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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q8EC35 | MKSWCKNLLAAGLSLAMLSACSSSDVEEEPVSELTAIQATVFPEVSWSASVGDGVGDYYSRLTPAVRYGKIFAADRYGAVMAFDEASGEQVWRKDFSEEFRDNALAKNKGARLAAGITAARNKLFIGGESGLLAALNAEDGQVLWHVIAGGELLSKPTVADDVVVVSTSSGSLEAYNVDTGAKLWVYDMQLPNLTLRGTGSAAYEAGGFFIGTADGKVAVVVKNNGQAAWEQAIYNPTGGNEFTRMADVDMTPLILGDNLYAVSYNGNLVSMELRTGRIIWTRKYSSFNELTTAGLSLFLVDDHSRIYSVDRRNGLELWSNSELVNRTLTSPEVYKDYLVVGDFEGYLHFIDRSTGSIVGRIQVDSSGLFSQPIVVDDKIYVQGRSGKLAVVTLP | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42690
Sequence Length: 395
Subcellular Location: Cell outer membrane
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C0HLZ9 | MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY | Function: Secreted immune-induced peptides induced by Toll signaling . Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705 . In adult males, activity appears to be important for neuromuscular processes that mediate correct wing posture upon Toll activation .
PTM: Proteolytically cleaved.
Sequence Mass (Da): 28036
Sequence Length: 257
Subcellular Location: Secreted
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O57878 | MVSMTKWDEIRKYTSKKIEKNLEIVKLDEKYIPRASGFKYYPMVIERSSGSRIWDKDGNEYIDFLTSAAVFNVGHTHPGVVKAVEEQIKKFFNYTMGYLYVEPPVRLAELLVEITPGNFEKKVTYGFSGSDAVDSSIKAARAYTKRVNIISFLHSYHGMTYGALSATGILDPKLKKLLHPMGNFHHVEFPDPYRNSWGIDGYEDPSELANRALDEIERKIKELNEDVAGIIIEPIQGDAGVVIPPEEFVRDLKKLTEEYGIVFIDEEVQTGMGRTGRWWGIEHFGVTPDLIVSAKALGGGMPISAVVGKAEIMDSVPVPFFVFTHIGHAVNASAAIATINVIKEEKLVERSEKLGEYMLKRLRELQETYPIIGDVRGKGLLIGVDIVKEGTREPDRSLAQKISWRAWEKGLIMITFGKHGNVLRIAPPLNIPQEDLDKGVEIIEESIKDAVEGKIPDEVLKFLRAW | Function: Amino-acid racemase able to utilize a broad range of substrates . Can use Met, Leu, Phe, Ala, Ser, Ile, Val, Trp, Tyr and Thr . Is mostly active with Phe, Leu, Met and Tyr, followed by Ile, Thr and Trp. Has weaker activity with Val, Ser and Ala . Shows no activity toward Pro, Asp, Glu, Arg, His, Gln and Asn .
Catalytic Activity: an L-alpha-amino acid = a D-alpha-amino acid
Sequence Mass (Da): 52392
Sequence Length: 466
EC: 5.1.1.10
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P0AEC7 | MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSETPLEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTPTRLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSGISSRVVTPEVNEIVVNPNATLDWQLALRQAAGKTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSGTKEEDLEPELLELLDEMDNVAREASKILG | Function: Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system. Phosphorylates UvrY, probably via a four-step phosphorelay (By similarity).
PTM: Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 102453
Sequence Length: 918
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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Q21209 | MFENTKKALETFRTAIECVKCKKPRGDLQYLGSSCKHAYCWECIATFQQKPSGKRSSVARHMCPSCAFPLDTSKITEAHMLKTCFDTLSELNDLLQKVGTTSLTQAEFACTQNIFNKEKTPADAVEKFLETQAHMPDEMGQLGEEDDDLMCKDENRENSNSPELDIFHDYSKEASPTRNSTKRPSTVSVHERKPKRSSILKTSVKNEPAAPVVDLFASQVPQRTHQNDLLTPFIERRSTAPAATGVATYAQAFGSSSNPVKAEIIEEDIFSKAIPLTKRQASMSASAKKQPKLEPEEPEEVPSTSRSRKNSIKSDKIERRSQSPMSFGEKSMSVKSEQRRSSYGTRRGEAVLVNSIRNNRIPQLRSAVEAGTCVNEKEDGKTPLYVAVENSSLEAVKILVEAGAVINASCGSTLETTLHEAVRRQNTQIVEYLLSKGASIKIRNIAGKTVEEMAKSDPKIRKIIEKFKTEQRVLQPVVAPPKSRLHFVQLIDEKMLTESEKRKLPGKINIVPADMDSPTHVVVTVDLKTRVLNINKEHIGEILKAIIKSGMIVSRDWLRACIIDPSKVDDDRSYMVQKVRWMEGEVFENTIEQWKKTITKMQPKLFAGCKFFIPKPKYNFLDRPALFEIIRSAGGQAAAREPIIDEKDPPPYHNANLKPNFVLYSLTHDIGDKFRDCTKYNLVSEQWLIEAILGCSITTPPH | Function: Constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity . When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recombinase rad-51 or the E2-ubiquitin-conjugating enzyme let-70, which activate the CeBCD complex as an E3-ubiquitin ligase . Moreover, association between the brc-1-brd-1 heterodimer and rad-51 and let-70, probably requires DNA checkpoint proteins such as atl-1 and mre-11 in order to induce ubiquitination at DNA damage sites . To this end, the brc-1-brd-1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability . Plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation for example . In particular, protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability .
PTM: Autoubiquitinated.
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): 78804
Sequence Length: 702
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q99728 | MPDNRQPRNRQPRIRSGNEPRSAPAMEPDGRGAWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMIQLCSKLRNLLHDNELSDLKEDKPRKSLFNDAGNKKNSIKMWFSPRSKKVRYVVSKASVQTQPAIKKDASAQQDSYEFVSPSPPADVSERAKKASARSGKKQKKKTLAEINQKWNLEAEKEDGEFDSKEESKQKLVSFCSQPSVISSPQINGEIDLLASGSLTESECFGSLTEVSLPLAEQIESPDTKSRNEVVTPEKVCKNYLTSKKSLPLENNGKRGHHNRLSSPISKRCRTSILSTSGDFVKQTVPSENIPLPECSSPPSCKRKVGGTSGRKNSNMSDEFISLSPGTPPSTLSSSSYRRVMSSPSAMKLLPNMAVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRPVDYTDDESMKSLLLLPEKNESSSASHCSVMNTGQRRDGPLVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDAVQSTLKCMLGILNGCWILKFEWVKACLRRKVCEQEEKYEIPEGPRRSRLNREQLLPKLFDGCYFYLWGTFKHHPKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYHARPDSDQRFCTQYIIYEDLCNYHPERVRQGKVWKAPSSWFIDCVMSFELLPLDS | Function: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.
PTM: Processed during apoptosis. The homodimer is more susceptible to proteolytic cleavage than the BARD1/BRCA1 heterodimer.
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): 86648
Sequence Length: 777
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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P0C6N0 | MARFIAQLLLLASCVAAGQAVTAFLGERVTLTSYWRRVSLGPEIEVSWFKLGPGEEQVLIGRMHHDVIFIEWPFRGFFDIHRSANTFFLVVTAANISHDGNYLCRMKLGETEVTKQEHLSVVKPLTLSVHSERSQFPDFSVLTVTCTVNAFPHPHVQWLMPEGVEPAPTAANGGVMKEKDGSLSVAVDLSLPKPWHLPVTCVGKNDKEEAHGVYVSGYLSQ | Function: Plays diverse functions in immunomodulation and oncogenicity, maybe by acting as a functional receptor for human CSF1. May inhibit interferon secretion from mononuclear cells. Exhibits oncogenic activity in vitro (By similarity).
PTM: Phosphorylated on serine and threonine by host.
Sequence Mass (Da): 24471
Sequence Length: 221
Subcellular Location: Secreted
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A1BIZ8 | MRLAFWLYEGTALHGISRITNSMKGVHTVYHAPQGDDYITATYTMLERTPDFPGLSISVVRGRDLAQGVSRLPSTLQQVDHHYSPDLTVIAPSCSTALLQEDLNQLAAHSGVPSEKLLVYALNPFRVSENEAADGLFTELVKRYAVAQEKTPTPSVNLLGFTSLGFHLRANLTSLRRMLEALGIAVNVVAPWGSGIDDLAKLPAAWLNIAPYREIGATAAAYLDETCGMPAMYEAPIGVEPTTAWLRKLLDEINRIAGQKGLSRLAMPAPRAFSLDGLSAPSGVPWFARTADMESFSNKRAFVFGDATHTVALVKFLRDELGMQIIGAGTYLERHADWVRKELDGYLPGELMVTDRFQDVAKFIDDQMPDLVCGTQMERHSCRKLDVPCMVICPPTHIENHLLGYYPFFGFDGADVIADRVYLSCKLGLEKHLIDFFGDAGLEYEESDDAAKAEPDQPVSNAHGHTESKTVSQGEPIASDEGGISWSDEAETMLKKVPFFVRKKVRKNTEDFALGIGESCVTAEVFRKAKESLGG | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 58733
Sequence Length: 535
Pathway: Porphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis (light-independent).
EC: 1.3.7.7
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D5ANS3 | MSPRDDIPDLKGFDGDGEGSVQVHDSEDIGLDVGGARVFSVYGKGGIGKSTTSSNLSAAFSLLGKRVLQIGCDPKHDSTFTLTGRLQETVIDILKQVNFHPEELRPEDYVTEGFNGVMCVEAGGPPAGTGCGGYVVGQTVKLLKQHHLLEDTDVVVFDVLGDVVCGGFAAPLQHADRALIVTANDFDSIYAMNRIIAAVQAKSVNYKVRLAGCVANRSRETNEVDRYCEAANFKRIAHMPDLDSIRRSRLKKRTLFEMDDAEDVVMARAEYIRLAETLWRSTGEPGLTPEPLTDRHIFELLGFD | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 33205
Sequence Length: 304
Pathway: Porphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis (light-independent).
EC: 1.3.7.7
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P26236 | MPSDYAEIRNRVEHYFDRTATRAWARLTTADEKVSKVRQTVREGRDTMRAVMLSRLPDDLTGCRVMDAGCGTGLTTVELARRGADVVAVDISPQLIDIAKDRLPPELRGKVSFHVGDMADPALGQFDYVVAMDSLIYYRAPDIGRVLTELGKRTHSAIVFTVAPKTAFLMAFWWLGKLFPRSNRSPVMIPHALDKLQRHAGDSLIKIDRVARGFYISECLEYRP | Function: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX methylester using S-adenosyl-L-methionine as a cofactor.
Catalytic Activity: Mg-protoporphyrin IX + S-adenosyl-L-methionine = Mg-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25225
Sequence Length: 224
Pathway: Porphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis (light-independent).
EC: 2.1.1.11
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P42333 | MAKKAKYPDVPIRFSETFSDTNLYIVLLIGVPLYGVITSYLFNREYAESTLKNLLTIPVSRISLIVSKLVLLLIWIMMLTLIAWVLTLLFGLIGQFEGLSSAVLIEGFKQFMIGGALLFFLVSPIIFVTLLFKNYVPTIIFTIIISMVSIMVYGTEYSALFPWSAVWVIASGTFFPEYPPEYSFISVAATTVLGLAATIVYFKKIDIH | Function: Part of the binding-protein-dependent transport system for bacitracin that confer resistance to this antibiotic; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23324
Sequence Length: 208
Subcellular Location: Cell membrane
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Q5WNX1 | MLNLISCELSKLKRSKMVLISVAGVLSTPLLMLIEALQTHFDKPEIIFTLSDIYSDSVLYIMLLVNMMIYVAIAAYLYSREYTENTLKTILPIPISRTKLLIGKFCTLLLWIVMLTLVTWAGIFIVCGLYHVVFTLEGYSLLVAISWLPKFLFGGILMFLTTSPFVFIAFKTKGFVAPVIASAVIVMGSVALSNQELGALYPWTATFFLIDGRIESTGYPLALAIGIIILVSAVGFFMTFHHFKKEDLK | Function: Essential for high-level bacitracin resistance . Part of the ABC transporter complex BcrAB. Probably responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27788
Sequence Length: 249
Subcellular Location: Cell membrane
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O87875 | MSAKTNPEVIKESSMVKQKEMIAGNYDRLTGTKESGEKVVSTFVPGNLNELIMCFDMVNNLPETNAIQNGMRKQSGGMIMDAEKAGHSEDVCTYVKADIGMMGRGNIAPNGKPMPAPDMLLLSYTGCFTFMKWFELLRHEYKCPTVMLQIPYQGDGKITKNMRDFVVKQLKEEVIPMFEQVSGVKFDIDRLREYLKNSAKAEDDLVWVLESAKNRPSPIDAYFGGVYYIGPMFTAFRGTADAVEYYGLLRGEIEQRIREGKGPITPEGDMKEEKYRLVVEGPPNWTSFREFWKLFYDEGAVVVASSYTKVGGLYDQGFRHDPNDPLGTLADYCLGCYTNNNLPQRVELLEKYMNEYQADGLLINSIKSCNSFSAGQLLMMREIEKRTGKPAAFIETDLVDPRYFSHANVKNRLESYFQMVDQKRSGASLATA | Function: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring.
