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Database: UniProt
Entry: D7KBH7_ARALL
LinkDB: D7KBH7_ARALL
Original site: D7KBH7_ARALL 
ID   D7KBH7_ARALL            Unreviewed;       521 AA.
AC   D7KBH7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase family protein {ECO:0000313|EMBL:EFH66301.1};
GN   ORFNames=ARALYDRAFT_334713 {ECO:0000313|EMBL:EFH66301.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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; GL348713; EFH66301.1; -; Genomic_DNA.
DR   RefSeq; XP_002890042.1; XM_002889996.1.
DR   AlphaFoldDB; D7KBH7; -.
DR   STRING; 81972.D7KBH7; -.
DR   EnsemblPlants; fgenesh1_pg.C_scaffold_1001278; fgenesh1_pg.C_scaffold_1001278; fgenesh1_pg.C_scaffold_1001278.
DR   GeneID; 9328856; -.
DR   Gramene; fgenesh1_pg.C_scaffold_1001278; fgenesh1_pg.C_scaffold_1001278; fgenesh1_pg.C_scaffold_1001278.
DR   KEGG; aly:9328856; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_026750_0_0_1; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
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:UP000008694};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..521
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003100769"
FT   DOMAIN          269..283
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         65..66
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         112
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         473
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        397..436
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   521 AA;  57788 MW;  EAFE6D363BF5963F CRC64;
     MSHFVFLFII FMFINLSEGA QMPYMTTDPK EVSGKSFDYI VVGGGTAGCS LAATLSEKYS
     VLVIERGGSP FGDPLVEERR YFGYSLLNTD EYSSVAQSFT SVDGIENYRG RVLGGSSAIN
     GGFYSRASDE FVKKTGWDKD LVQDCYKWVE SKVVFMPELT QWQSVVQFGF LEAGFYPYNG
     YSLEHTQGTK IGGSIYDQCG KRHTSADLLG FGKPNYITVL LNATVQSIIF DANKTRAVGV
     RFMESDENSN KSYKAHVEKH RGEVILTAGA LGSPQILLLS GIGPENHLKD FDIPVIVNLK
     EVGRKMSDNP AISLLVDRFS QNRTLEPPQV AAIAEGYKFI LESAVLPTDI TTTRISIAAK
     IAFPKSKGRL KLNSTNPMEN PAVKFNYLKN KEDLDACQEM VLHLQHVARS ECVTFFLGTQ
     AQDKLVAGDE DLKNFCKQNV RTYYHYHGGC IVGPVVDEAY KVNGVKRLRV IDGSTFEESP
     GTNPMATVLM LGRYQGIKIL KEREEQENMF LSPQGSPQPQ P
//
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