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Database: UniProt
Entry: A0A0D3H010_9ORYZ
LinkDB: A0A0D3H010_9ORYZ
Original site: A0A0D3H010_9ORYZ 
ID   A0A0D3H010_9ORYZ        Unreviewed;       584 AA.
AC   A0A0D3H010;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
OS   Oryza barthii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART08G13890.1};
RN   [1] {ECO:0000313|EnsemblPlants:OBART08G13890.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART08G13890.1};
RX   DOI=10.1007/s12284-009-9025-z;
RA   Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA   Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA   Knight J., Niazi F., Egholm M., Wing R.A.;
RT   "De novo next generation sequencing of plant genomes.";
RL   Rice 2:35-43(2009).
RN   [2] {ECO:0000313|EnsemblPlants:OBART08G13890.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-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, ECO:0000256|RuleBase:RU003968}.
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DR   AlphaFoldDB; A0A0D3H010; -.
DR   SMR; A0A0D3H010; -.
DR   STRING; 65489.A0A0D3H010; -.
DR   PaxDb; 65489-OBART08G13890-1; -.
DR   EnsemblPlants; OBART08G13890.1; OBART08G13890.1; OBART08G13890.
DR   Gramene; OBART08G13890.1; OBART08G13890.1; OBART08G13890.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_026750_0_0_1; -.
DR   Proteomes; UP000026960; Chromosome 8.
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:SF5; PROTEIN HOTHEAD; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR000137-3};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..584
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002276612"
FT   DOMAIN          122..145
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          283..297
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         78..79
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
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         518..519
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         547
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         558..559
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        453..510
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   584 AA;  64103 MW;  3F260A9DC4145787 CRC64;
     MGLINRGVFF KILAFLCFIR SSQGRNHFTT LDLPPLLKAS SFSRIQHEAY DYIIVGGGTA
     GCPLAATLSQ KYKVLLLERG GSPYGNRNIS HLENFHICLA DDSPNSPSQG FISTDGVINA
     RAKVLGGGTS VNAGFYSRAD PSFVQDAGWD AELVNQSYPW IEERIVYWPN ITPWQAALRD
     GLLEAGVSPY NGYSYDHLFG TKVGGTIFDE AGYRHTAADL LAAGNHNNLR VLLHASVTRI
     IFNTEQEHRK PRTIGVEFKD ENGGQQHAFL TRNRDSEIII SAGAIGSPQL LLLSGIGPRK
     ELKKHNISVV LRNEHVGKGM SDNPMNSIFI PTKDAPKQSL IQTVGITDGG AFIEASSGFS
     QSPDSIQCHH GIMSAEIGQL STIPPKQRNL DAVKKYVHKK YNLPKEVFSG GFILSKIDGP
     LSTGNLVLVD TDINSNPTVT FNYFQHPKDL SRCVYGIKTI ERILKTNHFT NFTLNGGGYP
     MEVVLNMSVT ANINLIPKHT NDSTSMEQFC RDTVVTIWHY HGGCHVGKVV DQQYRVIGVS
     GLRVIDGSTL FRSPGTNPQA TVMMMGRYMG VKILRRRLGR AAGV
//
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