Catalytic Activity: 2 ADP + cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + benzoyl-CoA + 2 H2O + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 48803
Sequence Length: 432
EC: 1.3.7.8
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P42334 | MSFSELNIDAFRFINDLGKEYSMLNPVVYFLAEYMMYFLALGLVVYWLTRTTKNRLMVIYAVIAFVVAEILGKIMGSLHSNYQPFATLPNVNKLIEHEIDNSFPSDHTILFFSIGFLIFLFHKKTGWLWLVLAFAVGISRIWSGVHYPLDVAAGALLGVLSALFVFWTAPKLSFIHQMLSLYEKVEQRIVPSKNKSNDKSKNF | Function: Part of the binding-protein-dependent transport system for bacitracin that confer resistance to this antibiotic; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23274
Sequence Length: 203
Subcellular Location: Cell membrane
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P94571 | MNYEIFKAIHGLSHHNSVLDSIMVFITEYAIVAYALILLAIWLFGNTQSRKHVLYAGITGIAGLVINYLITLVYFEPRPFVAHTVHTLIPHAADASFPSDHTTGALAISIAMLFRNRKIGWPLVIFGLLTGFSRIWVGHHYPVDVLGSLVVAIIIGFLFFRFSDLLRPFVDLVVRIYEAIINKLTKKPTDQNF | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21723
Sequence Length: 193
Subcellular Location: Cell membrane
EC: 3.6.1.27
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O87874 | MSTADIIARCEALYEDLDFTAARQWKEADPSRKVIAYMPVYVPREIIHAAGMLPLGIMGGGDGLEVIHGDAFYQSYICRIPRSTIELGLSKRMDFVDGMLFPSICDVIRNLSGMWKLMFPGKYVRYFDVPQNYRDDVGGNYYTAELNELREGLEHLSGRKITDDALRASIKVYNENRKLVQDVYGLRSREPWKVPSADVYLLMRAGLVLPVEEHNQMLKDYLAAAVKVEAQKRDNCRVIINGSFCEQPPLNLIKSIELSGCYIVDDDYMIVHRFLRNEVSTAGDPMQNLSLAFLHESISTAAKYDDKEEDKGKYLLEQVRTNAAEGVIFAAPSFCDPALLERPMLADRCSENKVPYISFKYAENSGQMQPIREQAGTFADSIKLWS | Function: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring.
Catalytic Activity: 2 ADP + cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + benzoyl-CoA + 2 H2O + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 43720
Sequence Length: 386
EC: 1.3.7.8
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O87877 | MTITAGIDIGTGAVKTVLFRVEGDKTEWLAKRNDRIRQRDPFKLAEEAYNGLLEEAGLKASDVDYVATTGEGESLAFHTGHFYSMTTHARGAVYLNPEARAVLDIGALHGRAIRNDERGKVETYKMTSQCASGSGQFLENIARYLGIAQDEIGSLSTQADNPEVVSSICAVLAETDVINMVSRGISAPNILKGIHISMAGRLAKLLKSVGARDGVVLCTGGLALDEGLLKTLNESIQEQKMAVVAYNHPDSPYAGAIGAALWGAFRHEKLARLGQQQVAEAA | Cofactor: The iron-sulfur cluster may be a [4Fe-4S] cluster.
Function: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring.
Catalytic Activity: 2 ADP + cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + benzoyl-CoA + 2 H2O + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 30157
Sequence Length: 282
EC: 1.3.7.8
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Q5WNW9 | MEFNEKLQQLRTGKNLTQEQLAEQLYVSRTAISKWESGKGYPNMESLKCISKFFSVTIDELLSGEELITLAETENRSNLKKIYNYIYGILDMMAVAFIFLPLYGNSVGGYVYAVNLLSFTATTPFNLAVYWSAFAALIIIGIGKIISTHLDKEKWGGIATKCSLTITALAVCFFAAAREPYITVLVFLLLIGKIFVWIKQMGMK | Function: Functions as both a membrane-bound sensor and transducer of bacitracin availability to activates transcription of the bcrABD operon in the presence of bacitracin . Binds specifically to two inverted repeat sequences on the bcrABD promoter, irrespective of bacitracin concentration .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22887
Sequence Length: 204
Domain: Contains an N-terminal helix-turn-helix DNA-binding domain, an intermediate oligomerization domain and a C-terminal transmembrane domain.
Subcellular Location: Cell membrane
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P28246 | MTTRQHSSFAIVFILGLLAMLMPLSIDMYLPALPVISAQFGVPAGSTQMTLSTYILGFALGQLIYGPMADSFGRKPVVLGGTLVFAAAAVACALANTIDQLIVMRFFHGLAAAAASVVINALMRDIYPKEEFSRMMSFVMLVTTIAPLMAPIVGGWVLVWLSWHYIFWILALAAILASAMIFFLIKETLPPERRQPFHIRTTIGNFAALFRHKRVLSYMLASGFSFAGMFSFLSAGPFVYIEINHVAPENFGYYFALNIVFLFVMTIFNSRFVRRIGALNMFRSGLWIQFIMAAWMVISALLGLGFWSLVVGVAAFVGCVSMVSSNAMAVILDEFPHMAGTASSLAGTFRFGIGAIVGALLSLATFNSAWPMIWSIAFCATSSILFCLYASRPKKR | Function: Involved in sulfonamide (sulfathiazole) and bicyclomycin resistance . Probable membrane translocase. A transporter able to export peptides. When overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth . Cells overexpressing this protein have decreased intracellular levels of Ala-Gln dipeptide, and in a system that produces the Ala-Gln dipeptide overproduction of this protein increases export of the dipeptide .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43353
Sequence Length: 396
Subcellular Location: Cell inner membrane
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P45123 | MNQQKSTFIFILTLGILSMLPPFGVDMYLPSFLEIAKDLDVSPEQVQHTLTSFAYGMAFGQLFWGPFGDSFGRKPIILLGVIVGALTALVLTEINSVGNFTALRFVQGFFGAAPVVLSGALLRDLFSKDQLSKVMSTITLVFMLAPLVAPIIGGYIVKFFHWHAIFYVISLVGLLAAALVFFIIPETHKKENRIPLRLNIIARNFLLLWKQKEVLGYMFAASFSFGGLFAFVTAGSIVYIGIYGVPVDQFGYFFMMNIVTMIFASFLNSRFVTKVGAETMLRIALAIQFLSGMWLILTALLDLGFWPMAIGVAFFVGPNPVISSNAMASALERCPQMAGTANSLIGSVRFAVGAIMGSLVASMKMDTAAPMLFTMGACVVISVLAYYFLTSRNLKSRG | Function: Involved in sulfonamide (sulfathiazole) and bicyclomycin resistance. Probable membrane translocase (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43459
Sequence Length: 398
Subcellular Location: Cell inner membrane
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Q54HY8 | MNHLKDQSKSIVLGISSGIGIFLISGGINIFKNVGQYILNRINSNIYYRIDVDSKDKSFEWLLYWLSENDSIKVSNHLNAETVYNLVGKNPKVILVPSVGKHRIVYKGKWIWIDRVRDQQFDMGAGAPFESISISTYKSNAQLINQLLQEAMTLSLNRDIGKTVIYINGGNGNWERFGNPRSIRSLSSVILADDLKSKLIEDIKSFITNESWYRNRGIPYRRGYLLYGEPGNGKSSLINAIAGELNLDICIVSLSSKDIDDKQINHLLNNAPPKSILLIEDIDAAFKSHRDNVDSNNNNSNNNNSLTYSGLLNALDGVASQEGRILFMTTNKIELLDSALIREGRIDLKIKVSNATKSQAAQLFTHFYNLPTDNQLAIRFSENLHDHQLSMSQIQGFLLKYINSPEKAIEEVQSITPFNLN | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47356
Sequence Length: 421
Subcellular Location: Mitochondrion inner membrane
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Q54DY9 | MENVITNNNKGLPKSILKFIPEPIQPLFENPFFSAGFGLIGVGSILAMGRKGFQQAMIQSRRYFFVSVEVPSKDKSFHWLMEWLATKKNKNTRHVSVETTFHQHESGDIVSRINFVPSVGTHYVFYRGRVIKVERSREKNVIDMNSGNLWESITLTTLGTGRQVFQNLIEEAKEMALEKEEGKTLIYTSMGTDWRRFGHPRRKRPISSVILDKGKSELIIQDVKKFLNNSDWYNDRGIPYRRGYLLYGPPGTGKSSFITALAGELQLSICILNLAGKSVSDTSLNQLLATAPQRSIILLEDIDSAIQTGNHDLSAKSNSANAPSISSGGLQYQGYYGNPSVSSGGSALTFSGLLNALDGVAASEGRILFMTTNHLEKLDKVLIRPGRVDLQIEIGLCSSYQMEQMFLKFYPTDFDLAKQFVEKLENYKFSPAQLQAYFMTYSNNSIEAINNLNELIKK | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 51361
Sequence Length: 458
Subcellular Location: Mitochondrion inner membrane
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Q5E9H5 | MPLSDFVLALKDNPYFGAGFGLVGVGTALALARKGAQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRHSTRTQHLSVETTYLQHESGRISTKFEFVPSPGNHFIWYQGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFGYPRRRRPLNSVVLEQGVTERIVRDIREFIDNPKWYIDRGIPYRRGYLLYGPPGCGKSSFITALAGELQHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVLLEDVDAAFLSRDLAAENPIKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHIDRLDPALIRPGRVDMKEYVGHCSRWQLTQMFQRFYPGQATSLAENFADRVLQATTQISPAQVQGYFMLYKNDPAGAIQNAESLRR | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47504
Sequence Length: 419
Subcellular Location: Mitochondrion inner membrane
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P50736 | MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNYPTHQTFFSSSEKLEIGDVAFITENRKPVRIQALSYYREVVKRKNIRVNAFEMVRKVTKTQNNTFVIETSKETYTTPYCIIATGYYDHPNYMGVPGEDLPKVFHYFKEGHPYFDKDVVVIGGKNSSVDAALELVKSGARVTVLYRGNEYSPSIKPWILPEFEALVRNGTIRMEFGACVEKITENEVVFRSGEKELITIKNDFVFAMTGYHPDHQFLEKIGVEIDKETGRPFFNEETMETNVEGVFIAGVIAAGNNANEIFIENGRFHGGHIAAEIAKRENH | Function: S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a NADPH-dependent bacilliredoxin reductase, which debacillithiolates (removes BSH) the S-bacillithiolated BrxB (BrxB-SSB), and to a lesser extent BrxC (BrxC-SSB). Involved in a redox cascade increasing the efficacy of BrxB function by reducing BrxB-SSB and thus reactivating it. Has NADPH-dependent oxidase activity under aerobic conditions producing hydrogen peroxide (H(2)O(2)).
PTM: C-terminal Cys can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation protects Cys residues against overoxidation by acting as a redox switch in response to oxidative stress.
Sequence Mass (Da): 36409
Sequence Length: 324
EC: 1.8.1.-
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Q08347 | MIGAFKRNRGSSQSFAKECQPSTLKANLEVAKELPFSDRRDFEDATQGYIGSLSDEQIIGPDGGVVWCMKSYGFLEPETPANTVNPSLWRQAQLNAIHGLFKITDNVYQVRGLDISNMTIIEGNTSLIIIDTLFTTETAQESLKLYYRHRPQKPVRTVIYTHSHSDHYGGVKGIVKEADVKSGEVQIIAPVGFMESVVAENILAGNAMHRRSQYQFGMLLSPSVKGHVDCGIGKAASHGTVTLIAPTIIIEEPVEERTIDGVDFVFQLAPGSEAPSEMLIYMPQQRVLNMAEDVTHHMHNLYALRGVEVRDGNQWAKYIDAARVAFGSKTDVLIAQHHWPTTGQMRINELLKKQRDMYKFIHDQTLRLLNQGYTSRDIAETLRMPSSLEQEWSTRGYYGTLSHNVKAVYQKYLGWYDANPANLNPLPPVAYAKKAVEYMGGADAVLARAYKDFQKGEFRWVASVVNQLVFADPNNHQARELCADALEQLGYQAEASTWRNAYLVGAMELRQGVPKRRSTGKRNNIAVLNNEMFFDFLAVRLNATKAEGKIIVSNWCFINSNERFVITLENCALTYIQGWQTDADATITLKRTTFEALLANEITMVDFLRSKEVEIEGNRLRIEELLKLFDDFDQSFPVVEPMGGST | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Alkyl/aryl-sulfatase. Enables the use of SDS and 4-nitrocatechol as sulfur source.
Sequence Mass (Da): 72646
Sequence Length: 646
EC: 3.1.6.-
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O13932 | MGSRFGRRKERNGDMLPLYESQSPQHLDSLENENDERISKLTGKVKSLKELTMNIGTEITSSTKLMESMNDSFDSTKSLLSGTMTRLKNVSKNGGISIWMWLAFFCLVALILVLVRF | Function: SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13251
Sequence Length: 117
Subcellular Location: Golgi apparatus membrane
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P22804 | MSSRFAGGNAYQRDTGRTQLFGPADGSNSLDDNVSSALGSTDKLDYSQSTLASLESQSEEQMGAMGQRIKALKSLSLKMGDEIRGSNQTIDQLGDTFHNTSVKLKRTFGNMMEMARRSGISIKTWLIIFFMVGVLFFWVWIT | Function: SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 15720
Sequence Length: 142
Subcellular Location: Golgi apparatus membrane
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A0A0C6DWS6 | MPPTNGQTAIIQSKTCPTPTTLPLVVAHGRPLPPLPSSHHVRVRVLAVGLNPTDHKMVTHFFMQDNTTGCDFCGIIEEVGSASALPLGLRVCGADFPYRPSNPYNGAFAEYAVADSRHLLQIPDAISNIQAAAIGAIGWGTAALAMSDPTALNLPGTPSKPDARSLPVLVYGGATATGIIAIQMLKRSGYIPIAVCSAQSAPLCISLGAVGTACYTSTTCVQDIKALANGQSIKHALDCITDPESTTVCLASLARIGGRYACLEAVSDACITRRSVAVKVVMGFEGQNFDVDLGHPVYSRKANPALHAVAAQWAAELQPLLNAGIIKTQPLEEIEGRFEGVIKALEMLQGGHIKGKKLVVNISS | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of betaenones, phytotoxic polyketides involved in leaf spot disease in sugar beets . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase bet1 and the enoyl reductase bet3 via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations . The C-terminal reductase (R) domain of bet1 catalyzes the reductive release of the polyketide chain . Because bet1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase bet3 . The short-chain dehydrogenase/reductase bet4 then catalyzes reduction of dehydroprobetaenone I to probetaenone I . The cytochrome P450 monooxygenase bet2 catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I . The FAD-linked oxidoreductase (orf1) is probably responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A (By similarity).
