ID B8NR38_ASPFN Unreviewed; 433 AA.
AC B8NR38;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=FAD dependent oxidoreductase, putative {ECO:0000313|EMBL:EED47781.1};
GN ORFNames=AFLA_004220 {ECO:0000313|EMBL:EED47781.1}, G4B84_007053
GN {ECO:0000313|EMBL:QMW31672.1};
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 {ECO:0000313|EMBL:EED47781.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED47781.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED47781.1};
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] {ECO:0000313|EMBL:QMW31672.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW31672.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; EQ963482; EED47781.1; -; Genomic_DNA.
DR EMBL; CP059869; QMW31672.1; -; Genomic_DNA.
DR RefSeq; XP_002382623.1; XM_002382582.1.
DR AlphaFoldDB; B8NR38; -.
DR STRING; 332952.B8NR38; -.
DR EnsemblFungi; EED47781; EED47781; AFLA_004220.
DR VEuPathDB; FungiDB:AFLA_011755; -.
DR eggNOG; KOG2820; Eukaryota.
DR HOGENOM; CLU_007884_0_1_1; -.
DR OMA; HTEYEHR; -.
DR OrthoDB; 1952715at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 4.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR PANTHER; PTHR10961:SF45; L-PIPECOLATE OXIDASE; 1.
DR PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 6..382
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 288..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 48145 MW; 13942E171C02D682 CRC64;
MDKNSRIVIV GAGVFGLSTA AKLASEGYKY VTVVDRHMPP VPDGSSSDIS RVIRFDYADE
DYLNIAYEAY QKWSQLPKYQ GIFFKAPFIL TGNTTVHGRA WIEKTTAALT KKQLPWAKLD
SAAAAKSRYP ILSGTLATPN FTGYYNEQAG WADANKAVSQ LRDDCLELGV SFICGRAGTV
ISLDTDSQKK IKAVRTLAGT SIEGDHFILA SGAWTSGLVD MYNSTLATAQ VIGYTPLTDA
EVKKYKDVPI YANFNTGWFN FPSHDDTKTL KMAVHGWGYT RAPTAEDHQS VKTNISSPPL
IPPRQRVNFT PPDGEDRLRT GLREILPELA DRPFERVALC WYTDTPSGDF IMDSHPDYKN
LFIAGGGSGH AFKFLPVLGD YTFLAFTKRL PEHLAKKWRF RTEYKDDKDT FLGDGSRGGP
ARRELHARER AKL
//
