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AFVE_ASPFN
ID   AFVE_ASPFN              Reviewed;         471 AA.
AC   B8N8R3;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Cytochrome P450 monooxygenase afvE {ECO:0000303|PubMed:26209694};
DE            EC=1.-.-.- {ECO:0000305|PubMed:26209694};
DE   AltName: Full=Aflavarin synthesis protein E {ECO:0000303|PubMed:26209694};
GN   Name=afvE {ECO:0000303|PubMed:26209694}; ORFNames=AFLA_108580;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   FUNCTION.
RX   DOI=10.1021/np50086a008;
RA   TePaske M.R., Gloer J.B., Wicklow D.T., Dowd P.F.;
RT   "Aflavarin and beta-aflatrem: new anti-insectan metabolites from the
RT   sclerotia of Aspergillus flavus.";
RL   J. Nat. Prod. 55:1080-1086(1992).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26209694; DOI=10.1128/ec.00092-15;
RA   Cary J.W., Han Z., Yin Y., Lohmar J.M., Shantappa S., Harris-Coward P.Y.,
RA   Mack B., Ehrlich K.C., Wei Q., Arroyo-Manzanares N., Uka V., Vanhaecke L.,
RA   Bhatnagar D., Yu J., Nierman W.C., Johns M.A., Sorensen D., Shen H.,
RA   De Saeger S., Diana Di Mavungu J., Calvo A.M.;
RT   "Transcriptome analysis of Aspergillus flavus reveals veA-dependent
RT   regulation of secondary metabolite gene clusters, including the novel
RT   aflavarin cluster.";
RL   Eukaryot. Cell 14:983-997(2015).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of aflavarin, a bicoumarin that exhibits
CC       anti-insectan activity against the fungivorous beetle C.hemipterus
CC       (Ref.2, PubMed:26209694). {ECO:0000269|PubMed:26209694,
CC       ECO:0000269|Ref.2}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26209694}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is induced by the developmental and secondary
CC       metabolism regulator veA (PubMed:26209694).
CC       {ECO:0000269|PubMed:26209694}.
CC   -!- DISRUPTION PHENOTYPE: Fails to produce aflavarin (PubMed:26209694).
CC       {ECO:0000269|PubMed:26209694}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; EQ963475; EED53482.1; -; Genomic_DNA.
DR   RefSeq; XP_002376728.1; XM_002376687.1.
DR   AlphaFoldDB; B8N8R3; -.
DR   SMR; B8N8R3; -.
DR   EnsemblFungi; EED53482; EED53482; AFLA_108580.
DR   VEuPathDB; FungiDB:AFLA_108580; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_022195_8_0_1; -.
DR   OMA; QTHINAI; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..471
FT                   /note="Cytochrome P450 monooxygenase afvE"
FT                   /id="PRO_0000436123"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         410
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"
SQ   SEQUENCE   471 AA;  53670 MW;  E6D051B46A2EBAE9 CRC64;
     MSACLRWWSR KFDCEKEYAE AYKQYSKTGK PYATRLKNND HGIVLPLNST KEWRTLPHDQ
     LSFLHALSEF ADLYMHINMT DRTPLQAVHY CNNTKTLSRF NRLMVDATDR ALPLIVGKDT
     ESEWKRANAF HTILSLCSTV AMSVLLGPEF SMDTSLIQTI MMYNTAIMPS CAKRTSYPRI
     LRPFVWRLSP LCRAMKSDLT KTKIKLTPEI KHRIDIARSK KGWLEEGPMS LLDGLIETAF
     EKGCLSRSSD RGDDDQQVAL LAEEIIFYHF ELSTPVAFFI IFAVYVIMNN KEYSTPLREE
     ISEALKLSGG SFTLDTLNHA PKLASFVKET CRFFRRVMKP IHLESINLSL KPGTIIMAPG
     RDVHLDPDYY DNPTTFNGYR FYDASRGTCT PHISTTSPTF LTFSHGISAC PARVLATQIT
     RTIFIMFLLK FDVELAHEEM PAYGFANGPA YLPNPSVMMR VRPCQKDVLG V
 
 
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