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Database: UniProt
Entry: V7CTM9_PHAVU
LinkDB: V7CTM9_PHAVU
Original site: V7CTM9_PHAVU 
ID   V7CTM9_PHAVU            Unreviewed;       230 AA.
AC   V7CTM9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Caffeoyl-CoA O-methyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHAVU_002G305200g {ECO:0000313|EMBL:ESW32241.1};
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:ESW32241.1, 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   -!- FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5-
CC       hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of
CC       feruloylated polysaccharides. Involved in the reinforcement of the
CC       plant cell wall. Also involved in the responding to wounding or
CC       pathogen challenge by the increased formation of cell wall-bound
CC       ferulic acid polymers. {ECO:0000256|ARBA:ARBA00002334}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00023453}.
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DR   EMBL; CM002289; ESW32241.1; -; Genomic_DNA.
DR   RefSeq; XP_007160247.1; XM_007160185.1.
DR   AlphaFoldDB; V7CTM9; -.
DR   STRING; 3885.V7CTM9; -.
DR   EnsemblPlants; ESW32241; ESW32241; PHAVU_002G305200g.
DR   GeneID; 18639612; -.
DR   Gramene; ESW32241; ESW32241; PHAVU_002G305200g.
DR   KEGG; pvu:PHAVU_002G305200g; -.
DR   eggNOG; KOG1663; Eukaryota.
DR   OMA; DRDCYEV; -.
DR   OrthoDB; 379471at2759; -.
DR   Proteomes; UP000000226; Chromosome 2.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002935; SAM_O-MeTrfase.
DR   PANTHER; PTHR10509:SF96; CAFFEOYL-COA O-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10509; O-METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   230 AA;  25726 MW;  04E0F7B169B6E84D CRC64;
     MSSNKTILQS EKLTKYILET SVYPREAETL RDLRNANATH PWGFMGADPD AGQLMALLLK
     LLNAKKTIEV GVFTGYSLLL TALTIPDDGK IIALDPDREA YEIGLPFIKK AGVEHKIDFI
     QSPALPVLDK LLEDDSNKES FDFAFVDADK DNYWNYHERL LKLVKIGGLI IYDNTLWGGT
     VAWPEEDVPL PKRKYRQAAL AFNKAVADDS RVEISAVSIG DGFTICRRAH
//
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