Catalytic Activity: acetyl-CoA + 10 AH2 + 2 H(+) + 7 malonyl-CoA + 5 S-adenosyl-L-methionine = 10 A + 7 CO2 + 8 CoA + dehydroprobetaenone I + 6 H2O + 5 S-adenosyl-L-homocysteine
Sequence Mass (Da): 38107
Sequence Length: 364
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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A0A0C6E5D0 | MKSFATTVLLVTPGIYAAALSGRQGQAINSSCKVIPGDTAWPSRQIWSQLNDTLDGRLIQSTPQAAVCRPGGYGSISENGTECTTLKEDWDYAKAFLDSAVEIMNPWYQNTSCSPFYRVDQPCTLGNYVSYAIPVSGPEDVVTAINFTQTHNVRLVIKNTGHDYLGKSTGTGGLSLWTHNLQSKQIVNYTSPAYSGPAIKVGAGVTGGEALLHASQFGYRLVSGDCSTVGYAGGYSSGGGHSLLNSVHGMAADNVLEWEVVTADGRHLVASATQNSDLYWALSGGGAGNLAVVLSMTAKVHPDGLVGAATLSFNATSSPSNTSYISAINAWWTFLPTLIDAGASPSFNIYTNNFLIYNTTAPGKSAQDMSTLYAPYLSTLSSLSIPYTFQTYTAPSFLQHYNATDGPLPYGPYVASQLFNSRMIPRSLSSSPSNLTTAILSSVATDAPGIWQLGCLGINVNSTRISHPDNAVAPHWRTAMAVCLEFSLYDWAIPEEEMVARRQHLADVIHPAIVKVTPGSGAYLNEADPLVYPVGEDGWKDAFYGANYERLRGLKREWDPERVFYAYTAPGSEEWVSDAEGRLCRV | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of betaenones, phytotoxic polyketides involved in leaf spot disease in sugar beets . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase bet1 and the enoyl reductase bet3 via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations . The C-terminal reductase (R) domain of bet1 catalyzes the reductive release of the polyketide chain . Because bet1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase bet3 . The short-chain dehydrogenase/reductase bet4 then catalyzes reduction of dehydroprobetaenone I to probetaenone I . The cytochrome P450 monooxygenase bet2 catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I . The FAD-linked oxidoreductase (orf1) is probably responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A (By similarity).
Catalytic Activity: betaenone C = betaenone A
Sequence Mass (Da): 62959
Sequence Length: 586
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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A6X2G8 | MKAQPKASHFIGGAFVEDKTGKPSPVIYPATGEEIARLYSATPDVIEAAYAAALKAQGEWAALKPVERGRILRRTADILREKNKKLSKLETLDTGKALQETLVADAASAADALEFFGGIISGFNGEFVELGGSFAYTRREALGICVGIGAWNYPIQIAAWKSAPALAMGNAFIFKPSENTPLSALALAEAYKEAGLPDGLFNVVQGFGDVGAALVNHRLTAKVSLTGSVPTGKRIMAQAGEHLKHVTMELGGKSPIIVFDDADIESAIGGAMLGNFYSTGQVCSNGTRVFVHKNLRERFVERLVERTRKIRIGDPLDEATQMGPLVNRAQRDKVLSYIEKGKAEGATLACGGGVPKLQGFDKGYFIEPTIFTDVTDDMTIAREEIFGPVMSVLEFSDEDEVIARANDTEFGLAAGVFTADIARGHRVIGQIKAGTCWINAYNLTPVEVPFGGYKQSGIGRENGIAALAHYSQIKTVYVEMGKVDSPY | Cofactor: Binds 2 potassium ions per subunit.
Function: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.
Catalytic Activity: betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH
Sequence Mass (Da): 52218
Sequence Length: 487
Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
EC: 1.2.1.8
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Q9WTZ9 | MANVHQENEEMEQPLQNGQEDRPVGGGEGHQPAANNNNNNHNHNHNHHRRGQARRLAPNFRWAIPNRQMNDGLGGDGDDMEMFMEEMREIRRKLRELQLRNCLRILMGELSNHHDHHDEFCLMP | Function: May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death.
PTM: Ubiquitinated (Probable). Degraded by the proteasome.
Sequence Mass (Da): 14542
Sequence Length: 124
Domain: The nuclear export signal is required for export from the nucleus and the interactions with itself and p75NTR/NGFR.
Subcellular Location: Nucleus
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Q9NWD9 | MESKEELAANNLNGENAQQENEGGEQAPTQNEEESRHLGGGEGQKPGGNIRRGRVRRLVPNFRWAIPNRHIEHNEARDDVERFVGQMMEIKRKTREQQMRHYMRFQTPEPDNHYDFCLIP | Function: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability.
PTM: Ubiquitinated and degraded by the proteasome.
Sequence Mass (Da): 14067
Sequence Length: 120
Subcellular Location: Cytoplasm
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Q9CWT2 | MASKFKQVILDLTVEKDKKDKKGGKASKQSEEEPHHLEEVENKKPGGNVRRKVRRLVPNFLWAIPNRHVDRNEGGEDVGRFVVQGTEVKRKTTEQQVRPYRRFRTPEPDNHYDFCLIP | Function: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability.
PTM: Ubiquitinated and degraded by the proteasome.
Sequence Mass (Da): 13820
Sequence Length: 118
Subcellular Location: Cytoplasm
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Q5R590 | MESKEELAANNLNGENAQQENEGREQAPTQNEETRHLGGGEGQKPGGNIRRGRVRRLVPNFRWAIPNRHIEHNEARDDVERFVGQMMEIKRKTREQQMRHYMRFQTPEPDNHYDFCLIP | Function: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability.
PTM: Ubiquitinated and degraded by the proteasome.
Sequence Mass (Da): 14051
Sequence Length: 119
Subcellular Location: Cytoplasm
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P22930 | MTTENAAIPTKKKKSFWKKMKPLFGLTVLIPTAFSAVYFGLFASDIYVSESSFVVRSPRSQSSLSGVGALLQSTGFSRSQDDTYSVQEYMRSRTALSALEQGLPLRTFYSEKGDLLSRFNGFGLNDTQEAFYRYFKERLSVDVDSISGIATLRVHAFDAEEGYQINERLLKEGESLINRLNERARKDTIEFAEQAVKDAEKNVNETAQALSQYRIKNKIFDLPAQSGVQLSLISSLKSELIRVETQLAQLVSITPDNPQVPALQMRQKSLKKEIDEQTRQLSGNGNSAATQTADYQRLMLANELAQQQLAAAMTSLQNTRGEADRQQLYLEVISQPSKPDWALEPSRIYNIIATFIIGLMLYGVLNLLIASIREHKN | Function: May form an ATP-driven capsule polysaccharide export apparatus, in association with the BexA, BexB and BexD proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42292
Sequence Length: 377
Subcellular Location: Cell inner membrane
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P9WQ26 | MNTSASPVPGLFTLVLHTHLPWLAHHGRWPVGEEWLYQSWAAAYLPLLQVLAALADENRHRLITLGMTPVVNAQLDDPYCLNGVHHWLANWQLRAEEAASVRYARQSKSADYPSCTPEALRAFGIRECADAARALDNFATRWRHGGSPLLRGLIDAGTVELLGGPLAHPFQPLLAPRLREFALREGLADAQLRLAHRPKGIWAPECAYAPGMEVDYATAGVSHFMVDGPSLHGDTALGRPVGKTDVVAFGRDLQVSYRVWSPKSGYPGHAAYRDFHTYDHLTGLKPARVTGRNVPSEQKAPYDPERADRAVDVHVADFVDVVRNRLLSESERIGRPAHVIAAFDTELFGHWWYEGPTWLQRVLRALPAAGVRVGTLSDAIADGFVGDPVELPPSSWGSGKDWQVWSGAKVADLVQLNSEVVDTALTTIDKALAQTASLDGPLPRDHVADQILRETLLTVSSDWPFMVSKDSAADYARYRAHLHAHATREIAGALAAGRRDTARRLAEGWNRADGLFGALDARRLPK | Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position (Probable). Is probably involved in the biosynthesis of 6-O-methylglucosyl lipopolysaccharides (MGLP) (By similarity).
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 57815
Sequence Length: 526
EC: 2.4.1.18
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Q5JDJ7 | MKGYLTFVLHTHIPYVRKHGKWPFGEEWVFEAISETYIPLLMEFERLRDSGVKFGIVINVTPVLAEQLTDEYMKKAFEEYMERKLKAMEEDLKSGKYDEKAVSYMLNYFRKVYDYWKAINGDIIGKLRELQDQGYVEVITSAATHGYLPLLGRDEAIRAQIANGVATYEKHFGMKPKGIWLPECAYRPAGEWELPGGRKVKRQGIEKFLEEFGLRYFFVESRLIDEGPASNVYGEVLIADTEKTTLRPYWIKGSNVAVFARNRETGHQVWSAHYGYPGDFWYREFHKKAPKSGGQYWRITSKEVGLGEKEFYDPDKAMERVEEHARHFVSLVERLLREHEEKFGEKGIIVAPYDTELFGHWWFEGVKWLGRVLELLYQRGVETPTLSRFLEEYSGEKHEIELPEGSWGANSDHSTWWNEETEWTWPHIYRAEDRMVAIVSRFRGRDELTNRVIEQLARELLILEASDWQFLITTGQAKEYAKRRVLIHSRDFHRLANELVRYVKIGEFDVKLLEELEERDNPFRPVVVGPYVSENPPELEEYVEPPEVPPEKEETEEKPKVLTEKATSLALAVKKVKPVKEETREVKKKAVEASKRGKRKSSKSKRLPRKVSKKAPSKGPSDLLSIKGIGPKTFQKLKRAGVETIEDLKNANIEDLARKTGISTKRLKKFIAQVE | Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two local maxima at DP 6 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Does not display alpha-galactosidase or pullulanase activity, since melibiose and pullulan are not substrates. Is not able to catalyze the hydrolysis or transglycosylation of maltoheptaose, suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity.
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 78549
Sequence Length: 675
Domain: The C-terminus contains two copies of a helix-hairpin-helix (HhH) motif that are dispensable for activity and thermal stability.
EC: 2.4.1.18
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Q5SH28 | MARFALVLHAHLPYVRAHGMWPFGEETLYEAMAETYLPLIRVLERLRAEGVEAPFTLGITPILAEQLADARIKEGFWAYAKDRLERAQGDYQRYRGTALEASARHQVAFWELTLDHFQRLSGDLVAAFRKAEEGGQVELITSNATHGYSPLLGYDEALWAQIKTGVSTYRRHFAKDPTGFWLPEMAYRPKGPWKPPVEGPPEGVRPGVDELLMRAGIRYTFVDAHLVQGGEPLSPYGEAALGPVESQEATYHVHELESGLRVLARNPETTLQVWSADYGYPGEGLYREFHRKDPLSGLHHWRVTHRKADLAEKAPYDPEAAFAKTEEHARHFVGLLERLAGRHPEGVILSPYDAELFGHWWYEGVAWLEAVLRLLAQNPKVRPVTAREAVQGPAVRTALPEGSWGRGGDHRVWLNEKTLDYWEKVYRAEGAMREAARRGVLPEGVLRQAMRELLLLEASDWPFLMETGQAEAYARERYEEHARAFFHLLKGASPEELRALEERDNPFPEADPRLYLFREA | Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 3 to 13, with two local maxima at DP 7 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis of the substrate, being 4% of the total activity. Can use amylose as substrate but not alpha-1,4-linked oligosaccharides of 2-7 glucose residues, beta-cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-maltosyl-beta-cyclodextrin. Is not able to branch amylopectin further, it only hydrolyzes amylopectin. Thus, displays preference for linear and long substrates (amylose) over branched structures (amylopectin).
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Sequence Mass (Da): 59169
Sequence Length: 520
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
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P47113 | MSIRPLTLNGLDEPETSFEELNTTLPRFQSHETLTLEENVPPLSTSTYIPPPSSVGTSDTGTVFSNSTSAFWSNKQADDDQDMEVDQDDEFLNDFQEFQNKKDDFDDAIKTNFHLRNGCRTGPFKNDIFAEEFDRKLSLEDKPRLKQPRSMMELKPKRKLSNSVTSRNLRSGNSVRFKKSMPNLALVNPAIREEEEDEEREREDQREFNYKIDNDTQDTILAKFSSDDEGDFLTGFEELEGEAIDETISSNDKESADHPRFLKKSSSSLPLKISPAQYDIVKHDELLTPGLHRRQRDWNTQQELDSFKEKRSVRHCSNQNVQLNGPAKIKTIKQQIDHNTPMKKGSMIYNPKTMKWEGNENVLSKFSDVDTANRKALLIKNKLQRDADSKKQKYSDLQHARATSRNQKVIGNMILDEQNLRWVSVSEEEADPFAGIPEINLPPVGKSMKKRSSSPFLRSKSQVNTPFVSNDNDGVYQSTAAQARLRKYHSMRTLNGTTETPEISSTFHLSSRALEKFYHEENRWCKKLASWFIPRDETIISVDEETIMDESTVNSKRKSYMYEIRNMVINSTKD | Function: Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. This cell-cycle arrest depends upon inhibition of the G-protein TEM1 by the BFA1/BUB2 complex.
PTM: Multiply phosphorylated in a cell-cycle-dependent manner with the major phosphorylation occurring in mitosis.
