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Database: UniProt
Entry: B8NYH6_ASPFN
LinkDB: B8NYH6_ASPFN
Original site: B8NYH6_ASPFN 
ID   B8NYH6_ASPFN            Unreviewed;       582 AA.
AC   B8NYH6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=GMC oxidoreductase, putative {ECO:0000313|EMBL:EED45262.1};
GN   ORFNames=AFLA_011460 {ECO:0000313|EMBL:EED45262.1}, G4B84_011599
GN   {ECO:0000313|EMBL:QMW36070.1};
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:EED45262.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED45262.1, 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:EED45262.1};
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:QMW36070.1, ECO:0000313|Proteomes:UP000515286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW36070.1,
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,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; EQ963486; EED45262.1; -; Genomic_DNA.
DR   EMBL; CP059873; QMW36070.1; -; Genomic_DNA.
DR   RefSeq; XP_002385391.1; XM_002385350.1.
DR   AlphaFoldDB; B8NYH6; -.
DR   EnsemblFungi; EED45262; EED45262; AFLA_011460.
DR   VEuPathDB; FungiDB:AFLA_013437; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_7_2_1; -.
DR   OMA; NYPWIHI; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   Proteomes; UP000515286; Chromosome 8.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          265..279
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        510
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        554
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   582 AA;  64474 MW;  FB68F51DF9E0AE23 CRC64;
     MGSTSEDVYD YIICGGGTAG CVVAGRLAEN PDVKVLVLEA GQHNKDLENV HMTGGWSNNF
     DSETDWNIVT TPMKGVDNRQ VKLSRGRFLG GCSGCNGTLC VRGSKQDYDD WELEGWSGEE
     FFAAMRKSET FHPKDWFQAD PQSHGYNGPL HTEPHDLAPI SNLLIDSLVS QGMPLHHDMF
     STGDVAHGCG HAPRTVHKGI RATAADFITK DYNRSNVTIQ TDTTVDRIVL EEGAAGLRAT
     GVLTRLADGT TRTFHARKEV VVSSGAYCSP AVLMRSGIGA REELDKFDIP CKVDLPGVGK
     NLMDHLIVFM FYETEKEGLT TDWHVYHDDN MEKTYAQWKE HKTGFLSTFP FGAFAFARLD
     ERLKDEPLWR DAPREPGRDP MGLTPQQPNI EFFTTECYGG PKQYDQFPVD HKHAFSMIAE
     LFAPKSRGTV TLKSKDPLEN PIVDCNYLAD PMDLLVLTEA CRFGNEVVMK GTGTKDIVKG
     SWPPNLTHHT YTTREEWIPY VKEHATTCYH ASGTCAMGKD DNPLAVLDNK LRVKGVAGLR
     VADCSVMPTL HGGHTQMPAY GIGERCADFI KETWSGQSIA RL
//
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