ID B9SN35_RICCO Unreviewed; 597 AA.
AC B9SN35;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Glucose-methanol-choline (Gmc) oxidoreductase, putative {ECO:0000313|EMBL:EEF34970.1};
DE EC=4.1.2.10 {ECO:0000313|EMBL:EEF34970.1};
GN ORFNames=RCOM_0312000 {ECO:0000313|EMBL:EEF34970.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ974042; EEF34970.1; -; Genomic_DNA.
DR RefSeq; XP_002527404.1; XM_002527358.2.
DR AlphaFoldDB; B9SN35; -.
DR STRING; 3988.B9SN35; -.
DR GeneID; 8266961; -.
DR KEGG; rcu:8266961; -.
DR eggNOG; KOG1238; Eukaryota.
DR InParanoid; B9SN35; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046593; F:mandelonitrile lyase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:EEF34970.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..597
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002889525"
FT DOMAIN 297..311
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 94..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 253
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 531..532
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 560
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 571..572
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 467..523
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 597 AA; 65143 MW; 2A56C5C0A28901E4 CRC64;
MASFGAVKKN LSLYLLLLLY TLSSSQGNNA AGEPYSYPSH YPFIKKASSF SSSSSSYSSS
GGDSAYDYIV VGGGTAGCPL AATLSQNFSV LLLERGGVPF TNSNVSFLNN FHITLADTSA
TSASQYFIST DGVLNARARV LGGGTSINAG FYTRASTRFI KKVGWDEKLV NESYPWVEKQ
IVHKPKVAPW QVTFRDSLLD VGVSPYNGFT YDHIYGTKFG GTIFDQFGRR HTAAELLASG
NPRLLTVLVH ATVQRVLFDT SRKHPKAVGV VFKDENGNQH QAFLANNPRS EIILSSGAIG
TPQMLLLSGI GPKDELKKMG IPVVLDNEFV GKGMADNPMN TIFVPSKKPV RQSLIQTVGI
TKFGVYIESS SGFGQSKDSI HCHHGMMSAE IGQLSTIPPK KRTLEAIQAY IKRKKDLPHE
AFKGGFILEK LASPISTGQL SLINTNVDDN PSVTFNYFKH PEDLRSCVNG VRMATKIVQS
EHFTNFTQCD KQTMEKILNI SVVANVNLIP KHPNDTKSIE QFCQDTVISI WHYHGGCHVG
KVVSPDHKVL GVDRLRIVDG STFDESPGTN PQATVLMMGR YMGLKILRDR LGKEAGA
//
