ID A0A428QA73_9HYPO Unreviewed; 580 AA.
AC A0A428QA73;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN ORFNames=CEP53_004857 {ECO:0000313|EMBL:RSL62138.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL62138.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL62138.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL62138.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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, ECO:0000256|RuleBase:RU003968}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSL62138.1}.
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DR EMBL; NKCJ01000083; RSL62138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428QA73; -.
DR STRING; 1325737.A0A428QA73; -.
DR Proteomes; UP000287544; Unassembled WGS sequence.
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; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000287544}.
FT DOMAIN 91..114
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 580 AA; 63862 MW; 6AA5C53543AA2A74 CRC64;
MAVISEAPKA FDFIVVGGGT AGCVVAGRLA ENPNVSVLIV EAGIDNPSAV DAITTPATAF
TLRGSTYDWS FKTGMIDRPE YTRIEKPNTR GKVLGGSSCL NYYTWIPGSA ATFDDWAEFG
GEEWTWKSCK EYLYKPATYH DDRGEHRPEL KYIGESGPLP VSHSDLLPET EAWRNALTKA
WVSKGEPLTD DVHNGEMHGL WKCINTIYNG KRSSSWRFLE GKPNVTVLGQ TNAKQLIFED
GKAVGVEVIG PDGQTLSLRA QYEVIVSLGV YETSKLLLLS GIGPEQELNK FGINSVVKSE
HVGQNLLDHP ILPHVFKIKD GYGLDKHLLQ PGLEKDAAAS AYRWKNKGPM TSGLLELVGL
PRIDSYLEKV PEYVEYKKAN GNVDPFGPGG QPHFEIDFVP MFCDAFQWHI PIPPTGDYMT
VIVDLLRPLS RNGTVTLKST DPLEQADINI NFFSNDLDLA AMRQGVRFVD DILLNGEGMK
DIIEEDYPWA MPRGSDEAMD VMIKERSQTG FHPCGTARLG KSIEQGVVDS KLKVFGASNL
RVIDASIIPV IPDCRIQNSV YMIAEKGADI IKAAYPGLYA
//
