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OTAC_ASPNC
ID   OTAC_ASPNC              Reviewed;         509 AA.
AC   A2R6G9;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cytochrome P450 monooxygenase otaC {ECO:0000303|PubMed:27667988};
DE            EC=1.-.-.- {ECO:0000305|PubMed:27667988};
DE   AltName: Full=Ochratoxin biosynthesis cluster protein 3 {ECO:0000303|PubMed:27667988};
DE   AltName: Full=Ochratoxin biosynthesis cluster protein C {ECO:0000303|PubMed:33391201};
GN   Name=otaC {ECO:0000303|PubMed:33391201};
GN   Synonyms=ota3 {ECO:0000303|PubMed:27667988}; ORFNames=An15g07900;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=22341916; DOI=10.1016/j.ijfoodmicro.2012.01.020;
RA   Ferracin L.M., Fier C.B., Vieira M.L., Monteiro-Vitorello C.B.,
RA   Varani A.M., Rossi M.M., Mueller-Santos M., Taniwaki M.H.,
RA   Thie Iamanaka B., Fungaro M.H.;
RT   "Strain-specific polyketide synthase genes of Aspergillus niger.";
RL   Int. J. Food Microbiol. 155:137-145(2012).
RN   [3]
RP   FUNCTION.
RX   PubMed=27667988; DOI=10.3389/fmicb.2016.01412;
RA   Susca A., Proctor R.H., Morelli M., Haidukowski M., Gallo A.,
RA   Logrieco A.F., Moretti A.;
RT   "Variation in fumonisin and ochratoxin production associated with
RT   differences in biosynthetic gene content in Aspergillus niger and A.
RT   welwitschiae isolates from multiple crop and geographic origins.";
RL   Front. Microbiol. 7:1412-1412(2016).
RN   [4]
RP   NOMENCLATURE, AND FUNCTION.
RX   PubMed=33391201; DOI=10.3389/fmicb.2020.581309;
RA   Ferrara M., Gallo A., Perrone G., Magista D., Baker S.E.;
RT   "Comparative genomic analysis of ochratoxin A biosynthetic cluster in
RT   producing fungi: new evidence of a cyclase gene involvement.";
RL   Front. Microbiol. 11:581309-581309(2020).
RN   [5]
RP   INDUCTION.
RX   PubMed=35143724; DOI=10.1021/acs.jafc.1c08160;
RA   Zhang J., Li L., Yang Y., Zhao C., Hu J., Xue X., Gao Q., Wang D.,
RA   Zhuang Z., Zhang Y.;
RT   "Deletion and overexpression of the AnOTAbzip gene, a positive regulator of
RT   ochratoxin A biosynthesis in Aspergillus niger.";
RL   J. Agric. Food Chem. 70:2169-2178(2022).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed
CC       of a chlorinated type I polyketide dihydroisocoumarin moiety linked to
CC       L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic,
CC       genotoxic, neurotoxic, and teratogenic properties (PubMed:27667988).
CC       OtaC catalyzes the oxidation of 7-methylmellein (7-MM) into 7-
CC       carboxymellein (By similarity). The pathway begins with the highly
CC       reducing polyketide synthase otaA that catalyzes the formation of the
CC       isocoumarin group during the initial stages of biosynthesis, starting
CC       from one acetate and 4 malonate units, to originate the characteristic
CC       pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The
CC       newly identified cyclase otaY might be involved in the polyketide
CC       cyclization reaction during the initial steps of the OTA biosynthesis.
CC       7-MM is then oxidized into 7-carboxymellein (also called ochratoxin
CC       beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by
CC       the otaB gene is involved in the linking of phenylalanine to the
CC       dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the
CC       production of ochratoxin B (OTB), which is the non-chlorinated analog
CC       of OTA and which subsequently serves as the substrate of the halogenase
CC       otaD for chlorination activity to form the final molecular structure of
CC       OTA, containing a chlorine atom in the C-5 position of the molecule
CC       (PubMed:27667988, PubMed:33391201) (Probable).
CC       {ECO:0000250|UniProtKB:A0A1R3RGJ7, ECO:0000269|PubMed:27667988,
CC       ECO:0000305|PubMed:27667988, ECO:0000305|PubMed:33391201}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:A0A1R3RGJ7}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by the ochratoxin cluster
CC       transcription factor otaR1, probably via its binding to the conserved
CC       5'-ACGT-3' bZIP binding motifs found in multiple copies (3 to 4) in the
CC       promoters of the OTA biosynthetic genes. {ECO:0000269|PubMed:35143724}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AM270352; CAK42677.1; -; Genomic_DNA.
DR   RefSeq; XP_001397311.1; XM_001397274.1.
DR   AlphaFoldDB; A2R6G9; -.
DR   SMR; A2R6G9; -.
DR   PaxDb; A2R6G9; -.
DR   EnsemblFungi; CAK42677; CAK42677; An15g07900.
DR   GeneID; 4988391; -.
DR   KEGG; ang:ANI_1_1830134; -.
DR   VEuPathDB; FungiDB:An15g07900; -.
DR   HOGENOM; CLU_001570_14_4_1; -.
DR   Proteomes; UP000006706; Chromosome 3R.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:1900818; P:ochratoxin A biosynthetic process; ISS:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="Cytochrome P450 monooxygenase otaC"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000440591"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         447
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   509 AA;  57715 MW;  A91B7E87F76783EF CRC64;
     MSIDTLLYTS LAVGAVYLAS VALYELYWSP LAHIPGPKLA ACTRLYEFFY DVVCGGQYTF
     KIADLHKQYG PIIRISPREI HIHDPNYYET LYATNSPRNK DPWFTAHFGV DESAFSTLDY
     RLHRSRRAMI APFFAKARMD GAQPLIKANL AKLIRHLDAH ASSQSVLKVE VAYNSFTGDV
     ITGYTSYRSF EYLETTDMVP IWSETVRNLV ESGMLSRHLP GFFPLLAWAG SRCIAAVYPK
     LLPVIAFRMK CAQEVNFMWT NSEEGKKEAI QSGCSEPALF PELVSRASSA PDITEERLLH
     EFITIVAAGT ETTAHTMTVC TFHIAHNQSI LDKLREELDN RFHSNADMDL QTLEQLPYLT
     GIIYEGLRLS YGLSHRLQRI SPIDPLKYKD IAIPPNTPVG MSSALMHHDE SIFPQSHEFI
     PERWTDPNDR RRLNKYMVSF SKGSRQCIGM NLAFAELYLG IATLFRRYDM KLHDTTLDDV
     QLHGDKMLPR AKNGSKGVRV TLRRAQSVG
 
 
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