ID E4ZHP2_LEPMJ Unreviewed; 610 AA.
AC E4ZHP2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 28-JUN-2023, entry version 49.
DE SubName: Full=Similar to alcohol oxidase {ECO:0000313|EMBL:CBX90875.1};
GN ORFNames=LEMA_P059090.1 {ECO:0000313|EMBL:CBX90875.1};
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; CBX90875.1; -; Genomic_DNA.
DR RefSeq; XP_003834240.1; XM_003834192.1.
DR AlphaFoldDB; E4ZHP2; -.
DR STRING; 985895.E4ZHP2; -.
DR EnsemblFungi; CBX90875; CBX90875; LEMA_P059090.1.
DR GeneID; 13292568; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_5_1_1; -.
DR InParanoid; E4ZHP2; -.
DR OMA; IMRRTKM; -.
DR OrthoDB; 2392848at2759; -.
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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 282..296
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 539..540
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 610 AA; 67303 MW; BE7FF3538A6FA044 CRC64;
MGIYNKLADD IDEVDVIIAG GGTAGCIIAG RLAESDPDLS ILVIEGGANN KDVASVVHPV
FYLQNLLPAT KTALFYKGNK AKQLADRECI VPCGGTLGGG SSINFMMYTR AQRSDFDSWN
TPGWSAHEMW PFLNKLETYH GPGEKKHHGQ SGPIHVSDGG FRAKASEDDF IRAAGEIGFP
EIEDLQNLEN NNGFQRWQRY VSPDGKRQDT AHRYVHPKLE DEKHPNLHVL VESKVVRVLF
DENKRASGVE YTPNPEFQME IGLTGHPVRS VKARKLVVFT CGACGTPPVL ERSGVGEKKI
LERAGVPVVE DLPGVGKDYQ DHHLLLYPYK TSLAPEDTID GVLSGRKDVP KMLETKDKML
GWNSIDVSAK LRPSEKDIDA LGPEFRAAWD RDFKNEANRP LMLCGLISCF LGDPTTVPAG
QYVTTGTYTA YPYSRGHMHI TGAKHDDPLD FDVGFFNDKN DIDLKKQIWA YKMQREIMRR
TKFYRGELAA GHPKFPEGSA AAIAETIDAP LENIKDIEYT KEDDAAIEQW LRENVNTTWH
SLGTCKMAPR EDYGVVDRSL NVYGVKGLKI ADLSIPPQNV GANTNNTALV IGEKAADIII
AELRGGAGTP
//
