ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A4G5P1 | MPDIDKHKLSLSFSRAAAQYDAIAGFQQQVAARLAQLLPAIPATCVLDGGCGTGTSSALLTRHWPDALLLACDLSPEMVRQAHARQLTAVCGDLEQLPFSKACFDVVWSSLVLQWCQPQLAYPELQRVLKHGGRLLFSTLTSGSLHELESTFGEIDRHRRVLPFASEQQVVDALYAAGFEHVQCQAERWVTQHADLKTLLTSIRGIGANQTGAARRPGMMGKTQWQAAQVRYENLRDADGMLPLTYSLLFVSAEKSRAQD | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28618
Sequence Length: 260
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
C1D5S5 | MTEAFYTDKSRVRASFDRAAATYDRAAVLQREVCDRMATRLDLIRHAPARVLDAGSGTGYGAGLLRARYPEAQVTELDLAPSMLRASRDKQLPQGRLRRLFARAPALVCADLEQLPLASGSLDMVWSSLALQWLNTPDAVLAEFHRVLRVDGLLMFATLGPDTLKELRQAFAGIDGATHVNQFIDMHDMGDALVRAGFATPVMDVERIVLTYDEVKAVMRDLKAIGAHNATAGRGRGLMGRQAWQRIEAAYDRLRQDGRLPATYEVVYGHAWRPAARPRRKLDDGRDIIEFHPHAPA | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33014
Sequence Length: 297
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
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Q5ZT34 | MTVNNEISKAFSKHADDYERVAKVQKEIGSRLFERLQYLKIAPRRILDLGCGPGFFSKELALLYPKAQIVGMDLSFAMLEQARKKQGWRRKWPLVSADMQKMPFATGAFDLVFANQVIHWSSSLGMVFRELNRVMNVNGCLMFTTLGPDTFKELQTAWSAANQYAHVNEFVDMHDIGDCLIAEHFMDPVIDMELLSIHYETLPQLLLALKTQGVRNINPKRNHGLTGKSAWKQFEAQYATMRTTTGKYPLTYEVVYGQAWKGAQRKMEQGIETWIPVSRVVKKS | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32488
Sequence Length: 284
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
A0L3L9 | MNLPNRGEGNRNGRVGKNFGRALNYHRKALVQQHVADELAERLVDFPLPERPRVLEIGCGTGFLSRHLMRQWPGGSFLFTDISAPMLVRCQSHLSDLPGQRQFMVMDGEHCAVRGPFDLVVSSMAMQWFGDLPGALQGLSSLLKTNGMLAFATLGDETFREWRGVCAQYGSPFGRPDYPDVAQLQEMWPSGGEGDVEEDHIPVAHSSGHGFLRALREVGAHQPSGQHRPVSAALMRRMLQATRGGQHGFTVTYHVLYGFYTRSFDDRPIH | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30083
Sequence Length: 270
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
A6W0X8 | MLITPDISALSYKRQLAKRFDRASQSYDSYADFQKVVLERLLAMLPLNQADVVLDLGTGTGQALGILSERLNPKCNIALDLSLQMLAVASERFSSLHNTHYVCADAERLPLQDRSCDLVFSSLAIQWCLSPLDLFKELYRVIKPGGYVVFSTLSQGSMPEISKAWFGLDNKEHVHQYMASDALLDSIRASELNLLSSQLSNISMWFDSPESAIYSLKKVGASLIASDGDPSVSPSKWKAFLLEYEKQRNELGIPLSYQVSFVVAQRPNSI | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30062
Sequence Length: 270
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
Q609U9 | MNSLPRPDIGPFADTPEKRWVGVSFGAAAVGYDGVAALQREVGESLLAGIRHLGPPPARMLDLGAGTGHFSGLLVAAFPTAECLALDIAEGMLRFLRSHRPGADGMGLVVGDAEALPLADESVDLIFSNMAFQWCERLDRAISECCRVLRPGGRLAFSTFGEATLAELRMAWRAVDGYTHVNAFATRRSVEQELRAQGFTKIRLDARTLRRGYPSVLALMKELKALGARNLTRNRPRHLLSRHTLERVSEAYGRLPGMASAVTASFEVLTALVEK | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29869
Sequence Length: 275
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
A1U4A9 | MAKHTFFVTGTDTGVGKTIVSAAILEAAKAAGKRTLAMKPIASGCDQTPEGLRNEDALMLQAAITEKLPYDTINPIALEPAIAPHVAAQQAGKQVTAQRIVGFCRGMQIRPADLLLIEGAGGWRVPLNDRETYAAVPGELKLPVILVVPLQLGCINHAMLSAEAIRADGLVVAGWVGNHPEEQVMSCEQDTLNYLSTHLGAPCLGVLPWLENTDTAEMPAILSRYLNITPLIEN | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
Sequence Mass (Da): 24936
Sequence Length: 234
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
Q58695 | MIFITGTDTGIGKTYVSSILAENLKKMGINVGYLKPVETGGREDTLTLKNILNTDDDLDLMNPINLKLPLSPNIAFDVENSPLTLDEIKEKIKNAYETLKEKYDFLIVEGAGGVCVPIKEDFLMSDLIKFLGLDAVVVSRPNLGTINHTLLTVEHLRNKGINVRGVIINCITDLSEVLYYEKTFETIEKVGNIEIIGIVKSREDFEIDFEKILR | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
Sequence Mass (Da): 23935
Sequence Length: 214
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
B8IBW1 | MSTLFVAGAGTEIGKTYVTAALTRALRASGRPVRALKPVASGVPDLSDPDFSASDTALLLAAQDLPVTPETVAAMTPWRFAAPLAPDLAAAREGRSLALADLVAWCETAIAAPAPGTAVLIEGVGGLMSPLTAEATGLAWLKALRLPVLLVSGSYLGAISHALTAIETLHHHAVDLRAVVVSETPGAPTPPETVAEAIARHAGVRVLCVARGGGFPAEGLDVVPA | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
Sequence Mass (Da): 22754
Sequence Length: 225
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
B0JX07 | MNSLLIAATDTDAGKTVVTTGLVAYWQKYYPSKALGLMKLMQTGQGDREWYEGLFQGQLEMITPLQYQAPLAPPVAADLEGRDIPLGTVWQALLNLQKSQDLVLIEGLGGLGCPVTHELTLADLAAQWRLKTLLVVPVKLGAISQTVANIALAEQKKVNLGGIILNCLEPRTETEIEQLTPIDLIQSLTNCPVLGVFPFIEDRRDLDKLASVVASWPEIKLSSI | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring (By similarity). This cyanobacterium does not encode bioA (which catalyzes the formation of the precursor for this reaction in the cannonical pathway), instead it encodes bioU, which replaces bioA and also performs the first half of the cannonical BioD reaction. Thus in this organism BioD has a different substrate (By similarity).
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
Sequence Mass (Da): 24417
Sequence Length: 224
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
B1MBZ5 | MTILLVTGTSTGVGKTVATAALAAAAVRQGIDVTVCKPVQTGDDHDAGEVARLSGVTRVQTLVRYPEPLAPVASASRAGLELLDHTQMATAIVALDRPGALTLVEGAGGLLVELAADGKTLRDLAMVLDAPVLVVTTADLGTLNHTALTLEALAVQSVPCAGLVVGSFPAEPDLAQRLNRENLANQFGTPVRAVIPEGAARLMPPVFAELSIELFEPQWVAGLVA | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
Sequence Mass (Da): 23095
Sequence Length: 225
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
A0QX66 | MTVLAVTGTDTGVGKTVTTAALACAARLARRDVAVCKPVQTGTIDGDDDLGEVRRLSGVTALHGGWRYPEPLAPVAAAGRAGAPLPTRTELVGSVRAVDAAGRLTIVEGAGGLLVALGADGVTLRDLAHDLGAQVLIVVSPGLGTLNHTALTLEALAAHGLSCAGLVIGAWPAEPGVAELDNRTALEALAPVRAVLPAGAGAASPERFEALSAAAFDADWITSLS | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
Sequence Mass (Da): 22430
Sequence Length: 225
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
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C8V1D1 | MGDSPKCLRDSLREALRRREDKLCRRKLTILPSSSVDFSSNDFLSLSTSPAYRARFLDILQQAPPLHPFASGGSRLLDGNSAYAEELENFIAAFHNAPSGLLFNSGYDANVGVFSSIPQPGDLIVYDELIHASAHEGMRLSRAGKRIKFPHSSPDGLRAVLQAEITADPRLLQGRRNVFIAFESVYSMDGDVAPIREFVEIVDQLLPYGNGYFLVDEAHATGVFGPRGSGVVQELGLEDRMFVRVHTFGKALASHGAIVLCCADTRDYLINYARSLIYTTALGFPFLASIRAAYELLVEGKTEQLQHKLGQLIAHFRTGLDNLNHKDSSTFEVEHFTNSPIFSLRSSVPRVLASVCQEQGYTVRAIMPPTVPAGKERVRVCLHAGNTVEEVDGLLETIATWLQRMEKQKARL | Function: 8-amino-7-oxononanoate synthase; part of the cluster involved in the biosynthesis of biotin (also known as vitamin B8 or vitamin H), a water-soluble vitamin that functions as a prosthetic group of many carboxylases, such as acetyl-CoA carboxylase and pyruvate carboxylase . Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON) (By similarity).
