(data stored in SCRATCH zone)

SWISSPROT: CAMT3_ARATH

ID   CAMT3_ARATH             Reviewed;         232 AA.
AC   Q9C5D7; Q8LBF3; Q9STR2;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 120.
DE   RecName: Full=Probable caffeoyl-CoA O-methyltransferase At4g26220;
DE            EC=2.1.1.104;
DE   AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase;
DE            Short=CCoAMT;
DE            Short=CCoAOMT;
GN   OrderedLocusNames=At4g26220; ORFNames=T25K17.30;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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 [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) 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 (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   -!- 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}.
DR   EMBL; AL049171; CAB38951.1; -; Genomic_DNA.
DR   EMBL; AL161564; CAB79477.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85172.1; -; Genomic_DNA.
DR   EMBL; AF360317; AAK26027.1; -; mRNA.
DR   EMBL; AY056313; AAL07162.1; -; mRNA.
DR   EMBL; AY087244; AAM64800.1; -; mRNA.
DR   PIR; T06006; T06006.
DR   RefSeq; NP_567739.1; NM_118755.4.
DR   SMR; Q9C5D7; -.
DR   STRING; 3702.AT4G26220.1; -.
DR   PaxDb; Q9C5D7; -.
DR   EnsemblPlants; AT4G26220.1; AT4G26220.1; AT4G26220.
DR   GeneID; 828728; -.
DR   Gramene; AT4G26220.1; AT4G26220.1; AT4G26220.
DR   KEGG; ath:AT4G26220; -.
DR   Araport; AT4G26220; -.
DR   TAIR; locus:2136799; AT4G26220.
DR   eggNOG; KOG1663; Eukaryota.
DR   eggNOG; COG4122; LUCA.
DR   HOGENOM; HOG000016839; -.
DR   InParanoid; Q9C5D7; -.
DR   KO; K00588; -.
DR   OMA; MGEHPRL; -.
DR   OrthoDB; 1116724at2759; -.
DR   PhylomeDB; Q9C5D7; -.
DR   BioCyc; ARA:AT4G26220-MONOMER; -.
DR   BioCyc; MetaCyc:AT4G26220-MONOMER; -.
DR   UniPathway; UPA00711; -.
DR   PRO; PR:Q9C5D7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9C5D7; baseline and differential.
DR   Genevisible; Q9C5D7; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0042409; F:caffeoyl-CoA O-methyltransferase activity; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR029063; SAM-dependent_MTases.
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;
DR   PRODOM; Q9C5D7.
DR   SWISS-2DPAGE; Q9C5D7.
KW   Lignin biosynthesis; Metal-binding; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..232
FT                   /note="Probable caffeoyl-CoA O-methyltransferase At4g26220"
FT                   /id="PRO_0000165678"
FT   REGION          73..74
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   METAL           149
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   METAL           175
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   METAL           176
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         7
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q40313"
FT   BINDING         49
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         71
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         79
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         97
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         126
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         149
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q40313"
FT   BINDING         151
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   CONFLICT        17
FT                   /note="K -> KVCPYILISTL (in Ref. 1; CAB38951)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   232 AA;  25946 MW;  D004DE1B46B5419F CRC64;
     MAKDEAKGLL KSEELYKYIL ETSVYPREPE VLRELRNITH NHPQAGMATA PDAGQLMGML
     LNLVNARKTI EVGVFTGYSL LLTALTLPED GKVIAIDMNR DSYEIGLPVI KKAGVEHKID
     FKESEALPAL DELLNNKVNE GGFDFAFVDA DKLNYWNYHE RLIRLIKVGG IIVYDNTLWG
     GSVAEPDSST PEWRIEVKKA TLELNKKLSA DQRVQISQAA LGDGITICRR LY
//

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