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Database: UniProt
Entry: J4GR99_9APHY
LinkDB: J4GR99_9APHY
Original site: J4GR99_9APHY 
ID   J4GR99_9APHY            Unreviewed;       327 AA.
AC   J4GR99;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=FIBRA_05578 {ECO:0000313|EMBL:CCM03445.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM03445.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM03445.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM03445.1,
RC   ECO:0000313|Proteomes:UP000006352};
RX   PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA   Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA   Diehl S.V.;
RT   "Short-read sequencing for genomic analysis of the brown rot fungus
RT   Fibroporia radiculosa.";
RL   Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE797114; CCM03445.1; -; Genomic_DNA.
DR   RefSeq; XP_012182728.1; XM_012327338.1.
DR   AlphaFoldDB; J4GR99; -.
DR   STRING; 599839.J4GR99; -.
DR   GeneID; 24098356; -.
DR   HOGENOM; CLU_850024_0_0_1; -.
DR   InParanoid; J4GR99; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000006352; 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   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF00732; GMC_oxred_N; 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};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT   DOMAIN          100..114
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   327 AA;  35322 MW;  DE4443EA552F8320 CRC64;
     MSNVILEASV NLGVSCTNDF NTEEGALGVG PFIGAIDGRN QRAWLYEILK RTQVYRKLCD
     HCISRSRGAQ TTQSDIITEQ ILFTTNSGGV AHKEVIVCAG AVGSPHLLMV SGIGPVAYLA
     EIGVPVVYDS PTVGSNLLDH LSVGAMISRA KPGMTLDFLY RPAFAAWALL QWLMFGSGPM
     SSLLSQIGLF IRSDDERLPF SVPSRGTVPP SADHTSGPNA PDVEVVTCPM AVIESEVVIP
     PANGVTIEPI LLQPESRGTV RLQSTRIWDK PLINPNYLAT EGGRNILKSM RLIIRLARTE
     PLASSLVLQD ANNDFDPYWP SDVNPTQ
//
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