ID   A0A0E0M9Y7_ORYPU        Unreviewed;       584 AA.
AC   A0A0E0M9Y7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC10G14760.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC10G14760.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC10G14760.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0M9Y7; -.
DR   STRING; 4537.A0A0E0M9Y7; -.
DR   EnsemblPlants; OPUNC10G14760.1; OPUNC10G14760.1; OPUNC10G14760.
DR   Gramene; OPUNC10G14760.1; OPUNC10G14760.1; OPUNC10G14760.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_026750_0_0_1; -.
DR   OMA; PSMMNHE; -.
DR   Proteomes; UP000026962; Chromosome 10.
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; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; PTHR45968; OSJNBA0019K04.7 PROTEIN; 1.
DR   PANTHER; PTHR45968:SF6; PROTEIN, PUTATIVE, EXPRESSED-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   Disulfide bond {ECO:0000256|PIRSR:PIRSR000137-3};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..584
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002367585"
FT   DOMAIN          283..297
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         124
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         237
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         522..523
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         562..563
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        459..514
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   584 AA;  63539 MW;  03187B77F07C77EA CRC64;
     MARLGRASSA APVLAAVVVL VSLCLAALSE QEQLENLRFV RHAQDAPLVS SYNYIVIGGG
     TAGCPLAATL SEHSRVLLLE RGGLPYANMS SEQHFTDALA DTSPASPAQR FISEDGVVNA
     RARVLGGGSC LNAGFYTRAS NEYVRAAGWD ARLVNSSYRW VERSLVFRPD VPPWQAALRD
     ALLEVGVTPD NGFTFDHVTG TKIGGTIFDN SGQRHTAADF LRHARPRGLT VLLYATVSRI
     LFKSQDGVPY PVAYGVVFSD PLGVQHRVYL RDGDKNEVIV SAGTLGSPQL LMLSGVGPQA
     HLEAHGIEVI VDQPMVGQGV ADNPMNSVFI PSPVPVELSL VQVVGITRSG SFIEGVSGSE
     FGMPVSDGAL RWARSFGMFS PQTGQLGTLP PKQRTPEALQ RAAEAMMRLD RRAFRGGFIL
     EKILGPVSSG HIELRTTDPR ANPSVTFNYF HEAEDLERCV HGIETIERVI QSRAFSNFTY
     ANASVESIFT DSANFPVNLL PRHVNDSRSP EQYCMDTVMT IWHYHGGCHV GAVVDDDYRV
     FGVQGLRVID SSTFKYSPGT NPQATVMMLG RYMGVKIQSE RWKK
//