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 45580
Sequence Length: 412
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
A7HMM1 | MFNYKILEDEMENLKNEGLYINIRTLESPQGAWIVVNGKRVLNLCSNNYLGFASDERLKQAAKKAIDEWGVGPGAVRTIAGTMKIHEELEKALAEFKGADATIFLQSGFIANQAAIPTVFGDENDAIISDELNHASIIDGVRLSKAKRYVYKHNDMNELEARLKEARDVQKARRILIITDGVFSMDGDIAPLPEIVELAEKYEAAVMVDDAHGEGVLGRGGRGIVDHFGLHGRVDMEIGTLSKAFGVLGGYIAGKETLIRYLKQKARPFLFSTGLTPADVAACLEAVKILQESDERVKRLWDNANYFKSEMKKLGFDLGVSQTPITPVMLYDAKVASQFSRELFEEGIFAQSIGYPTVPKGKARIRVMISAVHTKEDLDFALDKFEKVGKKFAII | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 43765
Sequence Length: 395
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
B9M8U3 | MQTFGEELESLRAAGLFRSMRLVEGEQSSRIILDGREVLLLCSNNYLGLADHPLLKEAAIRAVERFGVGSGAARLVSGNMELHFRLEERIAAFKGTEAALVFNSGYAANTGIISAIAGRGDLIFSDRLNHASIVDGALLSRAKVIRYSHNDMVALRRLLEENRSTSGRRIIVTDGVFSMDGDLAELAELAALKEEFGALLMVDDAHGTGVLGEHGRGSAELCGVMDRVDIHMGTLGKALGSFGAYAAASKEIIDYLVNRARSFIFSTSLPPAVLAASIAAFDLVDSQAGADLRKGLAANSTRFKDGLENAGFNTMGSETQIVPAFVGGAAETMKFSRKLLDQGIFVQGIRPPTVPVGSCRLRCTLMATHSQADVDRAVSAIAHVGRKLGVTGC | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 41786
Sequence Length: 393
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
Q5KY23 | MKTELTVKLHEWEQKAQKRQLRRAEASGATVILNGKPMLNLASNNYLGLADDRRLIEAGCEAMRAYGAGAGASRLVVGNHPLYERAEAALKQWKKAEAALIFNSGYTANIGVLTALIGRDDLVFSDKLNHASLIDGIRLSKAACFRYRHHDIDQLESLLKQSPPAKRKWIVTDAVFSMDGDMAPLEELVELKRRYRAVLLVDEAHSGGVFGPNGEGLLHHFGLEKEEDVIAIGTFSKALGSFGAYVTGEPWLVDYLINSARSLIFTTALPPSVLAANEAAIHIVQAEPKRRERLHALSERFRTKLKRLGFDTGGSETPIVPVIVGPNDRAVAMSEQLQEAGIAAVAIRPPTVPEGTARIRFSITAAMTEEDIDMAVDCIALAGKRIGLIS | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 42524
Sequence Length: 390
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
Q749W3 | MTRSIAGELQQLREQGLYRSLRTVAGSQGSRVVAEGREVVLLCSNNYLGLADHPSLKRAAVEAVERYGTGSGASRLVSGTMELHAALEERLARFKGTEAALVFNSGYAANSGIIPALVGRGDVVFSDRLNHASIVDGCLLSRARFVRYPHNDMNALERLLAEHRGAGRMLIVTDGVFSMDGDLAPLPALVALKRQYGALLMVDDAHGTGVLGESGRGSAEQFEVAADIDLQMGTLGKALGGFGAYVAASAEVVELLINRARSFIFSTSLPPAVLAAARAALDLVDSPEGKALRRRLARSAALFRDALQEAGFDTMGSETQIVPALVGEAEPAMTFTRRLLEEGFYVQGIRPPTVPAGTCRLRCTLMATHDESDLERAVAAMARIGKELGIV | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 41593
Sequence Length: 391
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
A5G6I9 | MQTFAEELAALRMEGLFRSMRLVEGNQSKRAVLDGREVLLLCSNNYLGLADHPLLKEAAIRAVERYGVGSGASRLVSGTMELHEALEARIAAFKGTNSALVFNSGYAANTGIISAIAGRGDVIFSDRLNHASIVDGALLSRARFVRYPHNNISVLRRLLEDTEVASGRRLIVTDGVFSMDGDLAKLSELVALKKEFDALLMVDDAHGTGVLGDGGRGSAEQCGVMAEVDIHMGTLGKALGSFGAYAAASREIIDYLVNRARSFIFSTSLPPAVLAASQAAFELVDSPSGAALRLALAANTIRFKAGLQAVGFDTMGSETQIVPVYVGGAQQTMEFSRLLLEEGVFVQGIRPPTVPAGSCRLRCTLMATHSENDLDQAITAITAIGEKLGVI | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 41490
Sequence Length: 391
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
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Q5NZF6 | MNRPDLVLLHGWGLGPQVWSALTPYLPAGLRVRTPALPGHGGTPARGPTLEAWSDALLPELPDDAVVCGWSLGGLVALDLARRHPHKVARLVLIGTSPCFVTRPENAAAPWPYGLAASTVTGFIDDFAHDPAATLRRFVALQALGDARRRTVSNALNAALANLEQCRPAALGAGLELLADTDWRAALDDVRQPVQLIHGAGDALMPLAAAEWLATRLPDARLARFDDCGHAPFLSHPEDCAVLIEDVVRG | Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol
Sequence Mass (Da): 26598
Sequence Length: 250
Pathway: Cofactor biosynthesis; biotin biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.1.1.85
|
Q89A54 | MNKKLHWKSLGTGTTNLILIHGWGVNSKIWSILVQSQLYQHFKLHFVDLPGFGHSNQLLPMTLNDTAELLSVYIPKNSILLGWSMGGLIASKIALNYPQKIKGIISVCSSPCFIVRPNWPGIPKKIFLKFYNKLNINFDRTISEFITLQSHNTNYLEIKNLKQQILSQPYPTIYTLKKNLETIFKTDLRTKIKKLKIPMLRIYGSLDTFVPKKIREILDILWPKTKSITIAHASHIPFVSHQKEFYESIINFKNYLNTLKITCQK | Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol
Sequence Mass (Da): 30655
Sequence Length: 265
Pathway: Cofactor biosynthesis; biotin biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.1.1.85
|
Q7NPW5 | MNLFVETLGQGPDVVMLHGWGLHGGVFARVAEQLATRFCVHLVDLPGHGASPALPRFDADAVADLLAAHFPLPAQVVGWSLGGLIAQHWAARHPDKVKSLALVATSPRFVRDETWPHAQARASIEAVAQSLDGAFEQTLERFLALQMMGAPSARDTLKALRGELFSHGRPQGLLPALGLLLEADARALAGRIQCPAALFYGARDAITPIGAGRWLAESLPDAVLYEFPQASHAPFLSHEQDFVRALAEHLETQA | Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol
Sequence Mass (Da): 27301
Sequence Length: 254
Pathway: Cofactor biosynthesis; biotin biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.1.1.85
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O07631 | MKLRNDLRNIAIIAHVDHGKTTLVDQLLHQAGTFRANEQVAERAMDSNDLERERGITILAKNTAINYKDTRINILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGCMPQTRFVLKKALEQNLNPVVVVNKIDRDFARPEEVIDEVLDLFIELDANEEQLEFPVVYASAINGTASLDPKQQDENMEALYETIIKHVPAPVDNAEEPLQFQVALLDYNDYVGRIGIGRVFRGTMKVGQQVSLMKLDGTAKSFRVTKIFGFQGLKRVEIEEAKAGDLVAVSGMEDINVGETVCPVDHQDPLPVLRIDEPTLQMTFVVNNSPFAGREGKYVTARKIEERLQSQLQTDVSLRVEPTASPDAWVVSGRGELHLSILIENMRREGYELQVSKPEVIIKEIDGVRCEPVERVQIDVPEEHTGSVMESMGARKGEMVDMINNGNGQVRLIFTVPSRGLIGYSTEFLSLTRGFGILNHTFDSYQPMQAGQVGGRRQGVLVSMENGKATSYGIQGIEDRGVIFVEPGTEVYEGMIVGEHNRDNDLVVNVSKMKQQTNVRSATKDQTTTIKKARIMSLEESLEYLNEDEYCEVTPESIRLRKKILNKNEREKAAKKKKTAGLS | Function: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 68389
Sequence Length: 612
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
O25225 | MKNIRNIAVIAHVDHGKTTLVDGLLSQSGTFSEREKVDERVMDSNDLERERGITILSKNTAIYYKDTKINIIDTPGHADFGGEVERVLKMVDGVLLLVDAQEGVMPQTKFVVKKALSFGICPIVVVNKIDKPAAEPDRVVDEVFDLFVAMGASDKQLDFPVVYAAARDGYAMKSLDDEKKNLEPLFETILEHVPSPSGSVDEPLQMQIFTLDYDNYVGKIGIARVFNGSVKKNESVLLMKSDGSKENGRITKLIGFLGLARTEIENAYAGDIVAIAGFNAMDVGDSVVDPANPMPLDPMHLEEPTMSVYFAVNDSPLAGLEGKHVTANKLKDRLLKEMQTNIAMKCEEMGEGKFKVSGRGELQITILAENLRREGFEFSISRPEVIIKEENGVKCEPFEHLVIDTPQDFSGAIIERLGKRKAEMKAMNPMSDGYTRLEFEIPARGLIGYRSEFLTDTKGEGVMNHSFLEFRPFSGSVESRKNGALISMENGEATAFSLFNIQERGTLFINPQTKVYVGMVIGEHSRDNDLDVNPIKSKHLTNMRASGSDDAIKLTPPRTMVLERALEWIEEDEILEVTPLNLRIRKKILDPNMRKRAKK | Function: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 66676
Sequence Length: 599
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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H9L427 | MIENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIIYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLTHLGLERIDSNIAEAGDIIAITGLGELNISDTICDPQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDIRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVILVPPIKMSLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRGQKEE | Function: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). A ribosome-stimulated GTPase, GTPase activity increases 4 fold in the presence of 70S ribosomes. Binds 70S ribosomes in the presence of GTP or its non-hydrolyzable analog GMPPNP; in the presence of ppGpp or under stress conditions it binds to 30S ribosomal subunits .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 67377
Sequence Length: 607
Domain: Has 5 domains; domain I (residues 1-202, also called the G domain), II (203-305, also called the beta barrel domain), III (306-386) V (387-479) and the C-terminal domain (CTD 480-607) which is BipA-specific. Domains I-V are homologous to domains in EF-G and LepA; although the domains are similar, their relative arrangement among these proteins is different. Domains I and II are not required for ribosome binding, although in their absence no 30S binding under stress is seen, whereas domains III, V and the CTD are required to bind both 70S and 30S ribosomes. The data suggests interdomain communication modulates GTPase and ribosome binding.
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q44056 | MYVLSVEKPTLRNKFAAGIGVVLVCVVASFIPTPVFALDTTKLIQAVQSEESALHARVGMTVFDSNTGTTWNYRGDERFPLNSTHKTFSCAALLAKVDGKSLSLGQSVSISKEMLVTYSPITEKSLSPETVTFGKICQAAVSYSDNTAANVVFDAIGGATGFNAYMRSIGDEETQLDRKEPELNEGTPGDVRDTTTPNAMVNSLRKILLGDALSASSRSQLTQWMLDDQVAGALLRASLPSDWKIADKTGAGGYGSRSIVAVIWPPSKQPLVVGIYITQTKASMQASNQAIARIGVVLKDTVAP | Function: Hydrolyzes carbenicillin. Methicillin and oxacillin are weakly hydrolyzed.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 32428
Sequence Length: 304
EC: 3.5.2.6
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P10424 | MKNKKMLKIGMCVGILGLSITSLVTFTGGALQVEAKEKTGQVKHKNQATHKEFSQLEKKFDARLGVYAIDTGTNQTIAYRPNERFAFASTYKALAAGVLLQQNSTKKLDEVITYTKEDLVDYSPVTEKHVDTGMTLGEIAEAAVRYSDNTAGNILFHKIGGPKGYEKALRKMGDRVTMSDRFETELNEAIPGDIRDTSTAKAIARNLKDFTVGNALPHQKRNILTEWMKGNATGDKLIRAGVPTDWVDADKSGAGSYGTRNDIAIVWPPNRSPIIIAILSSKDEKEATYDNQLIKEAAEVVIDAIK | Function: Acts preferentially on penicillins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 33596
Sequence Length: 306
Subcellular Location: Secreted
EC: 3.5.2.6
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Q59514 | MQRRHFLQKTLLALPIIFSGNLLTGCKTNLSDDYLPDDKITNNPNLLQNKLKEILPIWENKFNAKIGMTIIADNGELSSHRGNEYFPVNSTIKAFIASHILLLVDKEKLDLNEKIIIKESDLIEYSPVCKKYFDENKPISISELCEATITLSDNGSANILLDKIGGLTAFNQFLKEIGADMVLANNEPLLNRSHYGETSDTAKPIPYTKSLKALIVGNILSNQSKEQLITWLINDKVADNLLRKYLPKNWRIGDKTGTGSESKNIIAVIWNENNKPYFISLFITQPHDGKSLDFKNQKDEIMAQIGKEIYPFL | Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Location Topology: Lipid-anchor
Sequence Mass (Da): 35383
Sequence Length: 313
Subcellular Location: Cell membrane
EC: 3.5.2.6
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P52700 | MRSTLLAFALAVALPAAHTSAAEVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVLLDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRTGAKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIVFTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPHLIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYADAAEQKFDGQLAKETAGAR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30801
Sequence Length: 290
Subcellular Location: Periplasm
EC: 3.5.2.6
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Q9S169 | MRYIRLCIISLLATLPLAVHASPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARGTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR | Function: Hydrolyzes ampicillin. Can also hydrolyze cephaloridine, aztreonam and ceftazidime with a low catalytic rate.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 31166
Sequence Length: 286
EC: 3.5.2.6
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P04190 | MKKNTLLKVGLCVGLLGTIQFVSTISSVQASQKVEKTVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGEVGDKGLLLHTLDLLK | Cofactor: Binds 2 Zn(2+) ions per subunit. The enzyme can also function with only 1 Zn(2+) ion .
