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