Sequence Mass (Da): 66086
Sequence Length: 574
Subcellular Location: Cytoplasm
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A1DJ58 | MKFLLRRFIALAAASSVVAAPSVSHLSLQDAANRRELLQDLVTWDQHSLFVRGERLMIFSGEFHPFRLPVPGLWFDVFQKITSLGFNAVSFYTDWGLMEGNPGHVVTDGIWSLDEFFTAASEAGIYLIARPGPYINAETSAGGIPGWVLRLKGIIRSNSEDYLRATDTYMATLGKIIAKAQITNGGPVILVQPENEYTTWPNVSESEFPTTMNKEVMAYAEKQLRDAGVVVPTVVNDNKNLGYFAPGTGLGETDLYGIDAYPMRYDCGNPYVWPTYRFPRDWQHTHRNHSPTTPFAIMEFQGGSGDGWGGVTEDGCAILVNNEAVRVVYKNNYGFGVGVFNIYMTYGGTNWGNLGYHGGYTSYDYGAAITEDRQIWREKYSEEKLQANFLKVSPAYLTATPGNGVNGSYTGNKDIAVTPLFGNGTTTNFYLVRHADFTSTGSVQYQLSVSTSVGNVTIPQLGGSLSLNGRDSKFHVTDYDVGEFNLIYSSAEIFTWAKGDNKKRVLVLYGGAGELHEFALPKHLPRPTVVDGSDVKMAKKGSAWVVQWEVTAQRRVLRAGKLEIHLLWRNDAYQHWVLELPAKQPIANYSSPSKETVLVKGGYLLRSACITNNKLHLTGDVNATTPLEVISAPKRFDGIVFNGQSLKSTRSKIGNLAATVRYQPPAISLPDLKRLDWKYLDSLPEISPDYSDEGWMSLTNTYTNNTRKFTGPTCLYADDYGYHGGSLIYRGHFKANGDESWVFLNTSGGVGFANSVWLNQTFLGSWTGSGNNMTYPRNISLPHELSPGKPYVFTVVIDHMGQDEEAPGTDAIKFPRGILDYALSGHEVSDLKWKMTGNLGGEQYQDSTRGPLNEGAMYAERRGYHLPNPPTSSWKSSSPINDGLTGAGIGFYATSFSLDLPEGYDIPLSFLFNNSASDARSGTSYRCQLFVNGYQFGKYVNDLGPQTNFPVPEGILNYNGVNYVAVSLWALEPQGALVGGLELVASTPILSAYRKPVPAPQPGWKPRRGAY | Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 111421
Sequence Length: 1011
Subcellular Location: Secreted
EC: 3.2.1.23
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C8WV58 | MAKHAPIFPNVQGFLHGGDYNPDQWLAYPDVLEQDVQLMREAKWNVVSLGIFSWVSLEPEEGLFTFEWLDEAIERLTHAGVRILLATPSGARPAWLSAKYPEVLRVGPDGRRNRHGGRHNHCYTSPIYREKVRIINRKLAERYAHHPGVIGWHVSNEYGGECHCPLCQEAFREWLKRKYKTLDALNHAWWTPFWSHTYTDWSQIESPMPHGETSIHGLNLDWKRFVTDQTVDFCRHEIEPLKQVNPNLPVTTNFMGTYPGLNYWRFRDVLDVISWDSYPRWHAHETLVPEAVHTAMVHDLNRSILKKPFLLMESTPSVTNWQAVSKQKRPGVHVLVSLQAVAHGADSVQYFQWRKSRGSYEKFHGAVVDHVGHANTRVFRDVQAVGEMLERLAPMAGAEVKADAAVIFDWENRWALEDAKGPRNIGMHYEETVVNHYAALWRMGVPMDVIDEEQPLDGYKLVVAPMLYMVRPGVAERMKAFVERGGSLVLTYWSGIVDENDLVFLGGFPGPLRELAGVWAEEIDALYDGERVPVRVADGNPLGLAGHYEARELCEVVHLEGAEPIAVYGADYYEGMPAATVHRVGKGKVYYVAARLEDAFLRDFFARVAAEAGVARAIERELPDGVSAMVRSGDGVEYVMLMNFTPEAREVALDEAEYKPLYGEAPTDGAVRLPAYGVSVLERPARNG | Function: Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-nitrophenyl-beta-D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-xylopyranoside (PNPX) or p-nitrophenyl-beta-D-arabinopyranoside (PNPA). Also hydrolyzes lactose, including lactose in milk.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 77869
Sequence Length: 688
EC: 3.2.1.23
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A1A399 | MSARRNFEWPELLTADGRGIAFGGDYNPDQWSEDIWDDDIRLMKQAGVNTVALAIFSWDRIQPTEDRWDFGWLDRIIDKLGNAGIVVDLASATATAPLWLYESHPEVLPRDKYGHPVNAGSRQSWSPTSPVFKEYALTLCRKLAERYGTNPYVTAWHMGNEYGWNNREDYSDNALEAFRAWCRRKYGTIDALNQAWGTTFWGQEMNGFDEVLIPRFMGADSMVNPGQKLDFERFGNDMLLDFYKAERDAIAEICPDKPFTTNFMVSTDQCCMDYAAWAKEVNFVSNDHYFHEGESHLDELACSDALMDSLALGKPWYVMEHSTSAVQWKPLNTRKRKGETVRDSLAHVAMGADAINFFQWRASAFGAEAFHSAMVPHAGEDTKLFRQVCELGASLHTLADAGVQGTELAHSDTAILFSAESEWATRSQTLPSMKLNHWHDVRDWYRAFLDAGSRADIVPLAYDWSSYKTVVLPTVLILSAADTQRLADFAAAGGRVVVGYATGLIDEHFHTWLGGYPGAGDGLLRSMLGVRGEEFNILGAEAEGEPGEIRLSSADDSAALDGTTTRLWQNDVNVTGEHAQVLATYAGEEADEWELDGTAAVTRNPYGSGEAYFVGCDLDVADLTKLVRAYLAASSQENADVLHTVRASADATFDFYLPRGKKTVELQGIEGEPVILFQTDREEKPGSYTVRRNGVLVVRR | Function: Involved in the hydrolysis of transgalactooligosaccharides (TOS). Highly active towards Gal(beta1-4)Gal and Gal(beta1-4)-Gal-containing oligosaccharides. Low activity towards Gal(beta1-3)Gal, lactose and Gal(beta1-3)GalOMe. No activity towards Gal(beta1-6)Gal, Gal(beta1-4)Man, Gal(alpha1-4)Gal, Gal(alpha1-3)Gal(beta1-4)Gal, lactulose, 3'fucosyllactose, lacto-N-fucopentaose I, lacto-N-fucopentaose II, cellobiose, maltose or sucrose. No transglycosylation activity is found at high substrate concentrations (100 mg/ml) and only low transglycosylation activity at lower substrate concentrations (10 mg/ml).
PTM: The N-terminus is blocked.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 78025
Sequence Length: 700
EC: 3.2.1.23
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Q93GI5 | MEHRAFKWPQPLAGNKPRIWYVGDYNPDQWPEEVWDEDVALMQQAGVNLVSVAIFSWAKLEPEEGVYDFDWLDRVIDKLGKAGIAVDLASGTASPPMWMTQAHPEILWVDYRGDVCQPGARQHWRATSPVFLDYALNLCRKMAEHYKDNPYVVSWHVSNEYGCHNRFDYSEDAERAFQKWCEKKYGTIDAVNDAWGTAFWAQRMNNFSEIIPPRFIGDGNFMNPGKLLDWKRFSSDALLDFYKAERDALLEIAPKPQTTNFMVSAGCTVLDYDKWGHDVDFVSNDHYFSPGEAHFDEMAYAACLTDGIARKNPWFLMEHSTSAVNWRPTNYRLEPGELVRDSLAHLAMGADAICYFQWRQSKAGAEKWHSAMVPHAGPDSQIFRDVCELGADLNKLADEGLLSTKLVKSKVAVVFDYESQWATEHTATPTQEVRHWTEPLDWFRALADNGLTADVVPVRGPWDEYEAVVLPSLAILSEQTTRRVREYVANGGKLFVTYYTGLVDDRDHVWLGGYPGSIRDVVGVRVEEFAPMGTDAPGTMDHLDLDNGTVAHDFADVITSVADTAHVVASFKADKWTGFDGAPAITVNDFGDGKAAYVGARLGREGLAKSLPALLEELGIETSAEDDRGEVVRVERADETGENHFVFLFNRTHDVAVVDVEGEPLVASLAQVNESEHTAAIQPNGVLVVKL | Function: Specific for beta-D-anomer-linked galactoside substrates. Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG), chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal) and to a lesser extent lactose. Hydrolyzes p-nitrophenyl-beta-D-galacturonide very slightly. Does not hydrolyze maltose, sucrose, raffinose or melibiose. Has some transgalactosylation activity yielding galacto-oligosaccharides (GaOS), including O-beta-D-galactopyranosyl-(1,3)-O-beta-D-galactopyranosyl-(1-4)-D-glucopyranose.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 77453
Sequence Length: 691
EC: 3.2.1.23
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P49676 | MKMKQFNLLSLFLILITSFGSANSTIVSHDERAITIDGQRRILLSGSIHYPRSTSDMWPDLISKAKDGGLDTIETYVFWNAHEPSRRQYDFSGNLDLVRFIKTIQSAGLYSVLRIGPYVCAEWNYGGFPVWLHNMPDMKFRTINPGFMNEMQNFTTKIVNMMKEESLFASQGGPIILAQIENEYGNVISSYGAEGKAYIDWCANMANSLDIGVPWIMCQQPHAPQPMIETCNGFYCDQYKPSNPSSPKMWTENWTGWFKNWGGKHPYRTAEDLAFSVARFFQTGGTFQNYYMYHGGTNFGRVAGGPYITTSYDYDAPLDEYGNLNQPKWGHLKQLHTLLKSMEKPLTYGNISTIDLGNSVTATVYSTNEKSSCFIGNVNATADALVNFKGKDYNVPAWSVSVLPDCDKEAYNTARVNTQTSIITEDSCDEPEKLKWTWRPEFTTQKTILKGSGDLIAKGLVDQKDVTNDASDYLWYMTRVHLDKKDPIWSRNMSLRVHSNAHVLHAYVNGKYVGNQIVRDNKFDYRFEKKVNLVHGTNHLALLSVSVGLQNYGPFFESGPTGINGPVKLVGYKGDETIEKDLSKHQWDYKIGLNGFNHKLFSMKSAGHHHRKWSTEKLPADRMLSWYKANFKAPLGKDPVIVDLNGLGKGEVWINGQSIGRYWPSFNSSDEGCTEECDYRGEYGSDKCAFMCGKPTQRWYHVPRSFLNDKGHNTITLFEEMGGDPSMVKFKTVVTGRVCAKAHEHNKVELSCNNRPISAVKFASFGNPSGQCGSFAAGSCEGAKDAVKVVAKECVGKLNCTMNVSSHKFGSNLDCGDSPKRLFVEVEC | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 93019
Sequence Length: 828
Subcellular Location: Secreted
EC: 3.2.1.23
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Q9TRY9 | MARPAAVRVLWALLLPLLLGSARGLRNASQRTFTIDYSHNRFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPQPGQYQFSGEQDVEYFIKLAHELGLLVILRPGPYICAEWDMGGLPAWLLLKESIILRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPIITMQVENEYGSYFTCDYDYLRFLQKLFHHHLGNDVLLFTTDGANEKFLQCGALQGLYATVDFGPGANITAAFQIQRKSEPKGPLVNSEFYTGWLDHWGQPHSTVRTEVVASSLHDILAHGANVNLYMFIGGTNFAYWNGANMPYQAQPTSYDYDAPLSEAGDLTEKYFALREVIRKFEKVPEGFIPPSTPKFAYGKVALKKLKTVEEALNVLCPPGPINSLYPLTFIQVKQYFGFVMYRTTLPQDCSDPTPLSSPLSGVHDRAYVSVDGVPQGVMERSNVITLNITGKAGATLDLLVENMGRVNYGRYINDFKGLISNLTLGSSILTNWMIFPLNTEDAVRSHLGGWHGPNNGRHDKTFAHRSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQMTLFVPRHILVTSTPNTIMVLELEHAPCGDSGPEVCTVEFVDRPVIGAPPTPGHPPPDLSHRDLRLDYV | Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 74992
Sequence Length: 668
Subcellular Location: Lysosome
EC: 3.2.1.23
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Q9RFN0 | MLQQKKLFYGGDYNPEQWSKAIILEDMRLMKKANVNYVSLNIFGWASIQPTEEGFDFSFLDEMLDLLWENGIGIDLANGTASPPAWLVKKHPEILPVTSQGTPLVHGSRQHYCPSNKVYRSYVIRLTEEVAKRYATHPGIVMWHVNNEYTCHISECYCESCEKSFRQWLQMKYKKINTLNECWSTKFWSQSYSQWDEIFLPKEMPTFKNPAHQLDYKRFISDQNLTLFKAEKKAIRSYSKDIPVMTNLMGLHKHVDGFAFAEEMDVVGWDSYPNPFEEKPYPQFLANDLTRSLKKKPFLVMEQAPSAVNWRRANGAKSPGQMRLWSYEALAHGADGILFFQWRQSQGGAEKFHSGMVSHNQDTNSRIFKEVVQLGTEMSQLDELVGTNYNAEVAIVFDWENWWALELDAKPSGEINYIKQMRDLYTIFHELNIGVDFIHPKEDLSNYKLVLSIAQYLVTDDFSAKVKRYIKAGGHFLTTFFSGIVDEYDRVYLGGYPGAFKEVLGIYVEEFDPMPIGRKSQIKYGETYYTTELWKEVIHLQGAETIATFTEGYLMGQPALTKFGYGKGKTYYMGTKLAKDGNMKFIQTILAESKIQPLNQVEIESENSKISMTCRSNSSHDYIFLLNYGQTSEKVKLKKGGQSLLDGSMVEGEVSVKANDVKIIKLTK | Function: Capable of hydrolyzing the chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) at low temperatures. pNP-beta-galactoside, pNP-beta-fucoside and pNP-beta-galacturonide are also hydrolyzed, but not pNP-beta-galactosidase, pNP-alpha-galactoside, pNP-beta-mannoside, pNP-beta-arabanoside, pNP-beta-xyloside, pNP-beta-glucuronide nor pNP-betacellobioside at 20 degrees Celsius.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 76789
Sequence Length: 668
EC: 3.2.1.23
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D9SM34 | MRIGVDYYPEHWDRQLWEKDAQLMKEIGVKVVRLAEFAWCKLEPIEGQYDFKWLDDVIEIFSVRNIEIVLGTPTNTPPLWLYEKYPDAIQVNESGERQFIGIRGHRCYNSSSMRKYTKAIVEAMTERYANNKAVIGWQIDNELDATHCCCDNCTEKFRGWLKNKYSTLENINKEYGNVVWSGEYSAWSQVTAPLGGSPFLNPSYLLDYNRFASDSMVEYIDFQREIIRKNCPSQFITTNTWFTGNLPNFYDAFENLDFVSYDNYPTTNEITDEEELHSHAFHCDLMRGIKKKNFWIMEQLSGTPGCWMPMQRTPKPGMIKGYSFQAIGRGAETVVHFRWRNAIIGAEMFWHGILDHSNVKGRRFYEFAELCREVNKINEEIPDYKINNEVAILYSSDQDFAFKIQPQVEGLYYLQQLKAFHNALIRLGVGTDIINWSESLNKYKVVIAPTLYLTDDNVTTELYRFVEAGGTLILTNRTGVKNMNNVCLMEQMPSNLKECAGVVVKEYDPIGHSIHTIKDEAGKVYQCKQWCDILEPTTAKVIATYNDDFYIDEAAVTVNKYKKGNVYYLGTVFNSDYYIELLSKILDEKELPYYKKLPYGLELSVLENENGKYLMVFNNSNEIKCFEGKHEGKSIIRNELDGKSFTLEPYGIEVLQLVE | Function: Involved in plant cell wall degradation in cooperation with cellulosome. Hydrolyzes both p-nitrophenyl-alpha-L-arabinopyranoside (pNPAp) and p-nitrophenyl-beta-D-galactopyranoside (pNPGp), with higher activity for pNPAp. Shows hydrolysis activity against p-nitrophenyl-beta-D-fucopyranoside (pNPFp), but not against p-nitrophenyl-alpha-L-arabinofuranoside (pNPAf), o-nitrophenyl-beta-D-galactopyranoside (oNPGp), p-nitrophenyl-beta-D-xylopyranoside (pNPXp), p-nitrophenyl-beta-D-glucopyranoside (pNPGLp), p-nitrophenyl-beta-D-cellobiopyranoside (pNPCp), p-nitrophenyl-beta-lactopyranoside (pNPLp) or p-nitrophenyl-alpha-galactopyranoside (pNPalphaGp). No detectable activity against arabinan or arabinoxylan, but activity against arabinogalactan can be detected. Increases degradation activity of alpha-L-arabinofuranosidase (ArfA) and endo-1,4-beta-xylanase (XynA) when corn fiber gum and corn stem powder are used as substrates.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 76464
Sequence Length: 659
EC: 3.2.1.23
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Q8L7J2 | MGRIKSSSGRCSTARLEAVAVLVVVFGVASSSLRGCIAQQSGGGLTRGSFPEGFVFGTASAAYQYEGAVKEDGRGQTIWDTFAHTFGKITDFSNADVAVDQYHRFEEDIQLMADMGMDAYRFSIAWSRIYPNGVGQVNQAGIDHYNKLIDALLAKGIQPYVTLYHWDLPQALEDKYKGWLDRQIVDDFAAYAETCFREFGDRVKHWITLNEPHTVAIQGYDAGLQAPGRCSVLLHLYCKAGNSGTEPYVVAHHFILAHAAAASIYRTKYKATQNGQLGIAFDVMWFEPMSNTTIDIEAAKRAQEFQLGWFADPFFFGDYPATMRARVGERLPRFTADEAAVVKGALDFVGINHYTTYYTRHNNTNIIGTLLNNTLADTGTVSLPFKNGKPIGDRANSIWLYIVPRGMRSLMNYVKERYNSPPVYITENGMDDSNNPFISIKDALKDSKRIKYHNDYLTNLAASIKEDGCDVRGYFAWSLLDNWEWAAGYSSRFGLYFVDYKDNLKRYPKNSVQWFKALLKT | Function: Hydrolyzes glycosides, oligosaccharides and hydrophobic glycosides . Possesses gibberellin ester beta-D-glucosidase activity. Can hydrolyze gibberellin A4 beta-D-glucosyl ester in vitro .