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Active on cephalosporin and penicillin.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 28092
Sequence Length: 257
Subcellular Location: Periplasm
EC: 3.5.2.6
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O07293 | MQRSLSMSGKRHFIFAVSFVISTVCLTFSPANAAQKLSCTLVIDEASGDLLHREGSCDKAFAPMSTFKLPLAIMGYDADILLDATTPRWDYKPEFNGYKSQQKPTDPTIWLKDSIVWYSQELTRRLGESRFSDYVQRFDYGNKDVSGDPGKHNGLTHAWLASSLKISPEEQVRFLRRFLRGELPVSEDALEMTKAVVPHFEAGDWDVQGKTGTGSLSDAKGGKAPIGWFIGWATRDDRRVVFARLTVGARKGEQPAGPAARDEFLNTLPALSENF | Function: Has a broad substrate profile, hydrolyzes amoxicillin, ticarcillin, cephalothin, ceftazidime, cefotaxime, and aztreonam, but not imipenem or cephamycins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30602
Sequence Length: 275
EC: 3.5.2.6
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P13661 | MKNTIHINFAIFLIIANIIYSSASASTDISTVASPLFEGTEGCFLLYDASTNAEIAQFNKAKCATQMAPDSTFKIALSLMAFDAEIIDQKTIFKWDKTPKGMEIWNSNHTPKTWMQFSVVWVSQEITQKIGLNKIKNYLKDFDYGNQDFSGDKERNNGLTEAWLESSLKISPEEQIQFLRKIINHNLPVKNSAIENTIENMYLQDLDNSTKLYGKTGAGFTANRTLQNGWFEGFIISKSGHKYVFVSALTGNLGSNLTSSIKAKKNAITILNTLNL | Function: This is an oxacillin-hydrolyzing beta-lactamase.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30880
Sequence Length: 276
EC: 3.5.2.6
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O84955 | MIIRFLALLFSAVVLVSLGHAQEKTHESSNWGKYFSDFNAKGTIVVVDERTNGNSTSVYNESRAQQRYSPASTFKIPHTLFALDAGAVRDEFHVFRWDGAKRSFAGHNQDQNLRSAMRNSTVWVYQLFAKEIGENKARSYLEKLNYGNADPSTKSGDYWIDGNLAISANEQISILKKLYRNELPFRVEHQRLVKDLMIVEAKRDWILRAKTGWDGQMGWWVGWVEWPTGPVFFALNIDTPNRMEDLHKREAIARAILQSVNALPPN | Function: This is an oxacillin-hydrolyzing beta-lactamase.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30449
Sequence Length: 266
EC: 3.5.2.6
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Q00982 | MKTIAAYLVLVFYASTALSESISENLAWNKEFSSESVHGVFVLCKSSSNSCTTNNAARASTAYIPASTFKIPNALIGLETGAIKDERQVFKWDGKPRAMKQWEKDLKLRGAIQVSAVPVFQQIAREVGEIRMQKYLNLFSYGNANIGGGIDKFWLEGQLRISAFNQVKFLESLYLNNLPASKANQLIVKEAIVTEATPEYIVHSKTGYSGVGTESSPGVAWWVGWVEKGTEVYFFAFNMDIDNESKLPSRKSISTKIMASEGIIIGG | Function: Hydrolyzes both oxacillin and methicillin.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 29432
Sequence Length: 267
EC: 3.5.2.6
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P0A3M4 | MKKILLLHMLVFVSATLPISSVASDEVETLKCTIIADAITGNTLYETGECARRVSPCSSFKLPLAIMGFDSGILQSPKSPTWELKPEYNPSPRDRTYKQVYPALWQSDSVVWFSQQLTSRLGVDRFTEYVKKFEYGNQDVSGDSGKHNGLTQSWLMSSLTISPKEQIQFLLRFVAHKLPVSEAAYDMAYATIPQYQAAEGWAVHGKSGSGWLRDNNGKINESRPQGWFVGWAEKNGRQVVFARLEIGKEKSDIPGGSKAREDILVELPVLMGNK | Function: Oxacillin-hydrolyzing beta-lactamase. Confers resistance to beta-lactam antibiotics but at a significantly lower level than the TEM bla gene product.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30568
Sequence Length: 274
EC: 3.5.2.6
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A1KXI1 | MKVLVLFCLVSLAAAGPLKDALNKAQVDAFYAEGYIVDGSNAADGDAPYQVSLQRTSHFCGGSIIADNYILTAAHCIQGLSASSLTIRYNTLRHNSGGLTVKASRIIGHEKYDSNTIDNDIALIQTASKMSTGTTNAQAIKLPEQGSDPKASSEVLITGWGTLSSGASSLPTKLQKVTVPIVDRKTCNANYGAVGADITDNMFCAGILNVGGKDACQGDSGGPVAANGVLVGAVSWGYGCAQAKYPGVYTRVGNYISWIKGKGVPV | Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Mass (Da): 27555
Sequence Length: 266
Subcellular Location: Secreted
EC: 3.4.21.4
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Q03170 | MKFLLAFSLLIPSVVFASSSKFQQVEQDVKAIEVSLSARIGVSVLDTQNGEYWDYNGNQRFPLTSTFKTIACAKLLYDAEQGKVNPNSTVEIKKADLVTYSPVIEKQVGQAITLDDACFATMTTSDNTAANIILSAVGGPKGVTDFLRQIGDKETRLDRIEPDLNEGKLGDLRDTTTPKAIASTLNKFLFGSALSEMNQKKLESWMVNNQVTGNLLRSVLPAGWNIADRSGAGGFGARSITAVVWSEHQAPIIVSIYLAQTQASMAERNDAIVKIGHSIFDVYTSQSR | Function: Hydrolyzes penicillin, ampicillin and carbenicillin but not other antibiotics including oxacillin, methicillin and cloxacillin.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 31348
Sequence Length: 288
EC: 3.5.2.6
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A0A3B7TNM4 | MHCTVFFLLIACAKSSYGQTRSVSTAKSESKSDEYSYNSDAIDQSRLLRGAVNPVSENMALRKFIFDMPEMLRPEHFEPIFINPAAVKEVIKDYLAYGEALCGSGYDPRLLALFGVRPTVLKQELMKAKGVTLSVMPSSRKRPRALDEVESEVENFRNVLKDFFIPPTTTNPSKLIPDDIETLVPEHVSAHFNSLVYLMYFAVLHFDSQELATMSSSVLLKYALQKNLLLREKIESGTLGEWERDFRLMRVLNVYKSEQT | Function: Secreted effector that triggers a robust hypersensitive response (HR) in Lactuca serriola LS102. The response to BLN06 was visible as strong necrosis . Although effector recognition is frequently associated with single dominant R gene loci, the recognition of BLR38 requires 2 unlinked loci that display incomplete dominance .
Sequence Mass (Da): 29562
Sequence Length: 260
Domain: Has the canonical translocation motif RxLR, but lacks the canonical EER motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Secreted
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P25916 | MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEEKRIITDDEIISLSIEFFDQSRLDRKVNKEKPKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKMSHQRDGLTNAGELESDSGSDKANSPAGGVPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSANHQSSFASRPRKSSLNGSSATSSG | Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2 (By similarity).
PTM: May be polyubiquitinated; which does not lead to proteasomal degradation (By similarity). Monoubiquitinated.
Sequence Mass (Da): 36708
Sequence Length: 324
Subcellular Location: Nucleus
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Q53HL2 | MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK | Function: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.
PTM: Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169 and Thr-230. Phosphorylation (probably by CDK1) promotes targeting of the CPC to centromeric DNA.
Sequence Mass (Da): 31323
Sequence Length: 280
Domain: The C-terminal region (aa 207-280) represents the dimerization motif.
Subcellular Location: Nucleus
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Q8BHX3 | MAPKKRSSRGTRTNTLRSRKLASFLKDFDREVQVRTKQIESDRQTLLKEVENLYNIEILRLPKALQGMKWLDYFALGGNKQALEEAAKADRDITEINNLTAEAIQTPLKSVKKRKVIEVEESIKEEEEEEEEGGGGGGRTKKSHKNLRSAKVKRCLPSKKRTQSIQGRGRSKRLSHDFVTPAMSRLEPSLVKPTPGMTPRFDSRVFKTPGLRTPAAKEQVYNISINGSPLADSKEISLSVPIGGGASLRLLASDLQRIDIAQLNPEALGNIRKLSSRLAQICSSIRTGR | Function: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment (By similarity).
PTM: Phosphorylated by TTK, essentially at Thr-94. Phosphorylation (probably by CDK1) promotes targeting of the CPC to centromeric DNA.
Sequence Mass (Da): 32214
Sequence Length: 289
Domain: The C-terminal region (aa 216-289) represents the dimerization motif.
Subcellular Location: Nucleus
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O14613 | MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGSDMFGDISFLQGKFHLLPGTMVEGPEEDGTFDLPFQFTRTATVCGRELPDGPSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLETPQPSPQEGGSVDIWRIPETGSPNSGLTPESGAEEPFLSNASSLLSLHVDLGPSILDDVLQIMDQDLDSMQIPT | Function: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22484
Sequence Length: 210
Domain: The CRIB domain mediates interaction with CDC42.
Subcellular Location: Endomembrane system
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Q8JZX9 | MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGDDMFGDISFLQGKFHLLPGTAVEEAEEDGSFDLPFQFTRTTTVCGRELPDGLSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLESPQPSPQPSPQGAGNVDVWRIPEAGSPHNGMSPEPEAEEPFLSHASSLLSLHVDLGPSILDDVLQIMDHDLGRVQIPT | Function: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22997
Sequence Length: 214
Domain: The CRIB domain mediates interaction with CDC42.
Subcellular Location: Endomembrane system
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B1VN94 | MILVTGATGAVGREVAGRLADAGPVRILARRPERLTVRGTGVEVVQGAYGDRAALDRALRGVDAVFLVTNDPTEPDDERVAAAAAAAGVRHLVKLSMMAVEEPDAEDFITRRQRENEQAVRDSGVPWTFVRPRTFMSNTLSWAPGIRSAGVVRALYGDAPVACVDPRDVAAVAVAALTGTGHEGRAYAVSGPEAITAREQTAQLSRVLGRPLRFEELGVDAARTALMAKYPPPVAEAFLQSAERQRTGAKASVVPTVQELTGRPARPFRDWSAEHAEAFAPE | Function: Involved in the biosynthesis of A factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone), a gamma-butyrolactone autoregulator that triggers secondary metabolism and morphogenesis in Streptomyces . Catalyzes the reduction of the butenolide phosphate produced by nonenzymatic intramolecular condensation of the 8-methyl-3-oxononanoyl-DHAP ester .
Catalytic Activity: a [(3S,4R)-4-alkanoyl-5-oxooxolan-3-yl]methyl phosphate + NADP(+) = a (4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl phosphate + H(+) + NADPH
Sequence Mass (Da): 30055
Sequence Length: 282
EC: 1.3.1.113
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Q5JIZ3 | MREIIERVKEKTTIPVYERTIENVLSAIQASGDVWRIVDLSEEPLPLVVAVVTALYELGYVAFENNQVILTRKGKELVEKYGIGPRADYTCSHCQGRTVEIDAFSELLEQFKEITRDRPEPAHQFDQAYVTPETTVARVALMHSRGDLENKEVFVLGDDDLTSVALMLSGLPKRIAVLDIDERLTKFIEKAADEIGYENIEIFTFDLRKPLPDYALHKFDTFITDPPETVEAIRAFVGRGIATLKGPGCAGYFGITRRESSLDKWREIQRVLLNEFGVVITDIIRNFNEYVNWGYVEETRAWRLLPIKVKPSYNWYKSYMFRIQTLEGSKGFEDEITVGQELYDDEESSTT | Function: Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine. Can also use spermine to produce N(4)-aminopropylspermine.
Catalytic Activity: 2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2 H(+) + N(4)-bis(aminopropyl)spermidine + 2 S-methyl-5'-thioadenosine
Sequence Mass (Da): 40229
Sequence Length: 351
Pathway: Amine and polyamine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.128
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P25125 | MNKEALVQVAEEVRRATGLPVGWRDVERTLGALRATRDLWEAVRLSRVPLRFLVPIWEGLARRGLLRVEEGLDLLAEVPAPRPGEAACPACEGRGLVGERLPGRAAERFLAWAKERPEAIQDFDQGYVTPESTLARVALAWNWGDLEGKEVLVLGDDDLTGLAAALTGLPKRVVVLDADPRIVRFLERAAKAEGLPLEAHVHDLREPLPEAWVHAFHTFFTDPVEGPLGLQAFVGRGLLALEGEGCAGYVGLTHVEASLAKWADFQRFLLENGAVITELRDGFHVYENWGYIEQMRAWPWLPVKRRPEKPWYTSALIRLELLRRADLENARVEGDLQDEEATY | Function: Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine.
