ID A0A199VD85_ANACO Unreviewed; 461 AA.
AC A0A199VD85;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=caffeoyl-CoA O-methyltransferase {ECO:0000256|ARBA:ARBA00012165};
DE EC=2.1.1.104 {ECO:0000256|ARBA:ARBA00012165};
GN ORFNames=ACMD2_02911 {ECO:0000313|EMBL:OAY75059.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY75059.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY75059.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY75059.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(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:OAY75059.1}.
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DR EMBL; LSRQ01002221; OAY75059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A199VD85; -.
DR STRING; 4615.A0A199VD85; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
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; 2.
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; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR PROSITE; PS51682; SAM_OMT_I; 2.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OAY75059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092600};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAY75059.1}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50425 MW; 995BC1FCA2FBEE15 CRC64;
MATSTNGEDE QKGGGGSSSS SSTIHAKTLL KSESLYHYIL ETSVDPREPE CLRELRRISA
AHPRNIMTSA PDEVQFFGML LKILNAKNTI ELGVFTGYSL LATALALPHD GKILALDTNR
ESYELGLPVI HKAGVAHKID FREGPALPVL DQLLADEKNK GTLDFAFVDA DKSNYLNYHE
RLVELVRVGG VIAYDNTLWE GTVAAPPDAP LSERDRMISE IMRAFNSVIA ADPRVEISHL
SIADGYILET SVDPREPECL RELRRISAAH PRGVMASAPD EVQFLGMLLK ILNAKNTIEV
GVFTGYSLLA TALALPHDGK ILALDTNRES YELGLPVIHK AGVAHKIDFR EGPALPLLDQ
LLANEKNKGT LDFAFVDADK TNYLNYHERL VELVRVGGVI AYDNTLWGGT VAAPPDAPLS
ERDRMLSEMT RAFNSTVAAD PRVEISHLSI ADGLTLCRRL G
//
