ID L8WEG9_THACA Unreviewed; 495 AA.
AC L8WEG9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=GMC oxidoreductase domain-containing protein {ECO:0000313|EMBL:ELU36330.1};
GN ORFNames=AG1IA_09639 {ECO:0000313|EMBL:ELU36330.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU36330.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU36330.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
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}.
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:ELU36330.1}.
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DR EMBL; AFRT01003672; ELU36330.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WEG9; -.
DR STRING; 983506.L8WEG9; -.
DR HOGENOM; CLU_551165_0_0_1; -.
DR OMA; DADESWC; -.
DR Proteomes; UP000011668; 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; 3.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
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 SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668}.
FT DOMAIN 368..485
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 330..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 54436 MW; E70EE4E8436B27B1 CRC64;
MGLPEGRVTS ISSLLGTSSA DSDAMDLYIR DSDADESWCP FRAEYLGMDD HSSELTTSSS
TETLRLTQRG PERMTSVLEM DSTYLLRREG AIIKLNMGRA TRSGVGTMPL FRKLHPSSFG
FPCWVSQLIR PRTFATRLFF CNPELLVEPV CAADTYESAA HRPNLVALTS AQAARIEFDH
SAKNVAAKGV SFHFKGTSFT AKARKEVVLS TGELIMRCGG VFKANKRLSG TLLTPQPLEL
SGIGNSDVLK KHQITPKVDL PGVGEDYQDH ILVSTTYEVK QGFVTYDNLG YNDTFRAATE
LWQDRAYAQV IVGGREEGEA YFASEGAVKG PRAVAEEEDG QRRNHSASRQ VHDSALCQES
LATAIRHHPL LPPAIDPNYL SKQVVKFADK IAKAEPLATM LVGRQDPSAD IKSDEDITNW
IKDNIHTLHH PIGTAATMHK SVGGAVDEKL KVYETSNLRV VDASVIPMHL ATHMQRTMYG
IAEKAAHIII SDWGF
//