Catalytic Activity: 2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2 H(+) + N(4)-bis(aminopropyl)spermidine + 2 S-methyl-5'-thioadenosine
Sequence Mass (Da): 38395
Sequence Length: 343
Pathway: Amine and polyamine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.128
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Q8DAR7 | MSSDIHQIKIGLTDNHPCSYLPERKERVAVALEADMHTADNYEVLLANGFRRSGNTIYKPHCDSCHSCQPIRISVPDIELSRSQKRLLAKARSLSWSMKRNMDENWFDLYSRYIVARHRNGTMYPPKKDDFAHFSRNQWLTTQFLHIYEGQRLIAVAVTDIMDHCASAFYTFFEPEHELSLGTLAVLFQLEFCQEEKKQWLYLGYQIDECPAMNYKVRFHRHQKLVNQRWQG | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 27378
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.3.2.29
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Q3BW59 | MAIHADTHDDLRLFQTGEHACGYWSDRQARDLVLDPHDPRLGAIYPQALAWGFRRSGDLVYRPHCERCRACVPVRIAVAAFHPDRSQRRCLARNQDLVVRVVAAERTDEQLALYRHYLKHRHPGGGMDEHGATEFDQFLIGGWSHGRFLEIREPAIAHLPGRLLAVAVTDVTGHALSAVYTFYTPEAAARSLGTFAILQQIQWAQRERRAHLYLGYWIDGHAKMNYKRRFSALEAYDGRHWRGLPAHASVD | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 28650
Sequence Length: 251
Subcellular Location: Cytoplasm
EC: 2.3.2.29
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A7INB9 | MSEHPRDTPQFYLTAPSPCPYLPGREERKVFTHLVGDKAASLNDVLTQGGFRRSQSIAYRPACEGCKACVSVRICVDDFTPGRSFRRVQADNSDLIGQIKPATPTSEQYALFRSYVTGRHGTGGMADMSVLDYAMMVEDTHVHTRLVEYRKRGPDSRIIPRGTGDLMAVALTDVLTDGLSMVYSFYNPQVHDRSLGTFLILDHITRARQMGLPYVYLGYWVQGSRKMDYKRRYLPQERLTPHGWERVEK | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 28301
Sequence Length: 249
Subcellular Location: Cytoplasm
EC: 2.3.2.29
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Q6ZLD3 | MKEMVSSSTFRAPGGLGFLGPSKIGLIPLRNRSGVRSRVKYIAPKCAVSSARPASQPRFIQHKKEAFWFYRFLSIVYDHVINPGHWTEDMRDDALEPAELYHHGLKVVDVGGGTGFTTLGIVKHVDNENVTLLDQSPHQLEKARQKVALNGVNIIEGDAEDLPYPTDTFDRYVSAGSIEYWPDPQRGIREAYRVLKLGGVACLIGPVHPTFWLSRFFADMWMLFPKEEEYIEWFQKAGFQDVKIKRIGPKWYRGVRRHGLIMGCSVTGVKRSSGDSPLQLGPKAEDVEKPVNPFTFIFRFVMGTICASYYVLVPIYMWMKDQIVPKDQPI | Function: Involved in a key methylation step in both tocopherols (vitamin E) and plastoquinone synthesis. Catalyzes the conversion of 2-methyl-6-phytyl-1,4-hydroquinone (MPBQ) to 2,3-dimethyl-6-phytyl-1,4-hydroquinone (DMPQ, a substrate for tocopherol cyclase), and 2-methyl-6-solanyl-1,4-benzoquinone (MSBQ) to plastoquinone (By similarity).
Catalytic Activity: 2-methyl-6-phytyl-1,4-benzene-1,4-diol + S-adenosyl-L-methionine = 2,3-dimethyl-6-phytylbenzene-1,4-diol + H(+) + S-adenosyl-L-homocysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37439
Sequence Length: 330
Pathway: Cofactor biosynthesis; tocopherol biosynthesis.
Subcellular Location: Plastid
EC: 2.1.1.295
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Q07457 | MTAEPATKKIKLELSDPSEPLTQSDVIAFQKEALFRCINRRRVDFEALRKQYELSRRECIDVSRKLANIMALIVTLARFIETFCTDANEKQLCREIAQGDETLIVQRSDSFMKLLTKYGKPNTTDSNTNSNASDHIQELTTELKNLRKSKEELFYENSQLTEEISALKEYYTNIIRKYDRDESFTIKRVFKEDKTDAVKELREDEKESNENNIKSGNKDSSAINGDNTSKKSEKGDELVQAEDERKEDAENEKLELDLKFSDLRAEINSLSSTIKDLENIRRENEEELIKTRSEVSNLKKQQIAAADQDPDFKSYDHESLLAKIQHLTEQNAELSEINSSFLSKFQVLAKEKEIYTKKVREEFQKSLDSLVEMNSSLEKDVVRIRTARDDLLSKIAILEAEKSKTEVLSDLQHAIDILKEQWTKIDQRSNDTKSSSTQDALIKEIQDLEKGFRELSDLTHKKYSEIINHESVISKLTVEKTKADQKYFAAMRSKDSILIEIKTLSKSLSKSNELILQLKDSDRLLQQKIGNLHKQLDLSQNNERRLIDSSKTETLKIIDLNNTSTKLKRSLEKLQEESNKSIADMTHLETKLNDTEIELKHFKQKASHLESKCEKLHDTLFRGNNKNKGSSDEALVEELANFRTLVYCSLCSKNWKNMAIKTCGHVFCENCCKERLAARMRKCPTCNKAFSSNDLLTVHL | Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Also modulates the formation of double-strand breaks during meiosis.
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): 80692
Sequence Length: 700
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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A8Y3H3 | MRQNRRASMIVNRILITLIVLVSLSFLFLRAGPKFSEADRACIQDEWQENKSLNVSSEINNETYQIVFADVQKEFKWIFLPKEISGNPDILMIVSSNRDNFARRNVIRKSWMNSDKNKIVAEKRMKILFLVGVNSENEKENTVVLKEAEVFGDIIVVDLEDNYQNLPYKSLTILLYGQSKTAESVKLIGKIDEDVIFYPDQLTPLINDGTINMSISAIYGEKWNAGVEVSNKDETNKWFIPKYSFKCQLLPSYLSGPFYLTTRKAAERILKSTKHRKFISVEDVFITGLLAGDVGVEKKQLPSMYMYDETTTDTAKAEILAWHNFKNNAEFLESWENLRLSRCKACRKSRNFRGSRSQLDEERNQ | Function: Transfers N-acetylgalactosamine onto carbohydrate substrates. Involved in susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-3, bre-4, and bre-5. Involved in resistance to the nematotoxic C.cinerea galectin Cgl2.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 42164
Sequence Length: 365
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q6QMT2 | MRQSRRASSRVNRLVVIFIIVASGFLLLYKNTQQFTQIDRECIQDEWQENNNLGNTIDDGSNFRIAFTDIQQNYTWLHLPNFLENSEILMIVSSNCDNFARRNILRKTWMNPENSQIIGDGRMKALFLVGINGADEKLNAVVLEEAKVFGDMIVIDLEDNYLNLSYKTISLLLYSISKTKSPNLIGKIDEDVLFYPDQLTPLINDKTINTSTFSIYGEKYEAGVAVNHGEDNAKWQISKNSFKCSVYPSYLSGPTYFLTRKAAKRIVEATKHRKFISVDVEDVFITGLLAGDVGIKKNQLPFMYMIEEATNDRESYEILAWHTKKRDQQYIEAFESLKLNRCKSCRKSKNPDLEELKEK | Function: Transfers N-acetylgalactosamine onto carbohydrate substrates (By similarity). Involved in susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-3, bre-4, and bre-5 . Involved in resistance to the nematotoxic C.cinerea galectin Cgl2 .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41370
Sequence Length: 359
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q9GUM2 | MAFRHLAVARLKSLLVLCAVLLLVHAMIYKIPSLYENLTIGSSTLIADVDAMEAVLGNTASTSDDLLDTWNSTFSPISEVNQTSFMEDIRPILFPDNQTLQFCNQTPPHLVGPIRVFLDEPDFKTLEKIYPDTHAGGHGMPKDCVARHRVAIIVPYRDREAHLRIMLHNLHSLLAKQQLDYAIFIVEQVANQTFNRGKLMNVGYDVASRLYPWQCFIFHDVDLLPEDDRNLYTCPIQPRHMSVAIDKFNYKLPYSAIFGGISALTKDHLKKINGFSNDFWGWGGEDDDLATRTSMAGLKVSRYPTQIARYKMIKHSTEATNPVNKCRYKIMGQTKRRWTRDGLSNLKYKLVNLELKPLYTRAVVDLLEKDCRRELRRDFPTCF | Function: Catalyzes the transfer of galactose onto proteins or lipids. Required for susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-2, bre-3 and bre-5.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43914
Sequence Length: 383
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
EC: 2.4.1.-
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Q95US5 | MFLCVRILKRKYHELSSFQKLLIFTITIFLLWVLGVVDKFRETSFGDFSWPLETRNLQLRSKFTKYPQCKFSGNGQKIIIIIIKSSAKNGPMRESVRKTWGVFRMIDGVEVMPIFIVGRVENMEIMRRIDVESEKYKDILAISDIDSYRNNTLKLFGAIDYAANPNQCSSPDFTFLVDDDYLVHIPNLVKFAKTKQKEELVYEGFVFDTSPFRLKIHKHSISLNEYPFSRYPPYVSAGAVFLTSETIARFRNSIRKLKMFPFDDVFTGILAKTVNVAATHNENFIFWCRRVSQKEWDDGVIAVHGYARKDLEYEYSQLNGFE | Function: Transfers N-acetylgalactosamine onto mannose groups of carbohydrate substrates. Required for susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-2, bre-3, and bre-4. Involved in resistance to the nematotoxic C.cinerea galectin Cgl2 .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 37587
Sequence Length: 322
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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A0A068ACU9 | MPGRELAPRQNVEFQTLDGLTLRGWLFPAQSRGPAVIITPGFNCVKEMFVSEVAESFQHSDVTALVYDPRTLGDSGGLPRNNIDPLAQVSDYSDALTFLKTLPIVDQTNISFWGMSFSALVALNAAALDKRARCCIAVCPLTGMQPEPDMLPKVLARCMQDRESQVVGNPPVTISVLTEQGRNPAGMGIGADKMEYDYMVNAKFRGAPNYENRTTLQSYYKMMAWQPFEIMKYLSKTRVLMIIPENDTISPADKQQVLFDGLPEPKTAHIAKGKGHLDVLSGADYEILAEMQAYFIKGPRGKGNAPSA | Function: Thiohydrolase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties . The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tailored throughout the backbone . The highly reducing polyketide synthase Bref-PKS is proposed to synthesize the precisely reduced octaketide precursor, which could then be directly offloaded by the thiohydrolase enzyme Bref-TH followed by a cytochrome P450 monooxygenase-mediated formation of the cyclopentane ring and macrocyclization to afford 7-deoxy BFA. Alternatively, the first ring annulation can also occur on the ACP-tethered intermediate before the thiohydrolase release and lactonization . The C7-hydroxylation by another cytochrome P450 monooxygenase is believed to be the final step in the process to obtain the final structure of BFA . In addition to the HRPKS Bref-PKS and the thiohydrolase Bref-TH, the brefeldin A biosynthesis cluster contains 4 cytochrome p450 monooxygenases (called orf3 to orf6), as well a the probable cluster-specific transcription regulator orf8 .
Sequence Mass (Da): 33884
Sequence Length: 308
Pathway: Mycotoxin biosynthesis.
