AFVA_ASPFN
ID AFVA_ASPFN Reviewed; 413 AA.
AC B8N8Q9;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=NADPH dehydrogenase afvA {ECO:0000305};
DE EC=1.6.99.1 {ECO:0000250|UniProtKB:P54550};
DE AltName: Full=Aflavarin synthesis protein A {ECO:0000303|PubMed:26209694};
GN Name=afvA {ECO:0000303|PubMed:26209694}; ORFNames=AFLA_108540;
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: NADPH dehydrogenase; part of the gene cluster that mediates
CC the biosynthesis of aflavarin, a bicoumarin that exhibits anti-insectan
CC activity against the fungivorous beetle C.hemipterus (PubMed:26209694,
CC Ref.2). {ECO:0000269|PubMed:26209694, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1;
CC Evidence={ECO:0000250|UniProtKB:P54550};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P54550};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26209694}.
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 NADH:flavin oxidoreductase/NADH oxidase
CC family. NamA subfamily. {ECO:0000305}.
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DR EMBL; EQ963475; EED53478.1; -; Genomic_DNA.
DR RefSeq; XP_002376724.1; XM_002376683.1.
DR AlphaFoldDB; B8N8Q9; -.
DR SMR; B8N8Q9; -.
DR STRING; 5059.CADAFLAP00004589; -.
DR EnsemblFungi; EED53478; EED53478; AFLA_108540.
DR VEuPathDB; FungiDB:AFLA_108540; -.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_2_1_1; -.
DR OMA; RITPGCV; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0018548; F:pentaerythritol trinitrate reductase activity; IEA:UniProtKB-EC.
DR CDD; cd02932; OYE_YqiM_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR044152; YqjM-like.
DR PANTHER; PTHR43303; PTHR43303; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; NADP; Oxidoreductase.
FT CHAIN 1..413
FT /note="NADPH dehydrogenase afvA"
FT /id="PRO_0000436112"
FT BINDING 53..56
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 88
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 211..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 264
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 370..371
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
SQ SEQUENCE 413 AA; 44699 MW; 2BA6C62DDA5444C6 CRC64;
MTQDIIDNIA AEGISYYTPA QVPPAGTQVE GSTKLFSPLT IRGVTFPNRL FLAPLCQYSA
KDGYANDWHL THIGGIVQRG PGLAIMEATA VQKVGRITPQ DLGLYDDGHI EPLKRITEFA
HSQSQKIGIQ LAHAGRKASA VAPWLSGNAM AVKEVGGWPD DIVAPSAIPQ EEGINAVPKV
LTGEDIGVLK KDWAEAAKRA VRANFDAIEI HAAHGYLLHQ FLSPVSNRRT DKYGGSFENR
VRILLEICEE VRAVIPTAMP LLVRISATDW FEFDDNLTKE FPESWTVAQS IRLALLLADR
GVDLVDVSSG GIHAKSAIAI RSGPGYQVHF AQEIKKAVGE KLLISAVGGI KTGALAEEVV
QSGIDAVQAG RWFQQNPGLV RAFANELGVK VRMATQIDWS FEGRGKKAKK SSL
