ID G7XE76_ASPKW Unreviewed; 479 AA.
AC G7XE76;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Glucose-methanol-choline (Gmc) oxidoreductase {ECO:0000313|EMBL:GAA85321.1};
GN ORFNames=AKAW_03435 {ECO:0000313|EMBL:GAA85321.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA85321.1};
RN [1] {ECO:0000313|EMBL:GAA85321.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA85321.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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; DF126453; GAA85321.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XE76; -.
DR STRING; 1033177.G7XE76; -.
DR VEuPathDB; FungiDB:AKAW_03435; -.
DR eggNOG; KOG1238; Eukaryota.
DR InParanoid; G7XE76; -.
DR Proteomes; UP000006812; 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; 3.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 3.
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; 3.
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 215..229
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 479 AA; 51385 MW; FA010A91528D22A4 CRC64;
MMASTLPHKT DYLIIGVLIL ESGPDCTADP RVKDPSAWRS LCGSELDWQL KTVPQAGLNG
REEEQTAGKM LGGSSALNGS AWVPPSQAVQ VTYPALEEGT PTEPLINAWN EALKDQGYDF
TSNILGGPKT IGTRAYTAAT DPDSHSRSST STYAQEKRSN LRIITGATVR KIPFNPELER
SDRPNPRAVA TGVEAELDAQ IVSISTEKDV ILAAGAFHTP KILELSGVGQ KDRLTELGIP
VVMDLPGVGE NVQNHVWSIS PTPLKVEGVQ PGIKTLAFTH LDKDEQGNLI SDDPNDQTSD
RVIKSILRNP DNASACLALS AMPGGVALLV AISSFPFSRG SCHCSSANID AKPTVDPQFF
ANELDIETMA RHVQNLYKLS NAPTFQDIIQ PLEVPQLETI KSTLRGGSAL ATHHSCGTAA
MLPREAGGVV NENLRVYGTK NVRVVDASVF IPHANPMSTV YAVAEKAVDM MNEPDVSEY
//