ID E3RUX3_PYRTT Unreviewed; 603 AA.
AC E3RUX3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=PTT_12916 {ECO:0000313|EMBL:EFQ90472.1};
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:EFQ90472.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ90472.1,
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; GL535184; EFQ90472.1; -; Genomic_DNA.
DR RefSeq; XP_003301428.1; XM_003301380.1.
DR AlphaFoldDB; E3RUX3; -.
DR EnsemblFungi; EFQ90472; EFQ90472; PTT_12916.
DR KEGG; pte:PTT_12916; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_0_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 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:UP000001067};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..603
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003181550"
FT DOMAIN 284..298
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 538
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 581
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 603 AA; 65528 MW; CF96E0104A72A3A3 CRC64;
MKFLVLTWAA SGLLGHTCAA IVGHEQRQSA NSSAYDFIIV GGGTAGLAVA SRISLGLPDL
SILIIEAGPD GRQEPGITVP GRKGSTLGGK YDWNFTTVAQ PNANNRVFSQ NRGKVLGGSS
ALNLMTWDRT SAYELDAWEH ILGNEGWNWK NLYAAMLKVE TFLPSPAYGT EGVGKTGPIR
TLINRIFPKH QDTWYPTMNS LGLVTNLESL NGNPIGVSTQ PSNVSPNYTR SYAPEYLKLA
HQNVYLKVET RVAKINFKGM TATGVTLEDG TTITARREVI ISAGSFQTPG LLELSGIGNA
TLLQKLGIPV IKHLPSVGEN LQDHIRIQTS YQLKPEYPSF DVLKNATRAA AELALYNADR
VSLYDYTASG YAYFPWSIVS NATFSKLQNL VLNDKTLTST TDRLKLSYFS PTLSTMVPQL
EVIFSDGYTG LKGYPIANSS QFGIGTFALI GVVQHPLSKG YVHITSRNIS DKPLINPNYL
SNPYDLQAAT NLAKFLRKIA SSKPMSDVWT KEYEPGSSVQ TDEDWKKYAL ANTLSIYHPV
GSAALLPEKD GGVVDTKLKV YGTKGLRVVD ASVIPLLPSA HLQTLVYGIA ELAAEMIISE
HKG
//
