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Database: UniProt
Entry: B5JQG7_9BACT
LinkDB: B5JQG7_9BACT
Original site: B5JQG7_9BACT 
ID   B5JQG7_9BACT            Unreviewed;       487 AA.
AC   B5JQG7;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=GMC oxidoreductase family {ECO:0000313|EMBL:EDY83788.1};
GN   ORFNames=VDG1235_3415 {ECO:0000313|EMBL:EDY83788.1};
OS   Verrucomicrobiae bacterium DG1235.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX   NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY83788.1, ECO:0000313|Proteomes:UP000003839};
RN   [1] {ECO:0000313|EMBL:EDY83788.1, ECO:0000313|Proteomes:UP000003839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG1235 {ECO:0000313|EMBL:EDY83788.1,
RC   ECO:0000313|Proteomes:UP000003839};
RA   Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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; DS990592; EDY83788.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5JQG7; -.
DR   STRING; 382464.VDG1235_3415; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_008878_4_1_0; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000003839; 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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
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   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000003839}.
FT   DOMAIN          11..295
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          420..476
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   487 AA;  53760 MW;  33FAA6FBE1FBBB97 CRC64;
     MISKASPYVI VGGGLAGLAL ASELVKSGRR CLVVEAGGSA PVEDWRDLTW FDAERDKLEL
     DTTHEYNDKL ARVKALGGSC EAWEAYTPRW NRSDFKQNSS WGVGRDWPFG FEELETYYLR
     SERLMGVAGG KLGCRDEERS APFPLPAFSW TRYEEEIARR SASLGVFWHD YPQARNSRPY
     GGRGHCNGIG VCNACPIQAR WTPRAGLLPQ LQASELFELS CDTVCEGFVC SGSGRVDAVV
     LKRGDSETVR VDCEQVVLAA GAIECSRLLL LSRRNGVGEG AFQNPAIGKG FMDHPILRVC
     ADLSWDPGVS RQTNMLASSH SFRDFEVTSG AWGFMLNLNR RILPRLCLSA HLEMPAVEEH
     RVELSDKLVD RFGNPVAKLR IGNRYEGYSE SEERAYREME RIAREVGGKS VSKVPLQLWA
     CHPMGGCRIS KGESEGVVDP NLRVWAMQNM YVLSNGVFPS GAAVNPSLTL MALALRLGDH
     LKGGAYA
//
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