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Database: UniProt
Entry: I1JE08_SOYBN
LinkDB: I1JE08_SOYBN
Original site: I1JE08_SOYBN 
ID   I1JE08_SOYBN            Unreviewed;       249 AA.
AC   I1JE08;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=caffeoyl-CoA O-methyltransferase {ECO:0000256|ARBA:ARBA00012165};
DE            EC=2.1.1.104 {ECO:0000256|ARBA:ARBA00012165};
GN   Name=100811247 {ECO:0000313|EnsemblPlants:KRH70667};
GN   ORFNames=GLYMA_02G103500 {ECO:0000313|EMBL:KRH70667.1};
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:KRH70667.1};
RN   [1] {ECO:0000313|EMBL:KRH70667.1, ECO:0000313|EnsemblPlants:KRH70667}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH70667};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH70667.1};
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:KRH70667}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH70667};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH70667.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH70667.1};
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   -!- 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA
CC         + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104;
CC         Evidence={ECO:0000256|ARBA:ARBA00000581};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004928}.
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; CM000835; KRH70667.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1JE08; -.
DR   EnsemblPlants; KRH70667; KRH70667; GLYMA_02G103500.
DR   Gramene; KRH70667; KRH70667; GLYMA_02G103500.
DR   HOGENOM; CLU_1117346_0_0_1; -.
DR   Proteomes; UP000008827; Chromosome 2.
DR   ExpressionAtlas; I1JE08; baseline and differential.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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:SF81; CAFFEOYL-COA O-METHYLTRANSFERASE 1; 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:UP000008827};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   249 AA;  28197 MW;  B6F83B63177C149C CRC64;
     MPKPCCSMHK HYYKTNLANP GPDANRSNQT SHRFEPAFSF LISITLLHPP TSSSSNYQLF
     QKGEEKERKQ NAQRIIIAMA EQNQNQTTEA GRHQEVGHKS LLQSDALYQY ILETSVYPRE
     PESMKELREL TAKHPWNIMT TSADEGQFLN MLLKLINAKN TMEIGVYTGY SLLATALALP
     EDGKILAMDI NRENYELGLP VIKKAGVDHK IEFREGPALP VLDEMVKDVS FSISQCPNGK
     RKIFLMSQI
//
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