ID E4ZIN7_LEPMJ Unreviewed; 542 AA.
AC E4ZIN7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 28-JUN-2023, entry version 50.
DE SubName: Full=Similar to glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:CBX91058.1};
GN ORFNames=LEMA_P060920.1 {ECO:0000313|EMBL:CBX91058.1};
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; FP929065; CBX91058.1; -; Genomic_DNA.
DR RefSeq; XP_003834423.1; XM_003834375.1.
DR AlphaFoldDB; E4ZIN7; -.
DR STRING; 985895.E4ZIN7; -.
DR EnsemblFungi; CBX91058; CBX91058; LEMA_P060920.1.
DR GeneID; 13284293; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_7_1_1; -.
DR InParanoid; E4ZIN7; -.
DR OMA; NHFESCA; -.
DR OrthoDB; 3714148at2759; -.
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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 264..278
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 542 AA; 59845 MW; 2076F9B90360CD3E CRC64;
MAPTTTTIPK DASYDFVIVG GGTAGCVIAS RLTEYLPNKT VLLIEAGPSD FMDDRVLLLK
DWLNLLGGEL DYDYGTTEQP NGNSHIRHSR AKVLGGCSSH NTLISFRPFE YDCKRWEAQG
CKGWSFKTFM RVLDNLRNTV QPVHAKHRNQ LCLDWVDSCS TAMKIPKVDD FNKEIKEKGA
LKPSVGFFSV SYNPDDGRRS SASVAYIHPI LRGEEKRDNL TVLTNAWVSK VNVSGNKVTG
IDLTLQDGEK RTLNPRCETI LCAGAVDTPR LMMLSGLGPK QQLSDLGIPV VKDLPGVGEN
LLDHPESIIL WELNKPVPAN QTTMDSDAGI FLRREVPNAA GDDGDIADIM MHCYQIPFCL
NTARMGYDSP IDAFCMTPNI PRPRSRGRIF LTSSDPNVKP ALDFRYFTDP EGYDAATIVA
GLKAAREIAK QAPFSSWIKR EVAPGPSITT DEELSEYGRR VAHTVYHPAG TTKMGDVTKD
EYAVVDPELK VRDLKGVRIA DAGVFPEMPT INPMLTVLGI GERAAELIAQ EWGWKGLEKQ
KL
//
