ID E5A2F8_LEPMJ Unreviewed; 626 AA.
AC E5A2F8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 28-JUN-2023, entry version 46.
DE SubName: Full=Similar to choline dehydrogenase {ECO:0000313|EMBL:CBX97593.1};
GN ORFNames=LEMA_P090020.1 {ECO:0000313|EMBL:CBX97593.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929132; CBX97593.1; -; Genomic_DNA.
DR RefSeq; XP_003841072.1; XM_003841024.1.
DR AlphaFoldDB; E5A2F8; -.
DR STRING; 985895.E5A2F8; -.
DR EnsemblFungi; CBX97593; CBX97593; LEMA_P090020.1.
DR GeneID; 13281978; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_1_1; -.
DR InParanoid; E5A2F8; -.
DR OMA; SNAHQCC; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000002668; Genome.
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:SF115; DEHYDROGENASE XPTC-RELATED; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..626
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003194981"
FT DOMAIN 48..353
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 477..615
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 604..605
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 626 AA; 67505 MW; 7F93A0072849D8D3 CRC64;
MRFRNRGHVA MLIRTIILSL VVSFGQAQSH LGRKARSIQA DQLNNATYDF VIAGGGIAGL
TVADRLTENA NVAVLVIEHG PFDQKEDSVM IPGAYFPVPY LWLPLMSTPQ AALGGTSYGV
PCGRVVGGGS VVNAMFFHRS DAELYDSWED LGATGWGWTD LLPYFKKSET FTPPDTSYAA
ERNITWDLSV HGSTGPVQAS YAPYDYPGSA NFYNAAVNLG IRPSQDPNNG RAQGIFRLLR
SVNTKTQTRS SACVNHYDRV GERLNYHILA NTAVSRVIFE GTTALGVTFV SNNNGTVGEV
RAKKEVIIAA GGVHSPQILQ LSGVGDASHL KNLGIEPVSD LPGVGRNLQD HLVLKVNYNY
TSNHVPNGGT LQSNATYATE QRALYDAGHP SAYDLTVTTG NTMIQLPLSN WTSNTSSIMA
RVKANGLGAM LGRNVPSTVL NGYKKQRAII IRDINTVTVG GVSWNTGPET SIYLTRPFSR
GSITINSTSI FDTPLIDYGA LLDWTDLDIL HAIYLKNREL MASSDIAVLG PIETAPAPGL
SDDAEVKEML KKALAPSNAH QCCTVAMMNK EDGGVVDPKN KVYGTEQLSV VDASTWPLIV
GGGPQASVYA WAERAADMIK ERHDLM
//
