ID B8NJD4_ASPFN Unreviewed; 595 AA.
AC B8NJD4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Pyranose 2-oxidase, putative {ECO:0000313|EMBL:EED49745.1};
GN ORFNames=AFLA_065670 {ECO:0000313|EMBL:EED49745.1};
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:EED49745.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED49745.1, 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};
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).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; EQ963479; EED49745.1; -; Genomic_DNA.
DR RefSeq; XP_002380126.1; XM_002380085.1.
DR AlphaFoldDB; B8NJD4; -.
DR STRING; 332952.B8NJD4; -.
DR EnsemblFungi; EED49745; EED49745; AFLA_065670.
DR VEuPathDB; FungiDB:AFLA_008500; -.
DR eggNOG; ENOG502R261; Eukaryota.
DR HOGENOM; CLU_023699_0_0_1; -.
DR OMA; CCDENSK; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 457..585
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 595 AA; 66711 MW; DDBA42C806F546E4 CRC64;
MVDTEYDALI VGSGPIGATY AKILADAGKV VLMVETGTQE SKIAGEHKKN AINYQKDIDA
FVHVIKVISS RISTFECISL TFDLLLFQGS LHYTSVPTNK AAVPTLAPIS WKANGQIFNG
QNPRQDPNVN LDANVILTWT SWTCATPRQK EKVERSDIFS GDEWDSLYKE AEKLIGTSKT
VLNDSIRQEL VMEILNDEYG KRSAEPLPLA AKKNGSTAYI TWSSSSTILD AMNCKDKFTL
WPEHHCEKFV VEETDNGPQV TKAKIRKLAT DELITVKAKV FIACGGPILT PQLLFNSDFV
PTKPNRDPRT QIPLEDDEEG IAPPPDIPEY LKLPALGRYL TEQSMCFCQI VLKKEWIEAV
ANPKKNPYQS DGVKRKKWEK LKEGWKERVQ KHMKRFNDPI PFPFDDLDPQ VTLPLDYHHP
WHTQIHRDAF SYGAAPPAID KRTIVDLRFF GTVEPDWKNY VTFETDIRDA YGMPQPTFRY
KLNDEDRKRS HQMMKDMEEA AGALGGYLPG SEPQFLAPGL ALHVCGTTRA QKKEKECDPD
PKETSCCDEN SKIWGIHNLY VGGLNVIPGA NGSNPTLTAM CFAIKSAKSI LEGNS
//