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 58539
Sequence Length: 521
Subcellular Location: Secreted
EC: 3.2.1.21
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Q75I93 | MAARRANCALVLVLALALLAARDAGAAAVPKPNWLGGLSRAAFPKRFVFGTATSAYQVEGMAASGGRGPSIWDAFAHTPGNVAGNQNGDVATDQYHRYKEDVNLMKSLNFDAYRFSISWSRIFPDGEGRVNQEGVAYYNNLINYLLQKGITPYVNLYHYDLPLALEKKYGGWLNAKMADLFTEYADFCFKTFGNRVKHWFTFNEPRIVALLGYDQGTNPPKRCTKCAAGGNSATEPYIVAHNFLLSHAAAVARYRTKYQAAQQGKVGIVLDFNWYEALSNSTEDQAAAQRARDFHIGWYLDPLINGHYPQIMQDLVKDRLPKFTPEQARLVKGSADYIGINQYTASYMKGQQLMQQTPTSYSADWQVTYVFAKNGKPIGPQANSNWLYIVPWGMYGCVNYIKQKYGNPTVVITENGMDQPANLSRDQYLRDTTRVHFYRSYLTQLKKAIDEGANVAGYFAWSLLDNFEWLSGYTSKFGIVYVDFNTLERHPKASAYWFRDMLKH | Function: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 56872
Sequence Length: 504
Subcellular Location: Secreted
EC: 3.2.1.21
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Q75I94 | MGCAPAAHYLPGGGWRRLLVVVVALVVLDRAGARVRAADDDTGGLSRAAFPKGFVFGTATSAFQVEGMAASGGRGPSIWDPFVHTPGNIAGNGNADVTTDEYHRYKEDVDLLKSLNFDAYRFSISWSRIFPDGEGKVNTEGVAYYNNLIDYVIKQGLIPYVNLNHYDLPLALQKKYEGWLSPKIVGVFSDYAEFCFKTYGDRVKNWFTFNEPRIVAALGHDTGTDPPNRCTKCAAGGNSATEPYIVAHNIILSHATAVDRYRNKFQASQKGKIGIVLDFNWYEPLTNSTEDQAAAQRARDFHVGWFLDPLINGQYPKNMRDIVKERLPTFTPEQAKLVKGSADYFGINQYTANYMADQPAPQQAATSYSSDWHVSFIFQRNGVPIGQQANSNWLYIVPTGMYGAVNYIKEKYNNPTIIISENGMDQSGNLTREEFLHDTERIEFYKNYLTELKKAIDDGANVVAYFAWSLLDNFEWLSGYTSKFGIVYVDFTTLKRYPKDSANWFKNMLQASGPGSKSGSGTSDSQVGSATSASHPVGSAISSSHRLLLPLLVSLHFLFPSFFMFLSL | Function: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, cello-oligosaccharides, laminari-oligosaccharides, sophorose and gentiobiose.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 63098
Sequence Length: 568
EC: 3.2.1.21
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Q75C24 | MQNVASWLLALVVAVVQGELLPGKSAPALLWSYKLSEGIQEYQLAYNMTTVLPAPEFNAIALELLDHCNSHAYVFVNQPGLRLEDFDYEDAWTVLPNYLSRSSSALRFEQVEVSPSNVFENLIAHTKRRCDVQREIILRAEQTNQFEPYIDAQSRIIQVHFSPLPGDGRNERPSREDVLADHDQRLRRILGRLPSPAVTVIYTSLEPADRLSASPPRAGIFPEIFEHESRRIEYERNDRDLQVNRYFPSHHPKMEPIEEVELSLLDPKFIQSNLKLLKLIAVSAIGSLTWQLYSLFSPKLPVATPKGTAKRQKGQKKLVKLATAQAAKQAEEVKLEVSQQEKED | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39105
Sequence Length: 344
Subcellular Location: Endoplasmic reticulum membrane
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Q59WG7 | MRLFVLLAYIIPFILCQLTPVLVASHKLVRGLKEEINPSNTLPHNVTSVTNMLKKLITECSSDAYLLINQPGLTYADLTTEKKDNWPFLRNYLYMSSTIVGLPRVENPIDLDFLEQYIISNCDAETINVWHDSEDEVVDYYDIRKRVIRIDLSPLSISNHDDRVKEIFEHDQLIRKILRKLPSAHYTIILTSLEPGIIHPVPRFLMEETPASFEIFDDIINDPFHNREIEKNDRFHKVEPNWNPIRDSNDRYYRNKKKDEIHLFDYELWEKNEKLITTIFVMVLSLFMMKIISFFNYLKQKIIQKKQQKSKRGIIADDKKLD | Function: Required for normal beta-1,6-glucan synthesis, for hyphal morphogenesis, adhesion and virulence.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38099
Sequence Length: 322
Subcellular Location: Endoplasmic reticulum membrane
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Q6FKH5 | MCGLIGIIIGLLTRVALASSLDVGTSPAILFSTRLSEGILEYYDMFDSGAVVPREDFNTVCKTLISHCNSDAVVFVNQPGLSLGDLSEYADQFQYLSSYVRHSSSAMNIERVSVSQDDQESQFESLVRYAMDTCNIYEKVVIEPYEADTYKAYIDAEKKVILIELPEFLNTQNETDRMALISSNDNRLRNILGQLPSPDISVIYTSFQPSNLAADEFAEILPAAFDVFDKNAAVERNIRLKDATRPGFINYRPKFGDFNSISQIKLDKQFLEENLGLLSAILVSTILYLFGQRLSSHSKSQNTTSNSAKNTTKKAERGN | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35559
Sequence Length: 319
Subcellular Location: Endoplasmic reticulum membrane
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Q6BHZ8 | MFISIRRLVALVAITQLVASFSAVPVLVASHRLAKGLKEELNGSGPQAPESATNLIKRLVTECSSDEYLVINQPGLVLEDMTVNEADNWPFLRRYIAMASSVVGIPWVRGALDLDFIEQYIISTCHAETMNVVHDDDQEVGNYIDTRTRVIKIDLSELPPRSDLELRYSVIREHDELIRKIIRKLPSPHYTIILTSDMPQNVHPIPNMVVESQPDKYQIFHDLVNDPSRELEIERNDRFHQTIEPYWSPDRNTINRYMENKKKDEIHFFDYDLWTRNEKLILTIIVMVLTLFTFQLTKLVKLLTETVFKKDKGLITHTKSE | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37170
Sequence Length: 321
Subcellular Location: Endoplasmic reticulum membrane
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Q6CMA4 | MQPSFMTMNELIVFALLLTPLLAARQQSVPGLLFSYNLAPGIVKYQDKYDNAQLPQDDFLKVAKDLISQCHSETYVFVNQPGLSRSDFKQHKQSMHKLYNYVLTSSTTVKFEKIDIVQNDDIYEELIAYTMDKCNIDDKIDIGGNVTDRYQPFVEARTRVLRVDFPPLPQQGQYVEGIGTRKDVLQANDEYLRYVMGTLPTPKHTVFYMSLEKSEVPDTETSLSYDIWPEIFTNPQRKVEIDRNDRVAKEMPKLVPYRPRIDTEDDKYLTVLDQEFIDNHYGIIVLIIGVTIAFILLQLGAVKVKKPSKPQITKDVTKEKKTQ | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37243
Sequence Length: 323
Subcellular Location: Endoplasmic reticulum membrane
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Q6CB37 | MKLALLSLIGTALATPAVMLSHKELTAFEKYTNKQTSNSISAVELDRVARKLMHDCSANTYVVVNQPGLKAKDFQTESAFPFLKKLLERTSTMYTVPYADGGIELGKLANSVAKQCGAVKIDVNLDNNITPLEEYMDTTKRVIEINFEPLPNTYVSRLAALAANDEMLEKIVRATPSPFIALILTSQKGEEGDFETRNPDFKIFPGVARAKTVPGAKDKYKYHMELQNVPVDEKKLTAEALLKVKTPPTHAPEVRQTGDGELVDDKLLLMIVGSVVAILLSLLVFNGLMAAKPDVVKVDKTDAKVEKAVKKEVQKKERLVNGRVEQLKRETR | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 36711
Sequence Length: 332
Subcellular Location: Endoplasmic reticulum membrane
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P38813 | MQTVLKYLLLIMCGSFCASEELQNQTNVPAIFFSYKLTPGILKYQEDYDRAVTLPRDTFIEAAEKFLGVCNADTYVFINQPGLRKLDFLEFETEFVSLQRYIRRSSTAIKFEKVDLLPQDLYYDLAEFVKEYCNVDQVLNLRGNNTEDFQPFIDSEKRVIIIEYPKLPEDTNERKEAFRHYDKYLRTILAQIPSPEQNVIYTSLNPGTTLAHESIIPIQIFPDIFDIKSRVGEVEQNNRVLDVPRLSFNDYTPRFSEPPSEYVSIFDSQLIENNRGLLQLIFTILVGYILIQFFFTKKTIVDEKITNKKDNVKQTSPQLLKKVQEIQKKPSQQVS | Function: Required for normal beta-1,6-glucan synthesis.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39069
Sequence Length: 335
Subcellular Location: Endoplasmic reticulum membrane
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A1BCQ5 | MRPVPLHPDILQAYAVLETGEPVCRELAFALGELHGPDVLDLASLAHKVKLRHGGSSGSIHACSIMNARSGVCSENCRFCAQSAHHQAAIDVYGLVDVDAVLFHARQTASEGISHFGIVTSGFGYKTLSKEFRQILAMIDRLHQELPDLEICASLGVLGEEPALELARHGIAQYNINIQVAPRRYGELIADTHSVDDRIDTIKRLRRNNIDVCCGGIIGVGEQMKERVEMIFAFADLDVSVIPLNILVPIDGTPLEGSPGIPLDDIVKTFALCRLVHPRKIIKIAAGRETVMKDFQGLLMLSGADGLLTGGYLTTRGRATADDRMFMRQLQWFN | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36542
Sequence Length: 334
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
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B5ECN1 | MEKMINDIAHRIIAGGSITEAEAIQLTQVQGTEVYDLFRAATRVKEHFVGNEVHLCSIINAKSGRCAENCAFCAQSAHHKTDAPVYPLVQEEEMLASARMAETNGSACFGIITSGTTVNGPELEQILTALRRIRKETTILPSCSLGIIDEETARKLKEAGMDTYHHNLETAASFFPQICTTHDYQDDVNTVRAVKKAGVKVCCGGIFGLGESAAQRVEMALTLKDLDVDSVPMNFLNPIEGTRLEGAANITAQECLKTIAIYRLILPGKRITVCGGREKNLRDLQSWIFFAGANGTMIGNYLTTLGRNVDTDLTMFSDLGLKTVMCAH | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35748
Sequence Length: 328
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
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Q97MI6 | MKNQWNNILSIGEKVLNGEKITADEALTLSKSNGSDIFLLCSFANKLREKFNGNHVDLCSVINAKSGNCSEDCAFCAQSAHHKANVSCYPLLNEDKILEMAKQREAYGARHCDIATSGLGYTGDEKDFQTILKAFKKMKENTNLKLCACLGTLTEKAMNSLAAVGVERYNHNLETAKSFYKNIVSTHGYDERIKTINYAKNAKMEVCSGMIVGLGETMEQRIEHALLLRDLNVDAVPVNILNPVKGTKLENAKPLSPMEIIKTFAIIRFILPDKIIRYAGGREKNLRSLQPLGFLSGLNGMLIGNYLTTNGQSVNDDFNMLKDLELEY | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36428
Sequence Length: 328
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
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A7GFJ9 | MSNIIKYKKKILNGDLLTKEEVEEILEEDITDLAATANEIRESLCGNKFDLCTIINGKSGRCQENCKYCAQSAHFDTDIIEYNILNSDRIINSAISNYNKGVHRFSVVTSGRALNNNEVDTLCKTYSKLKETCSIRLCASHGLLKYEDLKRLKDSGVTRYHNNLETSRKFFTKICTTHKYDDKIETIKNAKKAGLEICSGGIIGLGETMEDRIDMAFTLRELSVESVPVNILNPIKGTPLENQEILSYEEIIKTLALFRFILPTVQIRLAGGRTIISDNGKKALESGVNGAISGDMLTTLGIETSEDIKMIKNLGFEV | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35492
Sequence Length: 318
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
|
A1SM80 | MQTSFDHLADRILAGGDATPADALAVLRADEKDLLHVVAAAGRLRRARFGNTVKVNYLVNLKSGLCPEDCHYCSQALGSRAPILKYNWLSSEEVLEQAGAGLRGGATRVCLVSSGRGPSDRDVDRVAAMAQELKGEQPGVEICACLGLLKDGQAERLRAAGVDAYNHNINTAESHHDTIVSTHSYSDRVDTIEKAAAAGLSPCSGLIAGLGETDEQLVEALFALKALGADSIPVNFLMPFDGTPSERTFELTPIRCVQILAMTRFVCPDTEIRIAGGREMHLRSLQALALHVANSIFLGDYLTSEGQDARADLEMLRDNGFAILGAEAKPAGTATAAHRAQTAHDIAGGTSVAGSAPDPAIRRRGAGTDVPANA | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 39431
Sequence Length: 374
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
|
A6LD84 | MTIEEAKQHILEGGKITEEQALSLANHPDKEALYEAAHQITRHFMGNKFDTCSIINAKSGNCSEDCKWCAQSGHYKTLVNLYPLLPAKECVYHAVYNRKQGIRRFALVTSGKRVSDKELEQITDTIRQIKRQSDIKCCASMGLLTRSQLQSLYDSGVENYHCNIETAPSYFRQLCSTHTIEQKMETIHTAREIGFRICCGGIIGMGETMKERIEMACFLQKEGVLSIPLNLLQPIPGTPMENTQILEEEEWLTTIALFRLINPNAFLRFSGGRAQLSEVTQRKSLHIGINSAIIGDLLTTIGSKVEEDKVLFTSEGYSLTENTDWEK | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36871
Sequence Length: 327
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
|