EC: 3.1.-.-
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A0A068A9T2 | MFDIYDYSPRLVALGLIAATIIIYSFTLTVYRLFFHPLARIPGPKLCAITGWYEIFWDVLVGGQFTFKIEEWHKTYGPVMRIGPNEVHFNDPDFYNELYPTIGATYEKPAQWRWRFGCGTAIFDTIGHEHHAQRKAPVAAFFSRQKILQFSGFIQDQTDILVKRIRDDHRGQVICANEAFDALTMDIIGYYAFGLSYNSLQYPGFKAPYRNVTADIARMVHVGAHFPWVFTILNALPEKYITRLLPPMSKIFMFRKEISSQIRRIKDNKEYLDKNVNEHRTVFHEILNSNQPACELNEGRIYHEALSLVGAALETSKRTTALAVYYILATPGVEDNLRAELTAAMPDKTKNLSVPELEALPYLNAVIKEALRLAIGVSQRMRRYSPTETITYKDYTIPPNTVFGMCHWEQLRDARIWDRPTEFLPERWLAEQPLALNGQPLNKYFVPFHRGPRMCLGKEFGMAQLNIGLATLFRQDDIKLELYETDRKDVDVVADFFVPLTVKESQGVRVLVK | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties . The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tailored throughout the backbone . The highly reducing polyketide synthase Bref-PKS is proposed to synthesize the precisely reduced octaketide precursor, which could then be directly offloaded by the thiohydrolase enzyme Bref-TH followed by a cytochrome P450 monooxygenase-mediated formation of the cyclopentane ring and macrocyclization to afford 7-deoxy BFA. Alternatively, the first ring annulation can also occur on the ACP-tethered intermediate before the thiohydrolase release and lactonization . The C7-hydroxylation by another cytochrome P450 monooxygenase is believed to be the final step in the process to obtain the final structure of BFA . In addition to the HRPKS Bref-PKS and the thiohydrolase Bref-TH, the brefeldin A biosynthesis cluster contains 4 cytochrome p450 monooxygenases (called orf3 to orf6), as well a the probable cluster-specific transcription regulator orf8 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59157
Sequence Length: 513
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A068AA98 | MYHLIPFAAILGMTYALSLAIYRLFLSPLAKFPGPKLAAVTGWVETYYQLFYGEGGQFIFLYKEWHQKYGPIIRINPWEVHISDSCFFEILYSTNRPLKKLPHLAKVFDNELSGFSTVSPELHRIRRKAVSHLFSKGEVLKRGAQIQSAMDRLSERLKLDFLGHGNRVICMNDMWSVYTADLIAEYAFGRHYGFIDQPNFEADFTKALVHLLEPTHLAQQFPWLTDILKALPTSVLEFLHPHMAAFNKFKAANQVRIAKANFAKDLSKGGTMFSAIFNSDLPDEEKSIERAHQEALAFAAAGAETVAATLSVASFHLLHDPKIRRRLDEELATVVPDSRSSDASMPSLEILWQLPYLTGIINEALRLSYGSYARIPRTSDTPIQYDEWTIPPGVVFSMDIAPAHHDERIFPDSYSFKPERWLDNPQAFDGKPLTRYLFSFSRGTRSCLGMQLALAEMYIGIVSFFSRFDAHLFETDLTDITFVRDRFAPRPRIGSRGVRVNRLTTRKF | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties . The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tailored throughout the backbone . The highly reducing polyketide synthase Bref-PKS is proposed to synthesize the precisely reduced octaketide precursor, which could then be directly offloaded by the thiohydrolase enzyme Bref-TH followed by a cytochrome P450 monooxygenase-mediated formation of the cyclopentane ring and macrocyclization to afford 7-deoxy BFA. Alternatively, the first ring annulation can also occur on the ACP-tethered intermediate before the thiohydrolase release and lactonization . The C7-hydroxylation by another cytochrome P450 monooxygenase is believed to be the final step in the process to obtain the final structure of BFA . In addition to the HRPKS Bref-PKS and the thiohydrolase Bref-TH, the brefeldin A biosynthesis cluster contains 4 cytochrome p450 monooxygenases (called orf3 to orf6), as well a the probable cluster-specific transcription regulator orf8 .
Sequence Mass (Da): 57951
Sequence Length: 508
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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A0A068AA78 | MANDVSGLGPTAFVRLLAFHLIGLFVSITVYRLFFHNLSGFRGPFIARLSSFYLAWLSAKRLHLHDEIDDLHSLYGDYVRTGPRELSIIDPQCVQVIYGSQTKCIKGPIYTLLDPRTNLSSTRDKTEHAKRRRAWDRGFSTTALHTYEPMVQELTEELMTIIDELSENPINITEWVDKYAFEVMGQLTFGKPFNMLKERKEAYFLELIRQDMNAIGYLLNLPWLSYLFLRTPGLNQNHLNFWRWIENEFAQRIARGQRRPDVFNWLHQAYLQGPQTKSDTLKLHGDGYLVIVAGSDTTASTITHLLFYLACNKALTQKLQAQLDALEGLTDESLRDVELLDACINETLRLRPAVPAGVQRETPKEGIYIGNRYIPGDTIVKVPMYTLFRDPRSFEQPNEFIPERFTTRPELVKDKSVFIPFLTGSYACVGRRLALMEVRRAVAAILCRYDIALAPGQNEEGFLDGKIDAFTLVAAPLSLKFTRRHQQKQ | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties . The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tailored throughout the backbone . The highly reducing polyketide synthase Bref-PKS is proposed to synthesize the precisely reduced octaketide precursor, which could then be directly offloaded by the thiohydrolase enzyme Bref-TH followed by a cytochrome P450 monooxygenase-mediated formation of the cyclopentane ring and macrocyclization to afford 7-deoxy BFA. Alternatively, the first ring annulation can also occur on the ACP-tethered intermediate before the thiohydrolase release and lactonization . The C7-hydroxylation by another cytochrome P450 monooxygenase is believed to be the final step in the process to obtain the final structure of BFA . In addition to the HRPKS Bref-PKS and the thiohydrolase Bref-TH, the brefeldin A biosynthesis cluster contains 4 cytochrome p450 monooxygenases (called orf3 to orf6), as well a the probable cluster-specific transcription regulator orf8 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56075
Sequence Length: 489
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q45340 | MYLDRFRQCPSSLQIPRSAWRLHALAAALALAGMARLAPAAAQAPQPPVAGAPHAQDAGQEGEFDHRDNTLIAVFDDGVGINLDDDPDELGETAPPTLKDIHISVEHKNPMSKPAIGVRVSGAGRALTLAGSTIDATEGGIPAVVRRGGTLELDGVTVAGGEGMEPMTVSDAGSRLSVRGGVLGGEAPGVGLVRAAQGGQASIIDATLQSILGPALIADGGSISVAGGSIDMDMGPGFPPPPPPLPGAPLAAHPPLDRVAAVHAGQDGKVTLREVALRAHGPQATGVYAYMPGSEITLQGGTVSVQGDDGAGVVAGAGLLDALPPGGTVRLDGTTVSTDGANTDAVLVRGDAARAEVVNTVLRTAKSLAAGVSAQHGGRVTLRQTRIETAGAGAEGISVLGFEPQSGSGPASVDMQGGSITTTGNRAAGIALTHGSARLEGVAVRAEGSGSSAAQLANGTLVVSAGSLASAQSGAISVTDTPLKLMPGALASSTVSVRLTDGATAQGGNGVFLQQHSTIPVAVALESGALARGDIVADGNKPLDAGISLSVASGAAWHGATQVLQSATLGKGGTWVVNADSRVQDMSMRGGRVEFQAPAPEASYKTLTLQTLDGNGVFVLNTNVAAGQNDQLRVTGRADGQHRVLVRNAGGEADSRGARLGLVHTQGQGNATFRLANVGKAVDLGTWRYSLAEDPKTHVWSLQRAGQALSGAANAAVNAADLSSIALAESNALDKRLGELRLRADAGGPWARTFSERQQISNRHARAYDQTVSGLEIGLDRGWSASGGRWYAGGLLGYTYADRTYPGDGGGKVKGLHVGGYAAYVGDGGYYLDTVLRLGRYDQQYNIAGTDGGRVTADYRTSGAAWSLEGGRRFELPNDWFAEPQAEVMLWRTSGKRYRASNGLRVKVDANTATLGRLGLRFGRRIALAGGNIVQPYARLGWTQEFKSTGDVRTNGIGHAGAGRHGRVELGAGVDAALGKGHNLYASYEYAAGDRINIPWSFHAGYRYSF | Function: Inhibits the classical pathway of complement activation and prevents accumulation of deposited C4.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 103377
Sequence Length: 1010
Domain: The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent cleavage. Finally, the mature protein remains tightly associated with the bacterium.
Subcellular Location: Periplasm
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P71345 | MFSRKDIIVLGMMIFALFLGAGNIIFPPMEGFSSGQHWTSASLGFVLTGVLMPFITLVVVAILGRGEELTKDLPKWAGTGFLVILYLTIGSTFAMPRITNVAYEMAWLPLGLTENNANVRFVFSLIFNLIAMGFMISPNTIISSVGKFMTPALLVLLIAVAITVFISPLSEIQAPSNAYENSHSLLIGLTSGYQTMDVLAAIAFGGIVARALSAKNVTKTKDIVKYTISAGFVSVILLAGLYFSLFYLGATSAAVAEGATNGGQIFSRYVNVLFGSAGTWIMAGIIVLASLTTLVGVTSASADYFSKFSVRFSYPFWAALFTAMTITVSQYGLTDLLRITIPALLLIYPVAIVLVLLQFLRKKLPSIKFTYNSTLLVTVCFSLCDSLNNVKMLPESINSLLKHFPLSSEGMAWLVPTLVMLVASIFIGKALHKTHS | Function: Branched chain amino acid transport system, which transports leucine, valine and isoleucine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47039
Sequence Length: 436
Subcellular Location: Cell inner membrane
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P54104 | MKEKLTHAESLTISSMLFGLFFGAGNLIFPAYLGEASGANLWISLLGFLITGVGLPLLAIASLGMTRSEGLLDLSGRVSHKYSYFFTCLLYLTIGPFFAIPRSFTVPFETGISALLPSGMAKSTGLFIFSLIFFAIMLFFSLRPGQIMDWIGKFLTPAFLLFFFFIMIMALLHPLGNYHAVKPVGEYASAPLISGVLAGYNTMDALAGLAFGIIVISSIRTFGVTKPEKVASATLKTGVLTCLLMAVIYAITALVGAQSRTALGLAANGGEALSQIARHYFPGLGAVIFALMIFVACLKTAIGLITACSETFAEMFPKTLSYNMWAIIFSLLAFGIANVGLTTIISFSLPVLMLLYPLAISLILLALTSKLFDFKQVDYQIMTAVTFLCALGDFFKALPAGMQVKAVTGLYGHVLPLYQDGLGWLVPVTVIFAILAIKGVISKKRA | Function: Branched chain amino acid transport system which is involved in the uptake of leucine, valine and isoleucine . The proton motive force is probably the driving force for transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47869
Sequence Length: 446
Subcellular Location: Cell membrane
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A2RJ04 | MKEKLAGKDYLFIGSMLFGLFFGAGNLIFPIHMGQEAGDAISQANFGFLVTAVGFPFLGIIALGISQSNGVFELATRVNRIYAYIFTILLYLVIGPFFALPRLATTSFEIGISPFLSNKLQTPLLALFSILFFGTAWFLSRKPTKLLDYIGKFLNPLFLVLLGLILIIAFSHPLGSVHQAEVGKLYQSSAFMNGFTQGYNTLDALAALAFGIIIITTIRQRGVKNSKIIAKETIKAGLISVGLMAIIYTCLSYLGAMSVGKFAISENGGIALAQISNYYLGTFGMIILALIVIIACLKTAVGLMSAFSETFVELFPKREYRFYLMIVSILPCIFANIGLTKIIELSVPVLMFLYPLAITLILLALLGPVFQHSKLVYQITTAFTLLAAIADGLNALPNPLKSLKPIAAILNFSKDSLPFFSLGMGWILLAVLGFIIGCLVHFLKRITNK | Function: Branched chain amino acid transport system which is involved in the uptake of leucine, valine and isoleucine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48900
Sequence Length: 449
Subcellular Location: Cell membrane
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P0A1W9 | MTHQLKSRDIIALGFMTFALFVGAGNIIFPPMVGLQAGEHVWTAAIGFLITAVGLPVLTVVALAKVGGGVDSLSTPIGKVAGLLLATVCYLAVGPLFATPRTATVSFEVGIAPLTGDSAMPLLIYSVVYFAIVILVSLYPGKLLDTVGNFLAPLKIIALVILSVAAIVWPAGPISNALDAYQNAAFSNGFVNGYLTMDTLGAMVFGIVIVNAARSRGVTEARLLTRYTVWAGLMAGVGLTLLYLALFRLGSDSATLVDQSANGAAILHAYVQHTFGGAGSFLLAALIFIACLVTAVGLTCACAEFFAQYIPLSYRTLVFILGGFSMVVSNLGLSHLIQISIPVLTAIYPPCIALVVLSFTRSWWHNSTRIIAPAMFISLLFGILDGIKASAFGDMLPAWSQRLPLAEQGLAWLMPTVVMVILAIIWDRAAGRQVTSSAH | Function: Liv-II branched chain amino acid transport system, which transports leucine, valine and isoleucine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46221
Sequence Length: 439
Subcellular Location: Cell inner membrane
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Q24157 | MQSKHRKLLLRCLLVLPLILLVDYCGLLTHLHELNFERHFHYPLNDDTGSGSASSGLDKFAYLRVPSFTAEVPVDQPARLTMLIKSAVGNSRRREAIRRTWGYEGRFSDVHLRRVFLLGTAEDSEKDVAWESREHGDILQAEFTDAYFNNTLKTMLGMRWASDQFNRSEFYLFVDDDYYVSAKNVLKFLGRGRQSHQPELLFAGHVFQTSPLRHKFSKWYVSLEEYPFDRWPPYVTAGAFILSQKALRQLYAASVHLPLFRFDDVYLGIVALKAGISLQHCDDFRFHRPAYKGPDSYSSVIASHEFGDPEEMTRVWNECRSANYA | Function: Neurogenic protein essential for the development and maintenance of epithelial structure. Required in the germline for establishing the follicular epithelium and for determining the dorsal-ventral polarity. Collaborates with Notch on the apical surface of follicle cells to mediate germline-follicle cell adhesion. Brn has a role in chorion formation.
