ID L2G9U4_COLFN Unreviewed; 547 AA.
AC L2G9U4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:ELA35409.1};
GN ORFNames=CGGC5_542 {ECO:0000313|EMBL:ELA35409.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA35409.1};
RN [1] {ECO:0000313|EMBL:ELA35409.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA35409.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KB020570; ELA35409.1; -; Genomic_DNA.
DR RefSeq; XP_007275555.1; XM_007275493.1.
DR AlphaFoldDB; L2G9U4; -.
DR STRING; 1213859.L2G9U4; -.
DR EnsemblFungi; ELA35409; ELA35409; CGGC5_542.
DR HOGENOM; CLU_002865_6_3_1; -.
DR OrthoDB; 3714148at2759; -.
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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF123; GMC OXIDOREDUCTASE (AFU_ORTHOLOGUE AFUA_2G01770)-RELATED; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT DOMAIN 254..268
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 490
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 528
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 547 AA; 59374 MW; 5DB7C0112F8529EC CRC64;
MLPTEVWDYV VVGGGLAGTV VSSRLLALNS SAKILVIEAG QSAAGRSDIL YVNSTNLIQG
DFDWNDYSIP QPQLDNRTIQ MAAGKGLGGG GWMRGARVDY DEWAELVNDS RWSYESQLPY
FKRTEDYWTR DVNSEQHGNE GPLKIEVPSV TGRVYPLRDA VLDSYASVGI EALPGLDANG
GSNIGVGEIS ENRRDGVRQI TPEYYSLDGA TVMTGTLVEK VLIDEDDLGN LVATGVRLAN
GTEIRGKQVI AAAGAYRTPQ LLMLSGIGPS DVLQQHGIEQ KVDLPEVGRN FADHPFFIAN
WRLAPEYRNT TVDSGNPLFF KPEYGLGQPN NFVASFNVED KTGLIEAISS EEGKKPDAET
HPLLKNERTL MEAFVLYVNT NPSLPSNYTY LTTANVGLLP TSRGSVTIAS RNPETPPLID
PNFFASEVDR FVWRDSIRRM IRMMIGGEST LSRGIVEAEA PPAELKALTG DSTDEEIEAR
IRAAVIGTYH PMGTCAMGKV VDSDLRVKGV ANLSVVDASV FPTIITAHIQ AAVYVLAEQA
AEIIASS
//