A5D4Y6 | MFNELVKKIKSGLEITFEEALALGGLDEDRLNELFLAALQVNRHFHGNRVDLCSIVNARSGRCSEDCAFCAQSGHYRTEAPVYPLLSKEEILERAREMELRGARRFALVTSGRGISESDFEKVLDIYQMLKEKTGLGLCASLGIIGYDKAVRLKEAGVGMYHHNLETCRSYFPHICTTHSFDERVETVKAAKEAGLEVCSGGIIGLGESWRHRVEMAFHLKELGVASVPINILTPVKGTPLWGRPLLEPVEVLRTAAMFRLVLPGALIRLCGGREAALRDLQPLALLAGVNALMVGNYLTTSGRRVEDDLQMVADLKLSVM | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35453
Sequence Length: 321
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
|
P32451 | MMSTIYRHLSTARPALTKYATNAAVKSTTASSEASTLGALQYALSLDEPSHSWTKSQLKEIYHTPLLELTHAAQLQHRKWHDPTKVQLCTLMNIKSGGCSEDCKYCAQSSRNDTGLKAEKMVKVDEVIKEAEEAKRNGSTRFCLGAAWRDMKGRKSAMKRIQEMVTKVNDMGLETCVTLGMVDQDQAKQLKDAGLTAYNHNIDTSREHYSKVITTRTYDDRLQTIKNVQESGIKACTGGILGLGESEDDHIGFIYTLSNMSPHPESLPINRLVAIKGTPMAEELADPKSKKLQFDEILRTIATARIVMPKAIIRLAAGRYTMKETEQFVCFMAGCNSIFTGKKMLTTMCNGWDEDKAMLAKWGLQPMEAFKYDRS | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 41884
Sequence Length: 375
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Subcellular Location: Mitochondrion
EC: 2.8.1.6
|
Q818W9 | MSGFFITATDTEVGKTVVAGAIAGVFRELGYNVGVYKPLQSGHVASNPEGDAARLKSLSGVPTQENEICPYSIEEPLAPRLAMKRAGRVVKLKEITDYYNGLLKEFNSLFVEGAGGLAVPYTEDALVIDFAKELQLPLIVVARPTLGTVNHTVLTIAYAKAHGLTVAGVILSGCKECEMERVQENKEMIEELSGVPVLGLLPFFAGEFTKEEVLESAKEHIMISKLEEFIQNESNVAGAPSM | 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): 26075
Sequence Length: 242
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
P53558 | MRGFFVTGTDTEVGKTVISSGLAALLKDNNRHVGVYKPFLSGISRHHPDSDTSLLKDMSQTSLSHEDITPFAFKAPLAPYVAGKLEGKTVTMEEVLSHWGRIREKHECFIVEGAGGISVPLGEDYLVSHVIKALQLPMIIVARPRLGTINHTFLTVKYAESMGLPIAGIIINGISDSPDEDEKTNPEMIERLCGVPILGVTPKLANVTKETVLHMVKDHINLSLLMNQVGV | 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): 25160
Sequence Length: 231
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
Q9AMS4 | MNKRIVVTGTDTGVGKTVFSAGLAGLLGANYWKPVQAGLEQEIDSECIRRLGGLSSDRIVPELYRLRTPASPHHSAEIDGVRIDTETLGLPDSGERRLVIEGAGGLMVPLTARTLYIDIFERWQLPVVLCARTGLGTINHSLLSIEALRKRQIRILGIAFIGERNAETESAVCEIGRVRWLGRLPWLVPLTNDRLQAAFKDSFVSSDFLNL | 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): 23218
Sequence Length: 211
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
C0QVL9 | MAKAIFITATGTDIGKTYVSGLIAKHMKDKGLNIGYYKAALSGSLDITDSDAWYVKQQADLLDSYDEMVSYTYKHAYSPHLAAQIEGNPPDIKVIKNAYENINKKHDYMIVEGSGGIICPIRYDNNQKIFLEDIIKELNIPSLIIADAGLGTINSAVLTIEYMRSKNLKVNGVILNRFEMANEMHDDNKKMIEEMTGVKIIGIVIDGILKLDEKNIETLFE | 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): 24683
Sequence Length: 221
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
Q9I614 | MPAFFVTGTDTEIGKTTIAAGLLHAARSAGLSTAAAKPVASGCEPTAQGLRNGDALVLLGQCSLALAYEQVNPLAFAPAIAPHLAAREAGVELSAARLHEAVREVLALQADFTLVEGAGGWRVPLLGRENLSDLARLLALPVVLVVGVRLGCINHALLSAEAILGDGLALAGWVANVVDPATSRLEENLATLAERLPAPCLGRVPRLEEATPAAVAAHLDLRPLGIGL | 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): 23337
Sequence Length: 228
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
Q3IGS9 | MKEFFITGTDTDAGKTHVTSLLLKLLAQHKKQAIGFKPLASGCEMAFDQLVNADALILMESATVSAKYDIINPFAFAPAIAPHIAAEQAGVTITADKLSSAYKNVKQQGADYILTEGAGGWALPISNTDYLYNWVKAEQLPVILVVGMKLGCLNHALLTAAHMQSMGINCIGWIANQVDPNMDEYQANLDSLKLRLPFPILAISPYSEQTPKLQIYKTLLENFALNT | 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): 24715
Sequence Length: 227
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
Q7URG0 | MASLYFVTGTDTEVGKTYCTAKTVERMRECGQRVGVYKPVASGCELRADGQRYSVDAATLWQAAGRPKNIDAVCPQRFLAALSPPQSAAREGVKVDTRQLRDGLAIWCDGDFDVVMIEGAGGLFSPISDDWLNVDLAIEMKRWSDQNGHSFELLLVAPDRLGVLHHVISTSRAAESAGIPIAGLILNRMDDHADESTQTNAEDLRRWCGIPMVASVRQPSGPLVVFSGPNGRNASGETSRETAGGVNFLNQTTIRR | 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): 27750
Sequence Length: 256
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.3
|
Q0AE73 | MLPDLAEALQQRRQEGLYRFRQVLEGPQSPRVTIDGRDFLAFCSNDYLGLANHPALIEAVAAGAQRYGVGSGASHLISGHSRAHHELEEALAEFVGLPRTLLFSTGYMANMAVVTALMGREDAIFADRLNHASLNDAALLSRARFIRYPHLDLVTLEKQLKTIQARRRLIVTDAVFSMDGDRAPVAELLALCQRFDAWLLLDDAHGFGVLGEQGKGSLYDPQEVERNVPHLIYMATLGKAAGVSGAFVAAQASMIETLIQHSRTYGYTTAAAPLLAHALLTSLQLISQGVWRRERLVQLIEQLRQKLQSLPWQLLLSDTPIQPLLVGGSREAVRLDQALRERGIWVPAIRPPTVPQGMARLRISLSAAHAGEDVDQLSAALHDLAGC | 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): 42405
Sequence Length: 387
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
Q81ZZ4 | MLADLSEALRERQQEGLYRSRPVLEGPQSPHVTIDGRDFLAFCSNDYLGLANHPALIEAAAEGARCYGVGSGASHLISGHFRAHHELEEALAAFVGLPRTLLFSTGYMANMAVVTALAGRGDAIFADRLNHASLNDAALLSRARFIRYPHLDLDTLARQLETTKARRRLVVTDAVFSMDGDMAPVAELLTLCQRFDAWLLLDDAHGFGVLGERGKGSLYHSQRIERDTPYLIYMATLGKAAGVSGAFVAAQAPVVETLIQHGRTYGYTTAAPPLLAHTLLTSLQLISQESWRRERLALLIERLRQRLHSLPWPLLLSETPIQPLLVGESQEAVRLDLALRERGIWVPAIRPPTVPQGMARLRISLSAVHTEADVDRLGAALRDLAQC | 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): 42481
Sequence Length: 387
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
A1AQT1 | MGRTVQDELEQIRAKGLFRSTRLIQGRQSARVTMEGRQLLLLCSNNYLGLAEHPALIAASMAAAEQFGSSSGASRLVSGSMEPHEALETAVAAFKRTESALAFNSGYAANTGIIQALVGRGDVIFCDRLNHASIIDGALLSGARLVRYPHNDAVALAGLMEKQRGTGRCLIVSDGVFSMDGDLAPLAELAELRRRHDALLMVDDAHGCGVLGEQGRGSAELLGVLSHIDIHVGTFGKALGSFGAYAALSRELRDLLVNRARSFIFSTSLPPAVLAVSTAALELVQAAEGDELRKRLRDNTSLFRGLLRDAGFFLGEGNTQIVPILTGGAEETMDFSRQLLEEGMFVQGIRPPTVPAGACRLRCTVMATHSPQDLTWAAERITHIGRRLGVV | 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): 41815
Sequence Length: 391
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
A9BGL0 | MDFYEQLREELKKLEDSGLLITIRTLESAQGAWININGKKVLNMCSNNYLGLANNERLKEAAINAIKNWGVGPGAVRTIAGTMKIHEELEKKLAEFKKVEATLVVQSGFNANQAVIPTITNEEDGILSDELNHASIIDGVRLSKAKRYIWKHKDLNSLEEQLVKAQRDNCRRKLIITDGVFSMDGDIAPLPGIVELAKKYDALVMVDDAHGEGVLGENGRGIADHFNLTEEVDIEIGTLSKAFGVVGGFIAGKKVLIDYLKQQARPFLFSSSLSPAETAAALEATKILYESDDLVKKLWDNAKYFQSKIKEMGYDIGGTETPITPVMIYDEKKTKEFSSKLYEEGIFASSIVYPTVPKGKARIRVMISALHSKEDLDFALSKFEKIGKSLGTL | 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): 43506
Sequence Length: 393
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
Q6LPR3 | MPLSNRRFNHKIKHALEARETQGLYRQRACLSRADQSVYHQGTSLLNFSSNDYLGLAQDPAILSAWQEGLTLFGAGSGASPLVTGFHSAHKALEDQLADWLGYDRALLFNSGFSANQAVLFTIPDKHDVLIQDKLNHASLMEAGLLSPATMRRFAHNDLSALTRLLHQTNDKFPSINPLVITEGVFSMDGDLSPLANISEQCSQHDAWLMVDDAHGCGVLGDKGRGSCDLAGVKADILIVTFGKAFGLSGAAVMCNNDTAEYLIQFARHFIYSTSMPPSQAHALSAACRLIQSDDWRREKLHDLGYLLFENVESSIQLVDTHTPIKPLIIGDSHKALSVSNALKAKGLWVSAIRPPTVPVNSARLRITLTAAHTEQDIKRLATTLNEVINDE | 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): 42875
Sequence Length: 392
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
A1VUJ6 | MLIDYLNHQLREREAQGLTRQRRIAESPCAPRQRVSQRGQPARDLLAFCSNDYLGLANHPALVRALAEGAQLYGAGSGASHLISGHSEAHAALEADLAAWLAPCIPNAQALYFCTGYMANLALLTALGGANATIFADKLNHASLVDGALLAKATLQRYAHKSLAVLARQLAACDTPIKLIVTDAVFSMDGDVADLPELLALAERFDAWLVVDDAHGFGVLGEEGRGSLSHFGLCSERLICMGTLGKAAGVGGAFVAAHPSIIDWLVQTARPYIYTTAAPPAVAHALRESLRLIGGTEGDQRRKQLQQLISQLRSQLAELIAAQPALGWHLADSSTAIQPLIVGSNEAALALAAALDAQGLWVPAIRPPTVPAGTARLRITLSASHSADDVRQLVDALAQAGKDLAGAQP | 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): 43052
Sequence Length: 409
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.3.1.47
|
Q8D1X1 | MKPFFWRIIGSGSVNLVFIHGWGLNSCIWNNIIIILSNYFKLHLVDLPGYGKNILYKEYSFSKITEIIACKSPKKSILIGWSLGGLIATNISIVYPEKFKGLIIVSSSPCFCEKKDWPGIKKEILNNFSFQLKNDFHNTVKKFFNIQFLGTKKNNNEIKKLKNIFFRQKEPSYKTLSSGLKILKNIDIRNYLKYIKIPTLRIYGNLDVIVPVKIIPIIKKLQNFNINKNIIIPSASHAPFLSHPFLFCKIIKYFIKKFN | 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): 30028
Sequence Length: 259
Pathway: Cofactor biosynthesis; biotin biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.1.1.85
|
Q9PDM3 | MYIEVTGYGPALVLIHGWAMHSGVFAPLVEQLRAHHTLYLVDLPGHGYNHTTLTPLALPHVVHAIAAATPPAVWLGWSLGGLFALHAAATLPQVRGLIMLAATPCFVRREDWPHAVEVSIFTQFAEDLKQNYTETINRFLALDTLGSTYAQSELRQLRQILNARHTPNTATLQAGLELLAHTDLRRAVIDLTPPSLWIAGQRDRLVPAASIHAATALAPSGQTELLTITGGGHAPFLSHANQMTAALQHFIATLP | 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): 27627
Sequence Length: 255
Pathway: Cofactor biosynthesis; biotin biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.1.1.85
|
A7FNV8 | MKQLYWYTCGEGDCDLVLLHGWGLNSGVWHCIIDRLAPHFRLHLVDLPGYGRSQDYGAMSLADMAERVAQQAPKQALWLGWSMGGLVASQIALSQPECVRGLITVSSSPCFTARDEWPGIKPEVLAGFQHQLSDDFHRTVERFLALQTLGTESSRQDARLLKSVVLQHQMPDVEVLTGGLAILRTADLRTALAGFTLPFMRVYGHLDSLVPRKVASLLDSAWPQTQSVVMQGAAHAPFISHPNDFAKLILNFAEENKK | 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): 28590
Sequence Length: 258
Pathway: Cofactor biosynthesis; biotin biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.1.1.85
|
Q89VI2 | MIHAISAVNRHLYEDVLEQHFRLRHDIFVEERHWETLRRPDGREVDSYDDEDTVYLLALEGRRVVGGHRLYPTTKPSMMSEVFPHLAAVRGCPSDPLIWEWSRYFVVRDRRDGALNLQLMAAVQEFCLDQGIAQVSAIMETWWLPRFHEAGFVVTPLGLPALVENAWTMAATVDIRRQTLDVLHDRIGMPSIVQQDGPRLDAVARANLCGLAAAQRKSA | Function: Catalyzes the synthesis of IV-HSL (isovaleryl-homoserine lactone), a quorum-sensing (QS) autoinducer molecule which binds to BjaR1 transcriptional regulator to activate expression of QS-dependent genes. Is active with isovaleryl-CoA but cannot use isovaleryl-ACP as acyl donor.