Catalytic Activity: ganglioside GM2 (d18:1(4E)) + UDP-alpha-D-galactose = ganglioside GM1 (d18:1(4E)) + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 37620
Sequence Length: 325
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.62
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Q63K32 | MAEKTEKPTAKKLRDAAKKGQTFKARDIVALIVIATGALAAPALVDLTRIAAEFVRIASTGAQPNPGAYAFAWAKLFLRIAAPFVLLCAAAGALPSLVQSRFTLAVESIRFDLTALDPVKGMKRLFSWRSAKDAVKALLYVGVFALTVRVFADLYHADVFGLFRARPALLGHMWIVLTVRLVLLFLLCALPVLILDAAVEYFLYHRELKMDKHEVKQEYKESEGNHEIKSKRREIHQELLSEEIKANVEQSDFIVANPTHIAIGVYVNPDIVPIPFVSVRETNARALAVIRHAEACGVPVVRNVALARSIYRNSPRRYSFVSHDDIDGVMRVLIWLGEVEAANRGGPPPETRAPTSAEPQARDGVAPPGDACADNAFPDDAPPGAAAPNAGSPDGPAPDGGAPARTGDQNA | Function: Part of the bsa type III secretion system, is involved in the intracellular replication of invading bacteria inside the host cell. Probably necessary for the lysis of the vacuole membrane and escape into the host cell cytoplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44458
Sequence Length: 411
Subcellular Location: Cell membrane
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D1MX89 | MIFLAPFEFLDPLRHALPLTCTGLIIIFAFYLSRHHSPKPAPNIPIHSYDREEYFRRGYELVQEGQKKHPSCFQLRTATGWKILVPIRFVEELRKNPSLSFARGNDKDAFIEYPGFEAMEAACHDDYFMQEVVRVKLTQTLNLLYSSVIDESAVAMSEVLGEDKIWRTLRIKDDINHIVARVTSRVFLGFPLCRNQKWLDIVVNHTKAVFMAQKRMRQTPPALRPLIHYFLPETKLLRQHLHAARTLISPELAKRRAAVEEALRHGKIPKESANAISWMVEVSQAQGRKIDVAVHVVSLSMTAIQTTSEVMTNCILQLCETPSIVDDLRAEIIFLLKEGGWTKYTLYKMRLLDSFIREVMRHHDFLRVTSWRGCTEDVVLSDGTVLPKGSCIYFDDSKVVDPEHYPDPEKFDPMRSFKKREQPGQEDRHQFVSLQTDHMAFGYGIHACPGRFFANMELKVMLCNFLLKYDVRLVPGEKRPVDILFEVQRMVPPDVRVQIKVRDQEPEVDLYSPISST | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59771
Sequence Length: 517
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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D1MX85 | MEMATTFTHDVTTSGKPLLLFLILITLTYSLGIVFYRLFRHPLAKFPGPRIAAATYLYEIAFDYFGNGAYLFEIERMHHKYGPIVRLNPAELSIKDGEFYDKVYVNGNVRRTEALPSFGDGMDFNNSHGMTVDHHQHRQRRKPLEPFFSKAGVARFESNLASVVSTLVDRLRDYEGTGSVLRLDHAFAALAGDIITTMCIDSTSMTFLDDKDFSRGWYELFHTLIISMPVFMNFPWIIRLVRLIPTSILKRVDPRSQMFRDWSDMSVAEIKKSLQRKATGEMLTYQKGIIKAPTLFDHLVNSDLPTSDMSVERLASEAQVLMGAGTVTTAQSMSHLVVNVLLRPDVEKRLREEFAVLMKQLGEASLPKARELEKLPYLQACVKEGLRLSHGLMHRLPRISPDVALEFNGLIIPPGTPVGMSAYFMHMDETVYENPREFIPERWLGDVDPKMDRNYVPFSRGSRRCLAPNLAYTEISMVMAALFSPWSPAIRLQDTNASDVDPVCAFLLPLPRLDSKGVRVIVRKNKE | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59821
Sequence Length: 527
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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D1MX86 | MESAQIHSTRDSLFILWLTTLLVSVLATAAYIKFQSRPRPYSGFPLVTLGGPSETDSSHAANWFRRGRALVNKGLSELSGAFQISNGSGYWIILPSKYMDELRNHPDMSLRDALREENFPNYRGFDGFRQAFKDSTFTQEVIRVKVTQSLGLITANLANECQHALQENLGESREWQQRFIIEDILNIVAQLTSRVFLGERLCRDKEWLQITKEYARNSFMGSEELRQCLPLTRPLMQFFMPACTQLRKFSAAARRLIDPEVQARKRRAEEAIKLGKKPPKVEDTIGWMVEVARGRQVDYVGGQLALSIAAIHSSTDNLSKAVVKLCEMPEIVAPLREEITTVLESTDGWSKPALYRMKLLDSFLKEVQRLAPFTIVGMHRRVMKGYVLSDGTHLPKNSRIMVMNDKLRDSSVYEDPDTFKYDRFARLREQPGQEDQHQLASTSSEFATFGHGEHACPGRFFAANQLKIIMACLLLKYDFCFQPGQAEKARVIPFEMVETIDPTLKIEVRRRSEELDVTKVAKETA | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59843
Sequence Length: 525
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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E0D7H5 | MSQSTLVIIGAGGIGEAIARRVGPGKEVLLGDWSNALLQEATQRMKRDGFRVTSQHVNISSHDSVIQFAEKAQSLGQVMHVVISAGLSPVSSTRETILAVNLAGTGFCIAEFGKLIGHGGTCVVISSLAGYTLAQDVPHGVIQHLARTSPSDVLGLPLLRETVLDQWSAYGVSKRVNYVQVQDASLSWARRGARINSISPGAIQTPMLSLESQASKEEVVHDLAQNVPCKRVGDSGEVAHVAAFLLGSESSFVTGTDILVDGGALAYLSRDTSS | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Sequence Mass (Da): 28830
Sequence Length: 274
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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D1MX87 | MLEGTLQDCWTSISKMQLHWTVLGLLPVLFIAILGPRVRQIWVNYVHLTKIPSPHKKDYFCFVTETTRAEFLNECARLLRKGFASGDVIRLHASWDHIVVLSPSYAECLRADEKFSPDTFSDKEMFGAVPGFEPYRFLCTHRDLVRNVISMRLNRCFVPATRYLSEAIDDALRKQMGNDSEWREVPLGNAVLKILTQSSFRALQGPELCYDDEWLDIATQYIVTSVTGVTALRKLPKFLVPLIHWFHPDAIKSRRLLSRARAKLIPFYEKRKKELYQARRNGTYRPEDADAFGWYEELADGRDYDPVVAQLTVAVAATHSTTDFMCQFLSDMVRYPEYIQPLRDELILALKEKGWKASTILQLPLLDSVMKESQRLKPVAMGFMRSIAQHDVYLQDAVKIPKNASVIVSAHSMRDATVYENPDSFDGYRFINPTKHPESRHFTSVSVNHMGFGFGKHACPGRFFVNLETKILIAHLLLKYDWKFANDGCPAIRTSGFDQVVDPSAKMLVRRRKEEIRIEALYE | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60169
Sequence Length: 523
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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C9K2Q2 | MAVQETDLDKQLLQLSIQVADLAARTDSRGSQKIQDFLIKTQQSLESPWETLMRYYDLDFQHVAIRIGCDMQVFTTLTTADKPMKLQDIANVNGASERLLGRVLRYLASINTIEEVGKDTFEANHITRTLSKPGIEGGIRLSSACQRPTNSALPDLLVERGFQDITSATETAFNKAWASREPFFTWVRSQPKIFEYLRLALDVQFREDWLNAFPLESHLGDFASRADPEKVLFVDVGGNLGIQCRGLKAKFPHLSGRIILEDLQETIDVALALEGVETLAQDYLTEQKVKGAKFYYYRNIFHDNPDDRCRLILDALKPAMEESSLLLIDDKVLLNQGSHRHVTMLDLAMMAQVASHERTRAQWQALLEGAGWKIEDIFQYSHEYDSIIVVKPAAQNA | Function: 16-O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Sequence Mass (Da): 44950
Sequence Length: 397
Pathway: Mycotoxin biosynthesis.
EC: 2.1.1.-
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Q08280 | MDASSVPPKVDDYGMYTTEISHHNPIELKNLLSSSDSRRNSQDEDSLPNNTNLIKEIDWQGEKVKTYPLNYQTVPLVKLQVIACLIMFVVFGMNDQTVGALLPTLIEYYHISRVDVSNVFIVQLCGYVMASLSKERLNKHFGMRGGMLLAAGLCIVFLIILATAPSSFYVCMFCGLPLGLGIGILDSTGNVLMGSLLVHKNELMGIMHGLYGAAAMVTPPLVSYFVEWGHWSLFFLIPLFFSIIGMIVIFPAFKFETASKYDYLCSVENKESNNDVEEAGDNSLMESTKASPGFFELLRNPAIFLYSLYLFLYLGAEITTGSWFFSYLLETKSSNKVAMSYIAASFWTGLTVGRLCLGFVTERFFENEYKASKAYAFLTLSSYTLFVLVGLINSSSVFYFVVLFFVVFCCGTFIGPLFPNASIVALQVLPKRLHVSGVGVAVAVGGCGGAAIPYLAGVIAHTVGIQYIPLLCWIMVALFTLEWTLYPKFIKGHEEYF | Function: Probable transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55084
Sequence Length: 497
Subcellular Location: Golgi apparatus
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D1MX88 | MASILWTTSLKVLLALIVWIGTTIIYNIYFHPLHSFPGPVLARATRLYSAYIRAVGLSERKSLQWHNQYGGIVRIAPDELSFNTGSAWNDIYGTKSRKSQRLQKDPHFYMGATAPNGEKNMGAVGDEDHSRIRSVLAHAFTDTALHAQESLIRAHVDRLVQRLQDLHGKPTDIVRWMHHHSYDVIAHLCFGQDLDALGSKDWFPPARVVFEGIREGVTLIEVLRFVPFKATVLDILVQAFGKARRENFNASVARAMLRLRLAETTSIDFISYILRVKESAKELTRSELTANVALLIDAGSETTATMLSGCLFYLSLNRTTLEELTHKLREDFRTHDQLSLQNLAKMKLLTYVIQESLRIYPPLPATLPRLTPATGAMINGVLIPPKTRVGMNAFAAYHSTQNFADADMFIPQRWDNTNDRFARDQRHVHRPFSLGSRGCLGKNLAWAEIRLTLACLLWNFDVILEPGQEEWHGKQLTWFIWNKDPLYMRFAPRTK | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56346
Sequence Length: 495
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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C9K2Q3 | MKYQFSIIVDPATYDNEGLSNGIDLRKNNFTHLEDRGAIRAQQDWATHIAPIKQFKGTLGHDYSFMTVCVPECIPIRLEIISYANEFAFMYDDDTELDTENNTSAENDKLMGTFLAGTQGWSPPQDQSSSGKTRILKQLFSEMMEIDKECAIATMKAWAEFLRVGSSRQHGTVFTRLKDYLPYRIKDVGEMFWFGVVTFGMALHIPDHEMDACHKLMEPAWIAVGLANDVFSWPKERDASQRLGRTHVVNAVWVVMQEHGFSQEQARQYCRELAAQFVAQYLDNIRNIKNEESISPDLRTYVEAMQYSISGNVIWSKFCPRYNPEKRFNQTQLDWMQNGLPSTVELDGASNTSSSFLSTSTHGSPASGSQTTIESKDGWTADSSGIVSLLLNCSLPPLSHKVISAPLTYVDSLPSKGTRDMFLDALNHWLHVDEQRASQVKMAIRMLHNASLMLDDVQDGSRLRRSKPSAHRVFGVAQTTNSAAFLVNESIKLIRELAGDQGVAAVLEKLTSLFVGQAQDLHSSRNLSPPSLTEYIQTIDQKTSALFELASRLMCLCSTATVVPNSSLSRFCILLGRFFQIRDDYQNLTSPEYTKQKGFCDDLDSGTYTLPLVYAISQQSENFLLQNLLSTRLAEGTLDDDQKRLALDQMQLVKTNEFLRKILDSLYDELRAELQCISSSFASENPQMELMLMMLKL | Function: Multifunctional diterpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Catalytic Activity: geranylgeranyl diphosphate = diphosphate + fusicocca-2,10(14)-diene
Sequence Mass (Da): 78573
Sequence Length: 697
Pathway: Mycotoxin biosynthesis.
