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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//