Catalytic Activity: 3-methylbutanoyl-CoA + S-adenosyl-L-methionine = CoA + H(+) + N-isovaleryl-L-homoserine lactone + S-methyl-5'-thioadenosine
Sequence Mass (Da): 25009
Sequence Length: 219
EC: 2.3.1.228
|
P9WIS2 | MGEGSRRPSGMLMSVDLEPVQLVGPDGTPTAERRYHRDLPEETLRWLYEMMVVTRELDTEFVNLQRQGELALYTPCRGQEAAQVGAAACLRKTDWLFPQYRELGVYLVRGIPPGHVGVAWRGTWHGGLQFTTKCCAPMSVPIGTQTLHAVGAAMAAQRLDEDSVTVAFLGDGATSEGDVHEALNFAAVFTTPCVFYVQNNQWAISMPVSRQTAAPSIAHKAIGYGMPGIRVDGNDVLACYAVMAEAAARARAGDGPTLIEAVTYRLGPHTTADDPTRYRSQEEVDRWATLDPIPRYRTYLQDQGLWSQRLEEQVTARAKHVRSELRDAVFDAPDFDVDEVFTTVYAEITPGLQAQREQLRAELARTD | Function: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Mass (Da): 40616
Sequence Length: 367
EC: 1.2.4.4
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P9WIS0 | MTQIADRPARPDETLAVAVSDITQSLTMVQAINRALYDAMAADERVLVFGEDVAVEGGVFRVTEGLADTFGADRCFDTPLAESAIIGIAVGLALRGFVPVPEIQFDGFSYPAFDQVVSHLAKYRTRTRGEVDMPVTVRIPSFGGIGAAEHHSDSTESYWVHTAGLKVVVPSTPGDAYWLLRHAIACPDPVMYLEPKRRYHGRGMVDTSRPEPPIGHAMVRRSGTDVTVVTYGNLVSTALSSADTAEQQHDWSLEVIDLRSLAPLDFDTIAASIQRTGRCVVMHEGPRSLGYGAGLAARIQEEMFYQLEAPVLRACGFDTPYPPARLEKLWLPGPDRLLDCVERVLRQP | Function: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Mass (Da): 38064
Sequence Length: 348
EC: 1.2.4.4
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O06159 | MSGEDSIRSFPVPDLGEGLQEVTVTCWSVAVGDDVEINQTLCSVETAKAEVEIPSPYAGRIVELGGAEGDVLKVGAELVRIDTGPTAVAQPNGEGAVPTLVGYGADTAIETSRRTSRPLAAPVVRKLAKELAVDLAALQRGSGAGGVITRADVLAAARGGVGAGPDVRPVHGVHARMAEKMTLSHKEIPTAKASVEVICAELLRLRDRFVSAAPEITPFALTLRLLVIALKHNVILNSTWVDSGEGPQVHVHRGVHLGFGAATERGLLVPVVTDAQDKNTRELASRVAELITGAREGTLTPAELRGSTFTVSNFGALGVDDGVPVINHPEAAILGLGAIKPRPVVVGGEVVARPTMTLTCVFDHRVVDGAQVAQFMCELRDLIESPETALLDL | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA
Sequence Mass (Da): 41061
Sequence Length: 393
EC: 2.3.1.168
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Q9FMZ0 | METNLQQVKNSSQTFSEKQNPKQEASPSPISSTCSSPSHDFSFTISLQPLSSSSKHISPTLRSPSKTTSSYQQTDPFAVDLSPADEIFFHGHLLPLHLLSHLPVSPRTSTGSYNDGFTLPVKDILPDQPTNNNNNTENAITNISTEAKDDNTEDKAEGEIRVKTKPIKSFSLFGLSKWRKGFESNEREQEQQQQKIKKPMSLDLSHAVKKYIRMLFQKRGNGTQFWNRRQTSSYSFSSSLMGPNGNSKTMINGSYNKRDLIRGRRGELFSAPASMRTSPTNSGHLRVSTAGLSSSSGSTSSSSSDSTMEELQAAIQAAIAHCKNSSAVDRDDKVKDS | Function: Negative regulator of brassinosteroid signaling. When associated to the membrane, limits the interaction of BRI1 with BAK1 by binding to the kinase-inactive form of BRI1.
PTM: Phosphorylated on Tyr-211 in response to brassinosteroid perception, leading to its inactivation: once phosphorylated, displaced into the cytosol where it is inactive.
Sequence Mass (Da): 37104
Sequence Length: 337
Domain: The c-terminal part (253-337) is necessary and sufficient for the interaction with BRI1.
Subcellular Location: Cell membrane
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Q9LFL7 | MGNCLKHFKQQLPSIAPKPLIIPPIFSARKRESESLQIRGLKKATKKFRQDRVVECEDYSVRKFYKGYIDETTFAPSRAGTGIAVSVMECDSSRSLQDWMAVVRSLGQLSHQNLVNFLGYCCEDNKPFFLVFEYSHKGSLDSHIFGKEEEALPWEIRVKIAIGTAQGLAFLHSIKNSPLNRELRMHNIMLDEQYNAKLFYLEPTKRSLVDEGLKRGRFTYLSPEWGSLGILDMTTDVYIFGMILLELLMGSKDRKKIKEEQGLVDYWTSSFLPDNYKIEEIIDPRLGSDYSANAATQMGTLINRCTAHNTKKRPLMQQVLDGLNHIAEIKD | Function: Collaboratively with BKN2/SZE2, involved in compatible pollen-stigma interactions.
Location Topology: Lipid-anchor
Sequence Mass (Da): 37870
Sequence Length: 331
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
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Q9LFL6 | MGNCLKPLKEQPPSASPKPLTIPSSSVEPVKENLKEFRFAELNKATKRFRKYMVIKGNDNGFTRTFYEGCINETTFAPSRTGITVSVMECYQDNSQTLQDWKEEVKSLGRISHPNLVKLLGYCCEENKSFLVFEYLHKGSLNRYIFGKEEEALPWETRVKIAIGAAQSIAFLHWVKNSALYRELRMYNILLDEHYNTKLFYLGSKKLCLLEESVTTAFIGRTVYIPPEYVISGHLGTKSDVYTFGVILLEILTGLKASDGKKNENMQSLHVWTKPFLSDQSKIREIIDPRLGNDYPVNAATQMGKLIKRCIKLDTRKRPSMQQVFDGLNDIAEIKD | Function: Together with SZE1 and ZED1, required for effector-triggered immunity (e.g. Pseudomonas syringae type III effector HopZ1a) via the activation of ZAR1, thus being essential for resistance against P. syringae pv. tomato DC3000 expressing HopZ1a . Collaboratively with BKN1, involved in compatible pollen-stigma interactions .
PTM: N-terminal myristoylation is critical for plasma membrane localization and implication in defense responses.
Location Topology: Lipid-anchor
Sequence Mass (Da): 38399
Sequence Length: 336
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
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Q5U5M8 | MESSQGRRRRPGTVVPGEAAETDSELSASSSEEELYLGPSGPTRGRPTGLRVAGEAAETDSEPEPEPTVVPVDLPPLVVQRDPAETWGTEETPAMAPARSLLQLRLAESQTRLDHDVAAAVSGVYRRAGRDVAALAGRLAAAQATGLAAAHSVRLARGDLCALAERLDIVAGCRLLPDIRGVPGMEPEQDPGPRA | Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking.
PTM: Phosphorylated.
Sequence Mass (Da): 20398
Sequence Length: 195
Subcellular Location: Cytoplasm
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Q94KL5 | MGLATTTSSMSQDYHHHQGIFSFSNGFHRSSSTTHQEEVDESAVVSGAQIPVYETAGMLSEMFAYPGGGGGGSGGEILDQSTKQLLEQQNRHNNNNNSTLHMLLPNHHQGFAFTDENTMQPQQQQHFTWPSSSSDHHQNRDMIGTVHVEGGKGLSLSLSSSLAAAKAEEYRSIYCAAVDGTSSSSNASAHHHQFNQFKNLLLENSSSQHHHHQVVGHFGSSSSSPMAASSSIGGIYTLRNSKYTKPAQELLEEFCSVGRGHFKKNKLSRNNSNPNTTGGGGGGGSSSSAGTANDSPPLSPADRIEHQRRKVKLLSMLEEVDRRYNHYCEQMQMVVNSFDQVMGYGAAVPYTTLAQKAMSRHFRCLKDAVAVQLKRSCELLGDKEAAGAASSGLTKGETPRLRLLEQSLRQQRAFHHMGMMEQEAWRPQRGLPERSVNILRAWLFEHFLNPYPSDADKHLLARQTGLSRNQVSNWFINARVRLWKPMVEEMYQQEAKEREEAEEENENQQQQRRQQQTNNNDTKPNNNENNFTVITAQTPTTMTSTHHENDSSFLSSVAAASHGGSDAFTVATCQQDVSDFHVDGDGVNVIRFGTKQTGDVSLTLGLRHSGNIPDKNTSFSVRDFGDF | Function: Transcription factor that establishes leaf shape by repressing growth in specific subdomains of the leaf. Negatively regulates knox homeobox gene KNAT1/BP expression.
Sequence Mass (Da): 69271
Sequence Length: 627
Domain: The SR/KY and BELL domains are responsive for the interaction between the TALE/BELL proteins and the TALE/KNOX proteins.
Subcellular Location: Nucleus
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Q9SJJ3 | MDMIKPDFQQIRRDKFRVEQMNDFPNTWTQQQHQNIRIPNNLDLIGILQNQISVPVQTDLYQDSAATFMNMPQSIHRDPQGPSNWRISDLSQPSTVNHGYDQAGIRPNNVADLLSDHFSSRNQILDRPLYVGRDSIPQSSMIRRSEVSCLDDNQKGCVTVACSGTGNEILRSSYDQGSSSGSYRGEFSFLPSLENQSVAHNASNWNHGPVNVTATSHTNSKKGFPLSLLSDIPPSRDVGNAAVLSTMNIHGPLGPFTGYASILKSSRFLEPAQKMLEEFCISYASKIISRSESTSMEDDDDDDDNLSGFSSSSEPLEPKNRLKKAKLLFLQEEVCKWYKLYNHQLQTVMSSFNTVAGLNTATPYISLALKRTSRSFKALRTAIAEHVKQISSHSSNGNNNNRFQKRQRSLIGNNVGFESQQQHIWRPQRGLPERAVAVLRAWLFDHFLHPYPTDSDKQMLATQTGLSRNQVSNWFINARVRLWKPMVEEIHTLETKAIKNADTSHNIEPSNRPNTVSSPSHEQTLTGLSGTKRSRLEYMDMVGFNRGNVSLTLELRRGVDNVIQTQTQDHQFGTGSQMFHDFVG | Function: Required for specifying floral primordia and establishing early internode patterning events during inflorescence development.
Sequence Mass (Da): 65775
Sequence Length: 584
Domain: The SR/KY and BELL domains are responsive for the interaction between the TALE/BELL proteins and the TALE/KNOX proteins.
