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Database: UniProt
Entry: V7CHC6_PHAVU
LinkDB: V7CHC6_PHAVU
Original site: V7CHC6_PHAVU 
ID   V7CHC6_PHAVU            Unreviewed;       542 AA.
AC   V7CHC6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=PHAVU_002G084200g {ECO:0000313|EMBL:ESW29607.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW29607.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CM002289; ESW29607.1; -; Genomic_DNA.
DR   RefSeq; XP_007157613.1; XM_007157551.1.
DR   AlphaFoldDB; V7CHC6; -.
DR   STRING; 3885.V7CHC6; -.
DR   EnsemblPlants; ESW29607; ESW29607; PHAVU_002G084200g.
DR   GeneID; 18637342; -.
DR   Gramene; ESW29607; ESW29607; PHAVU_002G084200g.
DR   KEGG; pvu:PHAVU_002G084200g; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   OMA; TDPDPNM; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000000226; Chromosome 2.
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:SF19; GLUCOSE-METHANOL-CHOLINE (GMC) OXIDOREDUCTASE FAMILY PROTEIN; 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:UP000000226};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..542
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004757775"
FT   DOMAIN          295..309
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         128
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         242
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         499
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        423..462
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   542 AA;  59799 MW;  329AE8DF0EA315E7 CRC64;
     MELPQINLVH KLLIAFVLFF LASLVLSVPL EPPGNIRQWH MTSDVKEVAG KSYDYIIVGG
     GTCGCALAAT LSEKFSVLLV ERGGSPYGNP LVIDRRYYGI PLLETDKYIS VAQSFTSQDG
     VDNVRGRVLG GSSAINGGFY SRASEEYVCK AGWDKKLVKE AYEWVESKVV FPPFYLSPWQ
     SVAEFSILEA GVLPYNGFSL EHIKGTKISG SVFDEFGKRH TSADLLNAGN PENLTVLINS
     TVKSIIFRHN SYRNETRAKG ISFMQSNGTL DETHEAYIKK VQNSSSRGDV ILAAGALGSP
     QLLLLSGIGP KEQLRRFNIT LVRDMQGVGK EMQDNPCIAV LVDSKPQNRL PDPPQIAGIT
     DDYKIIVEAS ILPLSSNSSR VNVAAKIAMP TSKGVLHLNN TDPRLNPSVR FNYLTSENDM
     QECVKMTKLL ERIARSKSIA FFLGESRQEK LTSADVDLRN FCKKNVRTIY HYHGGCTVGS
     VVDEHYKVYG IKGLRVLDGS TFSDSPGTNP MATLLMLGRY QGLRMLSERN AVSDYNVKDK
     TK
//
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