ID V2WW65_MONRO Unreviewed; 614 AA.
AC V2WW65;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Gmc oxidoreductase {ECO:0000313|EMBL:ESK84776.1};
GN ORFNames=Moror_547 {ECO:0000313|EMBL:ESK84776.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK84776.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK84776.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK84776.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK84776.1}.
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DR EMBL; AWSO01001227; ESK84776.1; -; Genomic_DNA.
DR RefSeq; XP_007855909.1; XM_007857718.1.
DR AlphaFoldDB; V2WW65; -.
DR KEGG; mrr:Moror_547; -.
DR HOGENOM; CLU_002865_6_0_1; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000017559; 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 InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 92..115
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 285..299
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 23..24
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 614 AA; 67177 MW; A94B496CB9CACD12 CRC64;
MPIVQIGYFV STKLDCLVIG GGTSGLVVAT RLSEDPTVTV GVIEAGANHA GDPSVDIPGN
MTKNARNPKY DWEFYTEPQV YAHNRKIQSS RGKGLGGSSG LNNLAFVRPV SEELDAFEKL
GNPGWNWNNV LGFMKKSEHL CVPPLSEGEK KSYAVDPDPA YHGTDGPIAV SFPPYVSPIH
NKILDSLETL GLPRNNEPNA GRNVGSYLVS TSVDPVTATR SYAASAYLHP HLTRNNLFVL
TEAFATKIHF DGANNGLKRA VAVDFIKEGQ SYQVKVAKEI ILSAGTFQTP QILETSGIGD
PRILEPLGIQ CIIKLPGVGE NLQDHMKAPT VVQVQQDLQT PELLRNPDEL NIQQELYKEK
KGILAGMLSS CFAFLPGNLI ADSEHVKAWK NLANVESSAP EVFAKTHPDV LRGIKKQYKI
LEQWIDDPVH PLAQLLNING HFPVVGLTPD NSKRYMTLIV AYTHPFSRGS VHITSADAQV
RPAIQPNYLS NRADLEILSK AIEFTLQLYQ TSPLRDLIVA PVAPPFFKPD DEEKVHEFAR
EILSTVHHPI ATASMMPRED GGVVDHNLLV YGTSNLRVVD CSIIPLQISC NIVPLAYAIG
EKGADIIKRH NSVV
//
