ID E3RSS6_PYRTT Unreviewed; 618 AA.
AC E3RSS6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=PTT_12014 {ECO:0000313|EMBL:EFQ91220.1};
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:EFQ91220.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ91220.1,
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|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; GL534903; EFQ91220.1; -; Genomic_DNA.
DR RefSeq; XP_003300681.1; XM_003300633.1.
DR AlphaFoldDB; E3RSS6; -.
DR EnsemblFungi; EFQ91220; EFQ91220; PTT_12014.
DR KEGG; pte:PTT_12014; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_1_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:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..618
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003181512"
FT DOMAIN 111..134
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 301..315
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 555
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 598
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 618 AA; 67162 MW; D7389AC2EE22520D CRC64;
MISTTNLAIL ALLGTARALP RNVERVETRA SDDTWDYVII GGGVTGLIVA NRLTENPKTN
VLVIEAGAAY DNPNIRMPYG TNLALNETLL WPYISEPEPA IANQTFPSRV ARVLGGGSIV
NGMMYDRGAA ADFDAWEALG NKGWGWEEMY PFFKKSTEFI PPSAEIAKQF GITWDPKAYG
NGPLKIGISD FQYPDVKDYF AAFKGAGVYA ARSGDTGDAY GTSWYANTMN LLTGERSHAR
NSYYDPVSKR SNLKVLLETL ATEIVFESGK ELTAKGVKIT DRKTGALSAV YAKKELILAA
GAVNTPQLLQ LSGIGPKSVL QAAGIPVKLE HDGVGANFQD HPYTRMHFNI SNMSTPNPSS
FKDPAFNASA WEQYRVNKTG PLTQARGNSL AFVPLQQVDP ERYSSLADQV RSSKNDAYLP
PIYKNSNKLL KGFKAQRKVL ADLYENTKAG VVEYKVPGSG DSQLVGLEKP VSRGTITINP
ADPQGPPKIF YNSLSNPIDR AVLGSCVRFI RKVWARPELS KFSLVETSPG AQYTTDDDIL
QKSVELGTIA PTLSHPSCSC AMMPEDQGGC VSDKLLFYGV KKMSIIDASI IPLVPSQHLQ
STMYAIGEKA ATIINSRG
//
