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Database: UniProt
Entry: A0A0K9PG69_ZOSMR
LinkDB: A0A0K9PG69_ZOSMR
Original site: A0A0K9PG69_ZOSMR 
ID   A0A0K9PG69_ZOSMR        Unreviewed;       249 AA.
AC   A0A0K9PG69;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=caffeoyl-CoA O-methyltransferase {ECO:0000256|ARBA:ARBA00012165};
DE            EC=2.1.1.104 {ECO:0000256|ARBA:ARBA00012165};
GN   ORFNames=ZOSMA_251G00290 {ECO:0000313|EMBL:KMZ67956.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ67956.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMZ67956.1}.
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DR   EMBL; LFYR01000869; KMZ67956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9PG69; -.
DR   STRING; 29655.A0A0K9PG69; -.
DR   OMA; CDITDRW; -.
DR   OrthoDB; 379471at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
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: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   ECO:0000313|EMBL:KMZ67956.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KMZ67956.1}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  28308 MW;  6AD632F6275AD869 CRC64;
     MAPTNDVLVQ QQKESRHQEA GHKSLLQSDD LYQYILETSV YPREPEIMKE LRERTAEHPW
     NIMTTPADEG QFLTMLLKLI NAKNTMEIGV FTGYSLLATA LAIPHDGKII AMDINRENYN
     IGLPMIEKAG VAHKIVFHEG PALPVLDQML EDKEKLGSLD FVFVDADKDN YLNYHEKIIE
     LVKVGGVIGY DNTLWNGSVA VSDDAPMRKY VRYYREFVLR LNKALSADPR IEICQLPVGD
     GITLCRRLF
//
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