CAMT1_ARATH
ID CAMT1_ARATH Reviewed; 232 AA.
AC Q9C9W3; Q39166;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative caffeoyl-CoA O-methyltransferase At1g67980;
DE EC=2.1.1.104;
DE AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase;
DE Short=CCoAMT;
DE Short=CCoAOMT;
GN OrderedLocusNames=At1g67980; ORFNames=T23K23.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-232.
RC STRAIN=cv. Columbia;
RA Zou J., Taylor D.C.;
RT "Isolation of an Arabidopsis thaliana cDNA homologous to parsley
RT (Petroselinum crispum) S-adenosyl-L-methionine: trans-caffeoyl-coenzyme A
RT 3-O-methyltransferase, an enzyme involved in disease resistance.";
RL Plant Physiol. Biochem. 32:423-427(1994).
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q40313};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:Q40313};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C9W3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01019}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62426.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC012563; AAG52015.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34731.1; -; Genomic_DNA.
DR EMBL; L40031; AAA62426.1; ALT_INIT; mRNA.
DR PIR; G96702; G96702.
DR RefSeq; NP_564916.2; NM_105468.3. [Q9C9W3-1]
DR AlphaFoldDB; Q9C9W3; -.
DR SMR; Q9C9W3; -.
DR STRING; 3702.AT1G67980.1; -.
DR PaxDb; Q9C9W3; -.
DR PRIDE; Q9C9W3; -.
DR ProteomicsDB; 239186; -. [Q9C9W3-1]
DR EnsemblPlants; AT1G67980.1; AT1G67980.1; AT1G67980. [Q9C9W3-1]
DR GeneID; 843126; -.
DR Gramene; AT1G67980.1; AT1G67980.1; AT1G67980. [Q9C9W3-1]
DR KEGG; ath:AT1G67980; -.
DR Araport; AT1G67980; -.
DR TAIR; locus:2200271; AT1G67980.
DR eggNOG; KOG1663; Eukaryota.
DR HOGENOM; CLU_067676_5_0_1; -.
DR InParanoid; Q9C9W3; -.
DR OMA; FPREHEQ; -.
DR PhylomeDB; Q9C9W3; -.
DR BioCyc; ARA:AT1G67980-MON; -.
DR UniPathway; UPA00711; -.
DR PRO; PR:Q9C9W3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9W3; baseline and differential.
DR Genevisible; Q9C9W3; AT.
DR GO; GO:0005829; C:cytosol; TAS:TAIR.
DR GO; GO:0042409; F:caffeoyl-CoA O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009809; P:lignin biosynthetic process; ISS:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Lignin biosynthesis; Metal-binding;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..232
FT /note="Putative caffeoyl-CoA O-methyltransferase At1g67980"
FT /id="PRO_0000165676"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 76..77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 176
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT CONFLICT 146..147
FT /note="AF -> GL (in Ref. 3; AAA62426)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="K -> M (in Ref. 3; AAA62426)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> T (in Ref. 3; AAA62426)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="V -> L (in Ref. 3; AAA62426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 26114 MW; 13A52BF26B6F2849 CRC64;
MANEIPTKGI LKSEALKQYI METSAYPREH ELLKELRKAT VQKYGNLSEM EVPVDEGHFL
SMLVKIMNAK NTIEIGVFTG YSLLTTALAL PEDGRITAID IDKEAYEVGL EFIKKAGVDH
KINFIHSDGL KALDQLVNDK CEFDFAFADA DKSSYVNFHE RLLKLVKVGG IIAFDNTLWF
GFVAEDEDGV PEHMREYRAA LIEFNKKLAL DPRVEVSQIS IGDGITLCRR LV
