ID F9XKL7_ZYMTI Unreviewed; 617 AA.
AC F9XKL7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=MYCGRDRAFT_49038 {ECO:0000313|EMBL:EGP84212.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP84212.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP84212.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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}.
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DR EMBL; CM001205; EGP84212.1; -; Genomic_DNA.
DR RefSeq; XP_003849236.1; XM_003849188.1.
DR AlphaFoldDB; F9XKL7; -.
DR EnsemblFungi; Mycgr3T49038; Mycgr3P49038; Mycgr3G49038.
DR GeneID; 13396586; -.
DR KEGG; ztr:MYCGRDRAFT_49038; -.
DR VEuPathDB; FungiDB:ZTRI_10.35; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_0_1; -.
DR InParanoid; F9XKL7; -.
DR OMA; ECKVENR; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000008062; Chromosome 10.
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; 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; 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:UP000008062}.
FT DOMAIN 287..301
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 617 AA; 66869 MW; 6E925E93FD462B18 CRC64;
MTNTSSDPEA FSSQTYDYLI VGGGTAGLVV AARLTEDSNV TVGVLEAGKN HLDDPLVDTP
AAFKDMMMKE DYDWGFLTEP QKYNSNLNHH IPRGKMLGGS SGSNFLMYVR GSDQDYDDWA
IITGDETWSS ANMKPYMRKH QTLDPIDEAA AFDRSLCPFV GENHGTSGPI HTGFNDTFFP
IEADLIKAFD DVTGMDKRPT DPYFGDHIGF YHTLGSIART GPHKGKRSYA ARTYFEPNAH
RPNLHVLTEA TVHKIELEGT TATGVTFSHG GKIFTAHANG EVIVSCGAIQ SPQILELSGI
GDPDVLKSAG VECKVANPAI GNNLQDHVLS AVGWEMKEGI LTLDSLARPD VIQAAQKQLI
EDQSGPLTCT STTHGFFPYK KFATQAKQDE IIKSIEASMS DATTFQQKQY ARIIAHLRAD
DSANLQVVVV PISCGYEAGV ADQRKLLRAP DSLDALNQVM VIMALQYPVS RGSVHIKTAN
VEDHPALDPG FLSHPADVAV LGAGITMLGR SAQSPHLADK ISRQVKPAPE VDICDPDQAE
AWVRQWILSE YHPCGSVALG DALDTRLRVK GAKNLRVIDA SVFPNHVSGN IQSSVYMVAE
RGADIIKEDR AAAVVQG
//
