ID Q0U0S7_PHANO Unreviewed; 486 AA.
AC Q0U0S7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=SNOG_14788 {ECO:0000313|EMBL:EAT77980.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT77980.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445357; EAT77980.2; -; Genomic_DNA.
DR RefSeq; XP_001804967.1; XM_001804915.1.
DR AlphaFoldDB; Q0U0S7; -.
DR STRING; 321614.Q0U0S7; -.
DR EnsemblFungi; SNOT_14788; SNOT_14788; SNOG_14788.
DR GeneID; 5981893; -.
DR KEGG; pno:SNOG_14788; -.
DR VEuPathDB; FungiDB:JI435_147880; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_0_3_1; -.
DR InParanoid; Q0U0S7; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
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:SF138; DEHYDROGENASE PKFF-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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT DOMAIN 189..203
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 417
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 461
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 416..417
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 462..463
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 486 AA; 52668 MW; 2E6B564CBA420573 CRC64;
MGRRFMFLSS ANKLTLQQAD LVGDDAWTFD NTLHYFARGV SYYPGNASLR AANASVPPPA
NNLAFNGTGP LHVSHPNFAQ IFASYIDGAM AESGIPVQQD FASGSLLGRQ YAPLTISYPG
EERSSSRSFL LGAWDSGKSN LVVYPNMLAR KIVFNGTLRA MGVEVEASSY GNTNTFVLNA
TKEVILSAGA FQSPQLLMVS GIGPREQLEA HGIPVLVDRP GVGANMEDHL DITPVFEIAI
ENGVGAIADP SVNAPLIEQY RTNRTGPFTN AGVDYIGWEK LPDMYRSNLS AAALADLARF
PADWPEVEYE VTAASLSGND PSKRFGTIVT VPVTPLSRGY VNITSNSMHD LPLVNPNHLS
HPTDREVAAQ AFKRARSFFD TEAMRPIVIQ EAMPGANVTS DEAILEYIMA SSYQNWHASC
TCRMGQRNDS MAVVDTHAKV IGVEGLRVVD SSSFALLPPG HPQSMVCKFI VFLFCVAGWF
QGKDEC
//