Subcellular Location: Nucleus
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Q9LZM8 | MADAYEPYHVLQQSRRDKLRIPSLDSHFHFHPPPPPSSGGGGGVFPLADSDFLAAGGFHSNNNNNHISNPSYSNFMGFLGGPSSSSSTAVAVAGDHSFNAGLSSGDVLVFKPEPLSLSLSSHPRLAYDLVVPGVVNSGFCRSAGEANAAAVTIASRSSGPLGPFTGYASILKGSRFLKPAQMLLDEFCNVGRGIYTDKVIDDDDSSLLFDPTVENLCGVSDGGGGDNGKKKSKLISMLDEVYKRYKQYYEQLQAVMGSFECVAGLGHAAPYANLALKALSKHFKCLKNAITDQLQFSHNNKIQQQQQCGHPMNSENKTDSLRFGGSDSSRGLCSAGQRHGFPDHHAPVWRPHRGLPERAVTVLRAWLFDHFLHPYPTDTDKLMLAKQTGLSRNQVSNWFINARVRVWKPMVEEIHMLETRQSQRSSSSSWRDERTSTTVFPDNSNNNPSSSSAQQRPNNSSPPRRARNDDVHGTNNNNSYVNSGSGGGSAVGFSYGIGSSNVPVMNSSTNGGVSLTLGLHHQIGLPEPFPMTTAQRFGLDGGSGDGGGGYEGQNRQFGRDFIGGSNHQFLHDFVG | Function: Transcription factor that is involved in the preservation of the spiral phyllotactic arrangement leading to a regular pattern of organ initiation. Required for maintenance of stem cell fate in the shoot apical meristem, and is essential for specifying floral primordia and establishing early internode patterning events during inflorescence development. Acts as transcription repressor of AG expression in floral and inflorescence meristems. Is also responsive of the nuclear import of SHOOT MERISTEMLESS (STM). In the fruit, plays a central role in patterning by negatively regulating SHP expression in order to prevent replum cells from adopting a valve margin cell fate.
Sequence Mass (Da): 62007
Sequence Length: 575
Domain: The SR/KY and BELL domains are responsive for the interaction between the TALE/BELL proteins and the TALE/KNOX proteins.
Subcellular Location: Nucleus
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Q9HNE6 | MGASPVALTPLTARARRTLARPALALGWVAISIAALPAITGVSLSPTARYAPLVASAVVFGMPHGAIDYLALPRAVTGTVTVRWLAVVGVLYLVLGGGYAAAWFFAPVPAAFAFVAITWLHWGQGDLYPLLDFLDVDYLDTRPRRAATVLIRGGLPMLVPLLGFPERYRSVVDAFAAPFGGSVGDLAVFDPRVRLWLGVAFAAATVAVLAAGRRRTHSPGAWRVDAAETLLLWVFFFVVPPVFAVGVYFCVWHSVRHVARAIAVDGSVHPSLRAGDILGPLARFGVEAAPMTAAALALGGVLWWAVPNPPTTLESGAALYLVLIAVLTLPHVAVVTWMDRVQGVL | Function: Appears to partially substitute for Brp function in retinal biosynthesis during bacteriorhodopsin production. Probably catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.
Catalytic Activity: all-trans-beta-carotene + O2 = 2 all-trans-retinal
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36507
Sequence Length: 345
Subcellular Location: Cell membrane
EC: 1.13.11.63
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Q4PNI0 | MGLMLIDWCALALVVFIGLPHGALDAAISFSMISSAKRIARLAGILLIYLLLATAFFLIWYQLPAFSLLIFLLISIIHFGMADFNASPSKLKWPHIIAHGGVVTVWLPLIQKNEVTKLFSILTNGPTPILWDILLIFFLCWSIGVCLHTYETLRSKHYNIAFELIGLIFLAWYAPPLVTFATYFCFIHSRRHFSFVWKQLQHMSSKKMMIGSAIILSCTSWLIGGGIYFFLNSKMIASEAALQTVFIGLAALTVPHMILIDFIFRPHSSRIKIKN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal. Exhibits the highest activity for beta-carotene, followed by beta-cryptoxanthin, beta-apo-4'-carotenal, alpha-carotene, and gamma-carotene in decreasing order, but has no activity on beta-apo-8'-carotenal, beta-apo-12'-carotenal, lutein, zeaxanthin, or lycopene, suggesting that the presence of one unsubstituted beta-ionone ring in a substrate with a molecular weight greater than C35 seems to be essential for enzyme activity.
Catalytic Activity: all-trans-beta-carotene + O2 = 2 all-trans-retinal
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31037
Sequence Length: 275
Subcellular Location: Cell membrane
EC: 1.13.11.63
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Q09457 | MVKSYTLAGLAAIACLLLAIGAVISTVYILNDISDFYSEAQEELVEFKDIANNIWEEMVFELTPEEMREAEDNDREKRSYEPEGPYQSETTTPSTTTSTAATTTEAAEDESGYDFVNDNGPPSSRPRKPEPPTMPRTIQGFRAPPPAATSTYRPPHGSNYDNYGREPASSRRPYPPQQPPSTSAPHSSPNNRTSLYNPQPPPKTGYPTNPRVPYNPPQPNYTRQPTYPEDNRAPYKPTRSPNTPPPRQPSGGYDSDGQTPPSSPRIYNTRRPNNHGPGYPEDQVPTAPPVPGQQRVPPTQTRNPPNPTNTRQPSRPVPPTSDGHIEATTPYNPSAQYPTGKRGSHPGFGPQRPRPGTRPRGNPCDQCSAQPNHCPSGPPGPRGRPGPPGFPGQDGPRGLRGLNGGYSGVQPSSYDPVIGCVQCPIGPPGERGPDGTPGVPGEDGIDGEQGVNGQDGQPGAPGAPGYHGMNGSPGTPGKPGLPGRNGQSCKSIPGPPGQPGVMGVPGRDGDPGTDGEHGQDGSPGIQGPPGRDGTSGPDGQPGVSAPGAPGTDGGYCPCPKRSSKFDFNDAYNDDEKRGLEEHRPRGYDSERAEEPRPRQTVRTNTYDENSGAEHQRRPNYEPSAEVAPPRQDRYEDEERVREPPPKRPPPPHRQTPHELYPEEQPYVRRPPPPQNRGNYEVERSREYVPEAPRPRQGYEHSSGYGGDDRKEQPKYMESRPVDEPRYETDAPSRSRPLKKVEIIRHPERGYDRRQPSYEDSKPRQEEPRRYETEAEPRYEEVPRKETHPPGFGRPKSEENPRETGRTYSEEAMPPVQQTEKYNGDKRKKNQPEYEDISKPEEDKERAMEKHHKKPNKFQEKQWEEHRKSQELRNSREHGGQVPVETSVPMQQVKPESSAEEKPVPPVHDNFQSSEKRAFSNENPLPSEQIPYRRRNRFYRNHYYEKFLV | Function: Probable cuticular collagen-like protein (Probable). Nematode cuticles are composed largely of collagen-like proteins (Probable). The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment (Probable). Acts downstream of the Wnt signaling pathway; perhaps in the formation of the adult cuticle . Required for proper strut formation within the unique medial layer of the adult cuticle (Ref.2).
PTM: May be processed for secretion by bli-4.
Sequence Mass (Da): 105364
Sequence Length: 948
Subcellular Location: Nucleus
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Q5ADQ9 | MDKFIQSFSHQYLDSSSSLKLTARRKRKLTILGLFLFSLISLMIIISYSNNNILPGLSGISISSTFSDYYSNPKQQNKFEQQIQDHQTTKKGKRTIIFPNNFNHVHDHKGSYMMKDSELVKYYVETMEQALDPEDLIYRNRFTYKLPNIPYTEQKIEMFSDGGGGGGDTSDSNTDMCPKLSTTIKVEASPAMNKNGDLKKILKTFLQEDSFYYRELSPFFPDLKKHFDEDTIDKHWYQFIGSTVWLEQYGVHLMVSRIIYTEKDQGSPKFSLAYLQVFDRNWKELDNVELIVPDPENISTTNNKNKNKKPYGYKSVLYPTIAPIPVYHNSKQTGGRFYGIEDPRIVLIKTRHGYEEPVLIYNSHHRKISEKHFDNDQEGKINFNNYRSLFIGWIWQTQLGKIHLEELPNNEFKKNEYIKIKEFVKPNNNRGRTEKNWALFINYNQRLNQGFDSHVYFANQLKNLKILKCSILNDNDDDCEWEFQMDDYEDAGVLHGGTELININQLLHQYDYPELNSIKDLIPNGREYWVGFARASLKNCGCGSRMYRPNLIVLMKDGKNYKFAYVSSFVGLGIEILPWYLDKGLCEHYNLIIPNGISSWTIEKDLHQKEKDKQVMDYMAFTISRRDATVDVVYVKGLLKALFTDSSSSKHLLAVEQTGFKSVTNVDCALKNSEKFCKIYGETF | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for addition of the first beta-mannose residue to acid-stable fraction of cell wall phosphopeptidomannan. Plays a key role in reducing host inflammatory response.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 79603
Sequence Length: 684
Subcellular Location: Membrane
EC: 2.4.1.-
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F2QZ65 | MVDLFQWLKFYSMRRLGQVAITLVLLNLFVFLGYKFTPSTVIGSPSWEPAVVPTVFNESYLDSLQFTDINVDSFLSDTNGRISVTCDSLAYKGLVKTSKKKELDCDMAYIRRKIFSSEEYGVLADLEAQDITEEQRIKKHWFTFYGSSVYLPEHEVHYLVRRVLFSKVGRADTPVISLLVAQLYDKDWNELTPHTLEIVNPATGNVTPQTFPQLIHVPIEWSVDDKWKGTEDPRVFLKPSKTGVSEPIVLFNLQSSLCDGKRGMFVTSPFRSDKVNLLDIEDKERPNSEKNWSPFFLDDVEVSKYSTGYVHFVYSFNPLKVIKCSLDTGACRMIYESPEEGRFGSELRGATPMVKLPVHLSLPKGKEVWVAFPRTRLRDCGCSRTTYRPVLTLFVKEGNKFYTELISSSIDFHIDVLSYDAKGESCSGSISVLIPNGIDSWDVSKKQGGKSDILTLTLSEADRNTVVVHVKGLLDYLLVLNGEGPIHDSHSFKNVLSTNHFKSDTTLLNSVKAAECAIFSSRDYCKKYGETRGEPARYAKQMENERKEKEKKEKEAKEKLEAEKAEMEEAVRKAQEAIAQKEREKEEAEQEKKAQQEAKEKEAEEKAAKEKEAKENEAKKKIIVEKLAKEQEEAEKLEAKKKLYQLQEEERS | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Involved in the beta-mannosylation of outer chains of N-glycans (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74338
Sequence Length: 652
Subcellular Location: Membrane
EC: 2.4.1.-
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Q59MA6 | MLAWLRHRIRSYNTSTYSSILPSASFGKVYKIGTKLNFTLLALCLLLACSVFFNYFYLADNNGLDIDTKGEEEENVFKDRKMVIFPNNFEITDKNLLEYYLKTLEEPLHPQDTIYRNRFIYKVPDVSYTSQTINLFSGLSQNSQSSKCEDLSSSYSFDVSGPQNKNCDLYKVLGKFLNDDSEYFQEISPLFPKLKEMLVKKEIEKHWFQLIGSSVWLEQYGVHLMTSRIFYSSTGDKVKPVVSLTYVQVFDHEWREIENVELIVPDGEGKYKPMTYPTFLPMSVYHNEKQQQGRFYGVEDPRITLVRNKLGYDEPIIVYNSHHRKITDAKSDNDGESNIHFKAYRSIFMAWLWQNQKGKNNVEEIETGKMKNRVYVKSKELIKPNNKREDKEKNWAPFINYQQRLQQGFDSHVYFMYQFQDLKILKCSLLDEEDCVWEYQFNDKNGAGRLRGGTELVNINQLLTTFDHPEIKRVKDLMPQNREIWIGVARAALEKCGCGDKMYRPNIVILIKDGDDQYRLSHVSPFVGLGIPILPWWPDKGLCDGKNLIIPNGISSWHLNKDEDNSVQDYLTLSISRADSTVDLLHIKGLLKSILFDDPNSKLLELNDYGFNNKNIECAVKSSDAFCKKYGSEYKLNNNKEEDKANGNGKGSSS | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for the addition of beta-mannose to the acid-labile fraction of cell wall phosphopeptidomannan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 75813
Sequence Length: 654
Subcellular Location: Membrane
EC: 2.4.1.-
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C4R7X8 | MRTRLNFLLLCIASVLSVIWIGVLLTWNDNNLGGISLNGGKDSAYDDLLSLGSFNDMEVDSYVTNIYDNAPVLGCTDLSYHGLLKVTPKHDLACDLEFIRAQILDIDVYSAIKDLEDKALTVKQKVEKHWFTFYGSSVFLPEHDVHYLVRRVIFSAEGKANSPVTSIIVAQIYDKNWNELNGHFLDILNPNTGKVQHNTFPQVLPIATNFVKGKKFRGAEDPRVVLRKGRFGPDPLVMFNSLTQDNKRRRIFTISPFDQFKTVMYDIKDYEMPRYEKNWVPFFLKDNQEAVHFVYSFNPLRVLKCSLDDGSCDIVFEIPKVDSMSSELRGATPMINLPQAIPMAKDKEIWVSFPRTRIANCGCSRTTYRPMLMLFVREGSNFFVELLSTSLDFGLEVLPYSGNGLPCSADHSVLIPNSIDNWEVVDSNGDDILTLSFSEADKSTSVIHIRGLYNYLSELDGYQGPEAEDEHNFQRILSDLHFDNKTTVNNFIKVQSCALDAAKGYCKEYGLTRGEAERRRRVAEERKKKEKEEEEKKKKKEKEEEEKKRIEEEKKKIEEKERKEKEKEEAERKKLQEMKKKLEEITEKLEKGQRNKEIDPKEKQREEEERKERVRKIAEKQRKEAEKKEAEKKANDKKDLKIRQ | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Initiates the beta-mannosylation of core N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74561
Sequence Length: 644
Subcellular Location: Membrane
EC: 2.4.1.-
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Q9UUH2 | MRPIPVKNRIGKNNIDNAKGLKGNKLIRHYHNLLKEKSRLIASSAPIEKIKNVESELENIGIDAYQRASRSGQAEGKGGDSSKILIKWIRTTPCFSYCARLKEPKDLLEIGSVSVDNKCSTCGLFRVSRIDLHSVHPLIKQQDFLERTPEEGLFTGISCSLVLNFAPPELRAKMLLHCTGLLMPPNKEQPPWLFLVLPSPCITNSRYMDEKTLHSIMIQFGFICRQKSISKKIAYYLYSYECFPMKEIDWKKKIVNDGATRNNFFIPCIL | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Sequence Mass (Da): 30760
Sequence Length: 270
Subcellular Location: Nucleus
EC: 2.1.1.-
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