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D7UTD1 | MASTSSTSTDGHLNIRPMVHGSDKKLNFGAYITGLDLNNASDAEVDQLREAILRHKIVVIKGQQAEKPDKNWEMIKKLDPMHHMITQEEFGQLFHPTGEGLIAMLKLATVPTTEHGHIHLMGKGYQGDDHYGLKKLNLGEAFAGNYYSKPLAEEDFRAGVTRFQSWHMDGPLYKVHPPYISSLRFIQLPDGEQTVEWADGSGLSLKTKPGRTAFFSTSQLYDMLTDEERAMVDNSAVEYMYYPYEWIRGCRGNPNGLNVADEGREKPLDAMEEIARDERWTKTYPMVWFNELTKEKSLQVQPNCVRRLLIRRSADQKEPEIIEGPERVREFMNKLQQRIVRPEYVYVGPEEEGDHVFWYNWGMMHSKIDYPIAYGPRIVHQGWIPSHRVPRGPTAVAH | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Alpha-ketoglutarate dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C . Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position . Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol . Follows the isomerization of the double bond and reduction of aldehyde to alcohol catalyzed by the short-chain dehydrogenase/reductase bsc3 to yield the diol compound fusicocca-1,10(14)-diene-8 beta,16-diol (Probable). The next step is the oxidation at the C-3 position of fusicocca-2,10(14)-diene-8-beta,16-diol catalyzed by the alpha-ketoglutarate dependent dioxygenase bsc9, to produce a triol compound . Methylation of the hydroxy group at position 16 is performed by the methyltransferase bsc6 . 16-O-methylation is followed by oxidation at the C-13 position to ketone and an alkyl shift of the methyl group leads to brassicicene C (Probable). Although the probable acetyltransferase bsc4 is included in the gene cluster, no acetylation reactions are necessary for brassicicene C biosynthesis. However, the fact that brassicicene E, which is a structurally related compound having an acetoxy group at position 12, was previously isolated from another strain of A.brassicicola suggests that the ATCC 96836 strain might also produce a small amount of brassicicene E (Probable).
Sequence Mass (Da): 45701
Sequence Length: 398
Pathway: Mycotoxin biosynthesis.
EC: 1.14.11.-
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Q6WRU0 | MAPTFYHYHPLPMDQKEPGCGIRWRCLAAASVLILVALVIPLIIFAVKANSEACRDGLRAQEECSNTTRLLQRQLTRSQDNLAQAEAQASTCNRTVVTLQDSLEKKVSQIQEKQALIQEQEAQIKEQEAQIKEQEAQIKEQKAHIQEQQVRIQKLEGEVEEFEQKLKKLRTAEEASITSKQNSAGSMAVSSLLVLAVPLFLLF | Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells (By similarity).
PTM: The GPI anchor is essential for its antiviral activity.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 22826
Sequence Length: 203
Domain: The extracellular coiled coil domain forms an extended 170 A long semi-flexible rod-like structure important for virion retention at the cell surface and prevention of virus spreading.
Subcellular Location: Golgi apparatus
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Q10589 | MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ | Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted . Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason-Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma-associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae: influenza A virus, paramyxoviridae: nipah virus, and coronaviridae: SARS-CoV . Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration . Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection . Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. Isoform 1 and isoform 2 are both effective viral restriction factors but have differing antiviral and signaling activities . Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in the presence of Vpu . Isoform 1 acts as an activator of NF-kappa-B and this activity is inhibited by isoform 2 .
PTM: Monoubiquitinated by KSHV E3 ubiquitin-protein ligase K5, leading to its targeting to late endosomes and degradation.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 19769
Sequence Length: 180
Domain: The extracellular coiled coil domain forms an extended 170 A long semi-flexible rod-like structure important for virion retention at the cell surface and prevention of virus spreading.
Subcellular Location: Golgi apparatus
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Q8R2Q8 | MAPSFYHYLPVPMDEMGGKQGWGSHRQWLGAAILVVLFGVTLVILTIYFAVTANSVACRDGLRAQAECRNTTHLLQRQLTRTQDSLLQAETQANSCNLTVVTLQESLEKKVSQALEQQARIKELENEVTKLNQELENLRIQKETSSTVQVNSGSSMVVSSLLVLKVSLFLLF | Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 19152
Sequence Length: 172
Domain: The extracellular coiled coil domain forms an extended 170 A long semi-flexible rod-like structure important for virion retention at the cell surface and prevention of virus spreading.
Subcellular Location: Golgi apparatus
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Q811A2 | MAPSFYHYLPVAMDERWEPKGWSIRRWWLVAAILVVLIGVVLVCLIVYFANAAHSEACKNGLRLQDECRNTTHLLKHQLTRAQDSLLQTEMQANSCNQTVMDLRDSLKKKVSQTQEQQARIKELENKIERLNQELENLRTQKEISTTVQVNSGGSVVVSSLLVLVAVLFLHF | Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection (By similarity). Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 19674
Sequence Length: 172
Domain: The extracellular coiled coil domain forms an extended 170 A long semi-flexible rod-like structure important for virion retention at the cell surface and prevention of virus spreading.
Subcellular Location: Golgi apparatus
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K4JY29 | MGPAVVFDCMTADFLNDDPNNAELSSLEMEELESWGAWSDDTDQSV | Function: Bottromycin D is a ribosomally synthesized and post-translationally modified peptide (RiPP) that displays antibiotic activity against methicillin-resistant S.aureus (MRSA).
PTM: The precursor peptide is first ribosomally synthesized and then highly tailored by specific enzymes to yield the final natural product. These modifications include several methylations, cyclization and the formation of t-Leu and Thia-beta-Ala residues.
Sequence Mass (Da): 5083
Sequence Length: 46
Subcellular Location: Secreted
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Q9LR78 | MAPDQSYQYPSPSYESIQTFYDTDEDWPGPRCGHTLTAVFVNNSHQLILFGGSTTAVANHNSSLPEISLDGVTNSVHSFDVLTRKWTRLNPIGDVPSPRACHAAALYGTLILIQGGIGPSGPSDGDVYMLDMTNNKWIKFLVGGETPSPRYGHVMDIAAQRWLVIFSGNNGNEILDDTWALDTRGPFSWDRLNPSGNQPSGRMYASGSSREDGIFLLCGGIDHSGVTLGDTYGLKMDSDNVWTPVPAVAPSPRYQHTAVFGGSKLHVIGGILNRARLIDGEAVVAVLDTETGEWVDTNQPETSASGANRQNQYQLMRRCHHAAASFGSHLYVHGGIREDVLLDDLLVAETSQSSSPEPEEDNPDNYMLLDDYLMDEPKPLSSEPEASSFIMRSTSEIAMDRLAEAHNLPTIENAFYDSAIEGYVPLQHGAETVGNRGGLVRTASLDQSTQDLHKKVISTLLRPKTWTPPANRDFFLSYLEVKHLCDEVEKIFMNEPTLLQLKVPIKVFGDIHGQYGDLMRLFHEYGHPSVEGDITHIDYLFLGDYVDRGQHSLEIIMLLFALKIEYPKNIHLIRGNHESLAMNRIYGFLTECEERMGESYGFEAWLKINQVFDYLPLAALLEKKVLCVHGGIGRAVTIEEIENIERPAFPDTGSMVLKDILWSDPTMNDTVLGIVDNARGEGVVSFGPDIVKAFLERNGLEMILRAHECVIDGFERFADGRLITVFSATNYCGTAQNAGAILVIGRDMVIYPKLIHPHPPPISSSEEDYTDKAWMQELNIEMPPTPARGESSE | Cofactor: Binds 2 manganese ions per subunit.
Function: Phosphatase that acts as a positive regulator of brassinosteroid (BR) signaling . Dephosphorylates BES1, a transcription factor that regulates the expression of BR-response genes, thereby playing an important role in the regulation of response to BRs . Inactivates the negative regulator of BR signaling ASK7/BIN2 by dephosphorylation at 'Tyr-200' .
PTM: Phosphorylated at Ser-395 and Ser-444. Phosphorylated at Ser-764 by CDG1 and CDL1.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 87789
Sequence Length: 793
Subcellular Location: Nucleus
EC: 3.1.3.16
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P33532 | MASKIASLFSPSETASKDQHENVAEDLELGTASSQSDGIHETNSEYDEKKREESPEVIDISNLISSDHPAHPQNWHWAKRWSIVFMFCLMQIYVIWTSNGFGSIEYSVMAQFNVSAQVATLCLSMNILGSGLGPMFLGPLSDIGGRKPVYFCSIFVYTVFNISCALPRNIVQMIISHFIIGVAGSTALTNVAGGIPDLFPEDTAGVPMSLFVWACAGGAIGAPMATGVDINAKYGWRWLYYINIIVGGFFLIVILIIPETLPIKVITRYENAKGRIVEGIPKNNLKEVLKKCKFVTTMGFRMMLTEPIILSMGLYNFYAYGISYFFLTAIWPVFYDTYKMSEMGASCTYLSGFVASTLLFLYQPIQDWIFRRDKAKNNGVARPEARFTSALFITLLFPAGMFLFAFTCHPPFPWMSPIVGNSMVTVANGHNWMCILNYLTDSYPLLSGSAVAAFTLPSFIGATVFAHVSQIMFNNMSVKWAVATMAFISISIPFIIYTFYFFGQRIRALSSLTGNKALKYLPLENN | Function: Thiamine-regulated, high affinity import carrier of pyridoxine, pyridoxal and pyridoxamine. Also imports, but does not export, amiloride and so confers sensitivity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58484
Sequence Length: 526
Subcellular Location: Membrane
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O67791 | MENLKKYLEVAKIAALAGGQVLKENFGKVKKENIEEKGEKDFVSYVDKTSEERIKEVILKFFPDHEVVGEEMGAEGSGSEYRWFIDPLDGTKNYINGFPIFAVSVGLVKGEEPIVGAVYLPYFDKLYWGAKGLGAYVNGKRIKVKDNESLKHAGVVYGFPSRSRRDISIYLNIFKDVFYEVGSMRRPGAAAVDLCMVAEGIFDGMMEFEMKPWDITAGLVILKEAGGVYTLVGEPFGVSDIIAGNKALHDFILQVAKKYMEVAV | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, and both D and L isomers of inositol-1-phosphate (I-1-P).
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 29336
Sequence Length: 264
EC: 3.1.3.11
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O30298 | MDERDALRISREIAGEVRKAIASMPLRERVKDVGMGKDGTPTKAADRVAEDAALEILRKERVTVVTEESGVLGEGDVFVALDPLDGTFNATRGIPVYSVSLCFSYSDKLKDAFFGYVYNLATGDEYYADSSGAYRNGERIEVSDAEELYCNAIIYYPDRKFPFKRMRIFGSAATELCFFADGSFDCFLDIRPGKMLRIYDAAAGVFIAEKAGGKVTELDGESLGNKKFDMQERLNIVAANEKLHPKLLELIK | Cofactor: Magnesium. Can also use manganese.
Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate and fructose-6-phosphate. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 27967
Sequence Length: 252
EC: 3.1.3.11
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Q57573 | MKWDEIGKNIAKEIEKEILPYFGRKDKSYVVGTSPSGDETEIFDKISEDIALKYLKSLNVNIVSEELGVIDNSSEWTVVIDPIDGSFNFINGIPFFAFCFGVFKNNEPYYGLTYEFLTKSFYEAYKGKGAYLNGRKIKVKDFNPNNIVISYYPSKKIDLEKLRNKVKRVRIFGAFGLEMCYVAKGTLDAVFDVRPKVRAVDIASSYIICKEAGALITDENGDELKFDLNATDRLNIIVANSKEMLDIILDLL | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 28578
Sequence Length: 252
EC: 3.1.3.11
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O26957 | MEESDIYYWKGVAVRMAEQVERAVSPLVGTEDAGEIIKMGADGTPTKLIDLVAEDEAVGVLESTGRPVTIISEEIGVLHINSEGDEPGIIFVVDPLDGTSNAIRNIPFYGISVAVAERHPDGAAPTLNNVLMGFVKNFATGDLYWAIKGQGAFLNEKAISSSSQSSLDRTSLGAFIYGTRFRRVDSICRVIRRMRILGSVALELAYVASGSYDAFMDLRENLRIVDIAASKLIVEEAGGVVTNERGGEIDGLLNVKARTSLVAAGNLELHEKIMQTLEVI | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, and both D and L isomers of inositol-1-phosphate (I-1-P).
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 30173
Sequence Length: 280
EC: 3.1.3.11
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Q5JH93 | MEFNWSEIALNTAKELEEKIMPLFGTKKAGENVGTNVSGDVTKYVDKVAEDIILKRLVPLGVNVVSEEVGTVDSGSDYTVVVDPLDGSYNFSAGIPIFAFSLGIFKGKKPVYGAIYEFLPENFYEAKPGKGAYLNGERIRVNEPEPGKEALSFYTRGRCLGLVKKVKRVRVLGAIAVELAYVARGSLDGVFDIRNYVRPTDVAAGVLLVREAGGIVTDERGREFEVKLSATEKTNIIAVANERLLNTILEAMKDEP | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate (FBP) and inositol-1-phosphate (IMP). However, while possessing a high FBPase activity in vitro, does not participate in gluconeogenesis in vivo.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 27985
Sequence Length: 256
EC: 3.1.3.11
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O33832 | MDRLDFSIKLLRKVGHLLMIHWGRVDNVEKKTGFKDIVTEIDREAQRMIVDEIRKFFPDENIMAEEGIFEKGDRLWIIDPIDGTINFVHGLPNFSISLAYVENGEVKLGVVHAPALNETLYAEEGSGAFFNGERIRVSENASLEECVGSTGSYVDFTGKFIERMEKRTRRIRILGSAALNAAYVGAGRVDFFVTWRINPWDIAAGLIIVKEAGGMVTDFSGKEANAFSKNFIFSNGLIHDEVVKVVNEVVEEIGGK | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P) but displaying a 20-fold higher rate of hydrolysis of D-I-1-P than of the L isomer, 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, 5'-AMP and NAD(+). May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 28647
Sequence Length: 256
EC: 3.1.3.11
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P18892 | MAVFPNSCLAGCLLIFILLQLPKLDSAPFDVIGPQEPILAVVGEDAELPCRLSPNVSAKGMELRWFREKVSPAVFVSREGQEQEGEEMAEYRGRVSLVEDHIAEGSVAVRIQEVKASDDGEYRCFFRQDENYEEAIVHLKVAALGSDPHISMKVQESGEIQLECTSVGWYPEPQVQWRTHRGEEFPSMSESRNPDEEGLFTVRASVIIRDSSMKNVSCCIRNLLLGQEKEVEVSIPASFFPRLTPWMVAVAVILVVLGLLTIGSIFFTWRLYKERSRQRRNEFSSKEKLLEELKWKRATLHAVDVTLDPDTAHPHLFLYEDSKSVRLEDSRQKLPEKPERFDSWPCVMGREAFTSGRHYWEVEVGDRTDWAIGVCRENVMKKGFDPMTPENGFWAVELYGNGYWALTPLRTPLPLAGPPRRVGVFLDYESGDIFFYNMTDGSHIYTFSKASFSGPLRPFFCLWSCGKKPLTICPVTDGLEGVMVVADAKDISKEIPLSPMGEDSASGDIETLHSKLIPLQPSQGVP | Function: May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane. Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 59277
Sequence Length: 526
Subcellular Location: Membrane
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Q13410 | MAVFPSSGLPRCLLTLILLQLPKLDSAPFDVIGPPEPILAVVGEDAELPCRLSPNASAEHLELRWFRKKVSPAVLVHRDGREQEAEQMPEYRGRATLVQDGIAKGRVALRIRGVRVSDDGEYTCFFREDGSYEEALVHLKVAALGSDPHISMQVQENGEICLECTSVGWYPEPQVQWRTSKGEKFPSTSESRNPDEEGLFTVAASVIIRDTSAKNVSCYIQNLLLGQEKKVEISIPASSLPRLTPWIVAVAVILMVLGLLTIGSIFFTWRLYNERPRERRNEFSSKERLLEELKWKKATLHAVDVTLDPDTAHPHLFLYEDSKSVRLEDSRQKLPEKTERFDSWPCVLGRETFTSGRHYWEVEVGDRTDWAIGVCRENVMKKGFDPMTPENGFWAVELYGNGYWALTPLRTPLPLAGPPRRVGIFLDYESGDISFYNMNDGSDIYTFSNVTFSGPLRPFFCLWSSGKKPLTICPIADGPERVTVIANAQDLSKEIPLSPMGEDSAPRDADTLHSKLIPTQPSQGAP | Function: May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane (By similarity). Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58960
Sequence Length: 526
Subcellular Location: Membrane
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Q9FMK7 | MAITATQNDGVSLNANKISYDLVETDVEIITSGRRSIPAHSGILASVSPVLTNIIEKPRKIHGGSSKKVIKILGVPCDAVSVFVRFLYSPSVTENEMEKYGIHLLALSHVYMVTQLKQRCTKGVGERVTAENVVDILQLARLCDAPDLCLKCMRFIHYKFKTVEQTEGWKFLQEHDPFLELDILQFIDDAESRKKRRRRHRREQNLYLQLSEAMECIEHICTEGCTLVGPSSNLDNKSTCQAKPGPCSAFSTCYGLQLLIRHFAVCKKRVDGKGCVRCKRMIQLLRLHSSICDQSESCRVPLCRQYKNRGEKDKKMVEDTKWKVLVRRVASAKAMSSLSQSKKKKSEVLFKEEAEDLIRIRNKLM | Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Also targeted for degradation by the 26S proteasome pathway. May be involved in gametophyte development.
Sequence Mass (Da): 41480
Sequence Length: 365
Domain: The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q9KSL2 | MDFHRLLQHKQQRWQRSSYLLIGLFLSVCVLYLLVGELWLSPFSAWSSLEQQLVWELRLPRLLAAAVIGASLAVAGATLQVLLGNVLAEPGVVGVSGGASVAMVILLLFFPSLNSPVAFMAAAVLGALLFTLLLVVMARKLRLTTARLLLVGVALGILSGAVVTWAFYFSDDLGLRQLMYWLMGSVAGVSWYQHLLSLVAVPVVIWLVLQGGVLDKLMLGEGHAKQLGIDIHRVRWRLILAIALLVGASVALGGVIGFVGLVVPHLLRLTLGSENRLLLPLSALCGALLLVSADLIARLALGSGELPLGVVTTTLGAPIFIWMLVRNHDSC | Function: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35497
Sequence Length: 331
Subcellular Location: Cell inner membrane
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B0R5G4 | MTLDVTGLDVELAGTRILDDVHASIRDGHLVGVVGPNGAGKSTLLRAMNGLITPTAGTVLVAGDDVHALSSAAASRRIATVPQDASVSFEFTVRQVVEMGRHPHTTRFGTDTDTAVVDRAMARTGVAQFAARDVTSLSGGERQRVLLARALAQAAPVLLLDEPTASLDVNHQIRTLEVVRDLADSEDRAVVAAIHDLDLAARYCDELVVVADGRVHDAGAPRSVLTPDTIRAAFDARVAVGTDPATGAVTVTPLPDRTSAAADTSVHVVGGGDSATPVVRRLVSAGASVSVGPVVEGDTDHETARRVGCPCTSVAPFTRLEDTTAASATRADIAAADVIAVPVAAAARPGVRGLLTGAVPTLAVGDAAGAPEWADRLVACDAVVSAVGALADTPSDGV | Function: Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably responsible for energy coupling to the transport system (By similarity).
Catalytic Activity: an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40466
Sequence Length: 398
Subcellular Location: Cell membrane
EC: 7.6.2.8
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Q2HGY8 | MAAADDAQFPPPKVLTYPASTPPTLITQGAEGRLYKTTHLTRDRPCALKYRPPKPYRHPVLDARLTKARLSSEAKVLERCWREGVPVPAVYAMDPAAGWMMMEWIEGIPVRVGINEWLGDRPEEGAEIPQVADETPIVDLMKRIGAAIGALHKTGVVHGDLTTSNMMLRPRGFNPVDGAPGDEGKAGSVEGDVVLIDFGLATQSMSDEDRAVDLYVLERAFASTHPRAERLFATLLESYKSTFKKASSVLIKLEDVRMRGRKRSMLG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 29394
Sequence Length: 267
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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P0CP73 | MAASTPLLSRGTLIKQGAEAKVYALPSLFPEPTTYHPGSSSSFSAASPTPVILKHRFTKTYRHPTLDASLTSQRLTFEARALARAAKAGVTVPKVVWVDEKAGVIGMERIEGWSVREILGGGAEGEVEVIEEQEIEEDVENKAEDSAVREEPEGPESEGLKALKNLGVTQEHLMRSIGAALARLHKTMIIHGDLTTSNMMVRLTPGGSGPYEIVLIDFGLSSQAQFPENYAVDLYVLERAFASTHPRSEKLYAGVLETYAEGLGEKKWKPIQIKLKDVRRRGRKRDMTG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 31670
Sequence Length: 289
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q6BHA8 | MTDHIVKKAQECLPNIPLTVISQGAEALVFYTDVHPYANEPYLQNRGKYVIKYRPSKPYRHPKVDSSITKSRTVGEVKFMYKLNKLNINSPRIISADYNNGIIWMEYIGYSLPNGDVSSFKNWLWYLERNNQDCTSESVEKMCFKVGQLIGKLHLHEMIHGDLTSSNILLNDDEPVLIDFGLSSYSGLAEDRAVDLYVLERAITSTHSVYAKEYNQWLLQGYEDVHKHKEFGKQGQKKLVEVLKKLDDVRLRGRKRSMLG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 29991
Sequence Length: 260
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
|
Q54W07 | MDANECSNSENSATTTIPKSASPSTTISTKVVKLDEIGILISQGAEAKTYETDLYGLKCIVKERFSKAYRHPILDQKISSKRILQEVRSLNKCKKKGIQVPSLYLVDIGNNRIYMEFIKGETVKHYLYKNQESTQHQNQIESIMKELGNQIGIIHEMNVIHGDLTTSNMLLRESTNELVFIDFGLSYTSNSVEDKAVDLYVLERAFISTHPNSEQLFQTILSNYELTSSNSKIVIQKLNQVRLRGRKKTCFG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Bud32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit osgep (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 28577
Sequence Length: 252
Subcellular Location: Nucleus
EC: 3.6.-.-
|
Q5BAB7 | MPPTNRPPPFSTILSSASLPSYSSTDELTPIYQGAEAHLYKTTFLSPSQPAALKIRPSKPYRHPILDRRLTRARILQEARCLQKLVKEGVSVPALLGVDWEPSAGDGSSWLVMEWIEGEPVRVILEEWEAYLKGIEREKRLGLGEGVQGSEEEKVRGLMRRIGRAVGGLHRAGVIHGDLTTSNLMLRPLGSADTTETIEERDQSPSMAGEVVMIDFGLAMQSSQDEDRAVDLYVLERAFGSSHPRTERFFEEVLVGYRESYKGAVSALKRLEDVRMRGRKRSMIG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 31806
Sequence Length: 285
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
|
Q8SVD9 | MGFHFQGAESIISADGETVVKKRARKAYRIEALDLKIINGRTKREAKILRKLEALGIPAPRLISTYGDTIVMEKVEGTVLKEMIDSSDNPGALFRDLGALVSRLHIADIIHGDLTTSNFIHGSKIYAIDFGLSYISRKDEDKAVDLYVFEKAVGCAHDAKFLEDFYCGYMGEGSESVLKKLGTVRLRGRKREAMAFG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 21847
Sequence Length: 197
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
|
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