKAIEDAGLKGLRRGSAEISMQHANFIVNHGDASDDDILWLISAVRKEVYSRTGFVMDCEVLYLSYSGDFRPAH... | 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
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Q67RL6 | MDVHGAAYATHGKGVTGIAALDIQQGVSLRDYSTMRLGGWAAYLAHVRSPAEVEEGIAWAEARHLPVIMVGGGSNIIWRDEGFAGLVLVNRIPGFELADQGGHLLLTVGAGENWDSVVARAVAAGASGIERLSLIPGTAGATPVQNVGAYGQEIADVLVSVDAYDRQERRFVRIPAAECAFGYRRSRFNQADRGRFFITALTLRLLREPPRAPFYPALGRYLEERGLTHPTVQQVRDAVIAIRRAKLPDPAHVANCGSFFRNPIIPAPQAAELLRRYPDMPHWPVPGGGVKLAAGWLIDRAGFRGVADPETGMGTWPAQA... | 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 | MDSSLAQEIAAIDGVELDSEVTFADLTTLRIGGKPRSAVRCQTTEALVSAIKLLDDASLPLLIVGGGSNLVVADGDLDVIAVIIETDDVSINLTDGLLTADAGAVWDDVVHLSVDAGLGGIECLSGIPGSAGATPVQNVGAYGTEVSDVLTRVQLLDRTTHQVSWVDASELDLSYRYSNLKFTNRAVVLAIELQLLTDGLSAPLRFGELGRRLAISEAEPHPRRPVRMVRDAVLELRRAKGMVVEHTDHDTWSAGSFFTNPIVDPALADAVFEKVGEPTMPRFPAGDGKEKLSAAWLIERAGFKKGHPGAGAKASLSTKH... | 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
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Q6FAZ1 | MIHIQHQVQLKPFNTLNLDVVASHYIKVQSVNELIEALDYAEQQQLNALILSGGSNMLLPQSLDALVLHIDIQGLEMIDEDSESVKIKVGGGQIWHDFVLMTTQKGWYGLQNLALIPGLVGASPVQNIGAYGVEVGEFIELVHVYDRSEKSVKTISCADCKFAYRHSIFKDEPYRYIITHVTFKLFKTPNLKLSYGDLLKAVGNEQTPENLQKQVIQIRESKLPNPKEYPNVGSFFKNPVISRQDFNQLLTEFPLIPHYPQPHDRVKIAAGWLIDQAGWKGKRLGAVGMFEKQALVLVNYANATLIDVQHTYRHVQSDIQ... | 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 | MTDPPALSALTTMRVGGTPERLLEPADRDALVATAREVWSTGDEWLLLGGGSNTIAADDGFEGTVLRIVTRGVERLAAEKGRIRLRVQAGEPWDALVALTVRNGWAGIEALSGIPGSTGAAPVQNIGAYGQEIESALIGVEFLDYLTGEVYTLARAELGLGYRTSALKRGMAGVVLSVDLELADHSVPGGVGASLSAPIAYAQLADALAVPLGSRVSVDELRRAVLALRASKGMVLDPADPDSVSAGSFFTNPIVSENVARALPSDAPRWSLGPPEPDTILSLGPEGVHPLDVPPFAAGPYEAKLSAAWLIENAGIRSGF... | 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 | MIDNKRGSSYLNSLPEGLSAEECDRYSAVVSLCWNVLGELQDVEFKWHEPLAYHTTFRVGGPAACLARPRSESALLALLERVRENSVPYVVLGGGSNVLVTDGPIPALVIQLIHVAAGLAFNKGRSSSRPLVVVGAGVPISRLLRFCVRNELGGLECLVGIPGSVGGAVVMNAGTAEGTIAEALEWLDALDGAGQRQLVFKADLPAGYRSMGLPEAWLILGGAFRLHVSSGRSLKREMRSLMVRRKATQPLGRPSAGCVFKNPVEAPAGALIERAGLKGFRMGNAQVSDKHANWIINLGSARARDILALISLVENEVFGK... | 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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