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Database: UniProt
Entry: K7L7M3_SOYBN
LinkDB: K7L7M3_SOYBN
Original site: K7L7M3_SOYBN 
ID   K7L7M3_SOYBN            Unreviewed;       591 AA.
AC   K7L7M3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   Name=100779461 {ECO:0000313|EnsemblPlants:KRH44146};
GN   ORFNames=GLYMA_08G193100 {ECO:0000313|EMBL:KRH44147.1};
OS   Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH44147.1};
RN   [1] {ECO:0000313|EMBL:KRH44147.1, ECO:0000313|EnsemblPlants:KRH44146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH44146};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH44147.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH44146}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH44146};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH44147.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH44147.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CM000841; KRH44146.1; -; Genomic_DNA.
DR   EMBL; CM000841; KRH44147.1; -; Genomic_DNA.
DR   RefSeq; XP_003531615.1; XM_003531567.3.
DR   AlphaFoldDB; K7L7M3; -.
DR   SMR; K7L7M3; -.
DR   STRING; 3847.K7L7M3; -.
DR   PaxDb; 3847-GLYMA08G20600-2; -.
DR   EnsemblPlants; KRH44146; KRH44146; GLYMA_08G193100.
DR   EnsemblPlants; KRH44147; KRH44147; GLYMA_08G193100.
DR   GeneID; 100779461; -.
DR   Gramene; KRH44146; KRH44146; GLYMA_08G193100.
DR   Gramene; KRH44147; KRH44147; GLYMA_08G193100.
DR   KEGG; gmx:100779461; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_026750_0_0_1; -.
DR   InParanoid; K7L7M3; -.
DR   OMA; IEQRQCL; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000008827; 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; 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:UP000008827};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..591
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014581032"
FT   DOMAIN          291..305
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         88..89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         134
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         247
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         525..526
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         554
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         565..566
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        461..517
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   591 AA;  65416 MW;  4CBD75FD8E141D7E CRC64;
     MASFGAVNYK FFLCLLLWLW NFLPLSQGNQ HWHENRYPFI RNASSFSSPS ISTTTSNNAY
     DYIIVGGGTA GCPLAATLSQ NFSVLVLERG GVPFTNPNVS FLENFHITLA DISPTSASQY
     FISTDGVYNS RARVLGGGSS INAGFYTRAN PRFIKKVGWD AKLVNESYPW VEKQIVHRPK
     FSPYQRAFRD SLLDSGVSPF NGFTYDHLYG TKVGGTIFDR FGRRHTAAEL LASGNHDKLT
     VLVCATVQKI VFDRKGKRPK AVGVIFQDEH GKQHEAILSN DKHSEVIMSS GAIGTPQLLM
     LSGIGPKAEL QKLSIPVVLD NHFVGKGMVD NPMNTMFVPS NRPVNQSLIE TVGITKMGVY
     IEASSGFSQS NDSIHCHHGI MSAEIGQLST IPPKERSPEA VQEFIKNKKD IPVELFKGGF
     ILSKVANPWS VGELRLNNTN VNDNPVVTFN YFSHPYDLHR CVKGIRLAIK VVQSKHFTNY
     TLCDKKTTEE LLNLTVKANV NFIPKHPNDT ASIAQFCKDT VITIWHYHGG CHVGKVVSPD
     YKVLGVDRLR VVDGSTFDES PGTNPQATVM MMGRYMGLKI LRHRLGKLAG I
//
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