ID V2YQQ7_MONRO Unreviewed; 603 AA.
AC V2YQQ7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative gmc oxidoreductase {ECO:0000313|EMBL:ESK94009.1};
GN ORFNames=Moror_12903 {ECO:0000313|EMBL:ESK94009.1};
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:ESK94009.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK94009.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94009.1,
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}.
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:ESK94009.1}.
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DR EMBL; AWSO01000158; ESK94009.1; -; Genomic_DNA.
DR RefSeq; XP_007846703.1; XM_007848512.1.
DR AlphaFoldDB; V2YQQ7; -.
DR STRING; 1381753.V2YQQ7; -.
DR KEGG; mrr:Moror_12903; -.
DR HOGENOM; CLU_002865_7_2_1; -.
DR OrthoDB; 3714148at2759; -.
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: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; 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, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 292..306
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 536
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 579
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 251
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 603 AA; 66645 MW; 9996B5B61BFE9A02 CRC64;
MPNYVTNHSA VGVPSSSPTD TESNTYDVII AGGGTSGCAL AARLSENPNL NVLLLEAGGS
GRSLSFSRIP SAFSKLLFQA KHVFQFYTEP QPNALDRKKF WPRAKMLGGC SSINAQMAQY
GAPGDFDEWA KIIGDDTWAW KNFKSSFTKF ERYTGDSEYP EVDTSLKGSH GPVQVGYFSY
LSETTKDFIK SCINLRVPFS PDFNTMGSSK GVNRVMTYIS EKCERVSSET AYLLDDVLAR
PNLKVVIHAS VTRILFEKQG DEMHAVGVEF ARDSTSIVYR AHARKEVVLC GGAIHSPQLL
LVSGVGPAEE LKKHGITIIH DLPGVGANLT DHPVVDFYFK DKSKMAPKYF LPQGPWEIVL
MLYYALVYMF TGKGPLGTNW GEAAAFCRSD DPVVFPADDF PRRKLIKDST SAPDSPDLEI
FITTLAYKNH GSWAWNLHAF SIHCCLLRPL SRGTVTLRSA SPWDHPIMDP RYLESQDDVE
KLVRGGRFCL KVARTEPIAS RIDHTDYGEG LDGQTHLKTD DELEEIVRDR VETLYHPTST
CRMAPLADKG VVDSRLRVYG IKSLRVCDAS IYPTIVSGHT AGAALAVGER GADIIKEDWN
SVD
//
