ID E3S3F7_PYRTT Unreviewed; 454 AA.
AC E3S3F7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=PTT_17002 {ECO:0000313|EMBL:EFQ87495.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ87495.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ87495.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL536983; EFQ87495.1; -; Genomic_DNA.
DR RefSeq; XP_003304412.1; XM_003304364.1.
DR AlphaFoldDB; E3S3F7; -.
DR STRING; 861557.E3S3F7; -.
DR EnsemblFungi; EFQ87495; EFQ87495; PTT_17002.
DR KEGG; pte:PTT_17002; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_2_1; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000001067; 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 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 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; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 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:UP000001067}.
FT DOMAIN 261..275
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 238
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 454 AA; 49217 MW; 71FB1C24D9596293 CRC64;
MPAKILDITA GAYDFIVVGA GSASCLIALC LSQQLLNHPV LVLEAGEHIR NDRKVQTPGL
ATSLLSNPTY DWDCSSAPEP GLNEKIVKHP RGKLVGGSSA INSHSVVFPN HEWHDRIADE
LLSGPGREVW SSQGISDCNR RWQAEQSRPS VDEDVGSLDH VQTSFPRTMD LIQSRWMEAF
KELGHSTNPT GFVESSAGAV SVTNAIDVSK GERSHAGTAF LEPALKRGSV TLKTGVKVDR
IAFDEGEAHL ISGREIIPCA GAFESSVILK RSGIGSKDVL AAANVTDPVR ASGVGKNLQD
HINCGMSFET KGDIPTRDDV LRNPQVRQAA LIEYEKSRTG RLSEGVAYSF AFTPLQMLET
AAETQEFTQK VQECVGRETN PNLKAQYALT QKAIESPSEA TATTFMLHLQ RHKYDDSLPN
NTPSVVDGNY ITVVAMPSHP FSRGSCHITP NHQV
//
