ID A0A0D9WSS6_9ORYZ Unreviewed; 594 AA.
AC A0A0D9WSS6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR06G19400.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR06G19400.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR06G19400.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR06G19400.1}
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; A0A0D9WSS6; -.
DR STRING; 77586.A0A0D9WSS6; -.
DR EnsemblPlants; LPERR06G19400.1; LPERR06G19400.1; LPERR06G19400.
DR EnsemblPlants; LPERR06G19400.2; LPERR06G19400.2; LPERR06G19400.
DR Gramene; LPERR06G19400.1; LPERR06G19400.1; LPERR06G19400.
DR Gramene; LPERR06G19400.2; LPERR06G19400.2; LPERR06G19400.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_026750_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 6.
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:SF2; (R)-MANDELONITRILE LYASE-LIKE; 1.
DR PANTHER; PTHR45968; OSJNBA0019K04.7 PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
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:UP000032180};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..594
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007398251"
FT DOMAIN 306..320
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 520..521
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 549
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 560..561
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 452..512
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 594 AA; 63151 MW; AF29EC32B43F15F0 CRC64;
MAAIPTPLLL LTVLILAPAL AAAQPRGFGG VAAPAPGYAR YVVDAAETAA EDVYDYIVVG
GGTAGCPLAA TLAGPGGGRV LLLERGGAPA EFPPLATAGG FVRTLAMADP APESDAPAQT
FTSEDGVPNV RARVLGGGTS INAGFYSRAH PAWFRGHGEG TEAMNWDMRL VNASYEWVER
ELTFQPVVRG WQAAVRAGLL EANVTPWNGF TMDHVSGTKV GATTFDASGR RRSAADLLAF
ARPGRLRVAT RAMVTRIIMN PIDPAARRGK LPQPAVAAVG VVYQDRLLQQ HHALLRPGGE
VILSAGALGS PQLLLLSGIG PASDLTSQGI PVSADVPDVG KHMFDNPRNS ISIIPSVPID
HSLIQVVGIP STNGTESYLE AASYIVPLAP VLRRTGPFYS PYSPLYVTVV TIMEKVPGPL
SEGSLWLASS NPLESPAVRF NYLSRPEDLA RCVTGMRRVA KVLESSTMDI FRSAAGSVSE
GRRGSARRDF RIVGAALPVD WSTNDTALGD FCQQTVATLW HYHGGCVAGS VVDRDFRVFR
VRSLRVVDGS TFRETPGTNP QATIMMMGRY MGMKMIEERH RRQVITSTDS SSNA
//
