TSM1_ARATH
ID TSM1_ARATH Reviewed; 233 AA.
AC Q9C9W4; Q0V808; Q8L5T6;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Tapetum-specific methyltransferase 1;
DE Short=AtTSM1;
DE EC=2.1.1.-;
DE AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase;
DE Short=CCoAMT;
DE Short=CCoAOMT;
GN Name=TSM1; OrderedLocusNames=At1g67990; ORFNames=T23K23.16;
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18557837; DOI=10.1111/j.1365-313x.2008.03576.x;
RA Fellenberg C., Milkowski C., Hause B., Lange P.R., Boettcher C.,
RA Schmidt J., Vogt T.;
RT "Tapetum-specific location of a cation-dependent O-methyltransferase in
RT Arabidopsis thaliana.";
RL Plant J. 56:132-145(2008).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19077165; DOI=10.1111/j.1365-313x.2008.03773.x;
RA Grienenberger E., Besseau S., Geoffroy P., Debayle D., Heintz D.,
RA Lapierre C., Pollet B., Heitz T., Legrand M.;
RT "A BAHD acyltransferase is expressed in the tapetum of Arabidopsis anthers
RT and is involved in the synthesis of hydroxycinnamoyl spermidines.";
RL Plant J. 58:246-259(2009).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19762055; DOI=10.1016/j.phytochem.2009.08.010;
RA Fellenberg C., Boettcher C., Vogt T.;
RT "Phenylpropanoid polyamine conjugate biosynthesis in Arabidopsis thaliana
RT flower buds.";
RL Phytochemistry 70:1392-1400(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RX PubMed=20869941; DOI=10.1016/j.ab.2010.09.029;
RA Wirsing L., Naumann K., Vogt T.;
RT "Arabidopsis methyltransferase fingerprints by affinity-based protein
RT profiling.";
RL Anal. Biochem. 408:220-225(2011).
CC -!- FUNCTION: Methyltransferase involved in phenylpropanoid polyamine
CC conjugate biosynthesis. In vivo, methylates only one of the 5-
CC hydroxyferuloyl moieties of N1,N5,N10-tri-(hydroxyferuloyl)-spermidine,
CC while is able in vitro to convert all three 5-hydroxyferuloyl residues
CC to the corresponding sinapoyl moieties and to methylate caffeoyl CoA
CC and tricaffeoyl spermidine. {ECO:0000269|PubMed:18557837,
CC ECO:0000269|PubMed:19077165, ECO:0000269|PubMed:19762055}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=73.3 uM for caffeic acid (for the recombinant enzyme)
CC {ECO:0000269|PubMed:18557837};
CC KM=15.5 uM for quercetin (for the recombinant enzyme)
CC {ECO:0000269|PubMed:18557837};
CC KM=13.5 uM for caffeoyl CoA (for the recombinant enzyme)
CC {ECO:0000269|PubMed:18557837};
CC KM=19.6 uM for caffeoyl glucose (for the recombinant enzyme)
CC {ECO:0000269|PubMed:18557837};
CC KM=14.6 uM for chlorogenic acid (for the recombinant enzyme)
CC {ECO:0000269|PubMed:18557837};
CC Note=kcat is 0.0029 sec(-1) with caffeic acid as substrate. kcat is
CC 0.0025 sec(-1) with quercetin as substrate. kcat is 0.0141 sec(-1)
CC with caffeoyl CoA as substrate. kcat is 0.0239 sec(-1) with caffeoyl
CC glucose as substrate. kcat is 0.0301 sec(-1) with chlorogenic acid as
CC substrate. {ECO:0000269|PubMed:18557837};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences and flower buds. Not
CC detected in roots, leaves or stems. Located exclusively in the tapetum
CC of developing stamen. {ECO:0000269|PubMed:18557837,
CC ECO:0000269|PubMed:19762055}.
CC -!- DEVELOPMENTAL STAGE: Expressed only in early stages of flower
CC development. {ECO:0000269|PubMed:20869941}.
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=AAG52012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012563; AAG52012.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34733.1; -; Genomic_DNA.
DR EMBL; BT026412; ABH04519.1; -; mRNA.
DR EMBL; AY088274; AAM65814.1; -; mRNA.
DR PIR; H96702; H96702.
DR RefSeq; NP_564917.1; NM_105469.2.
DR AlphaFoldDB; Q9C9W4; -.
DR SMR; Q9C9W4; -.
DR STRING; 3702.AT1G67990.1; -.
DR PaxDb; Q9C9W4; -.
DR PRIDE; Q9C9W4; -.
DR EnsemblPlants; AT1G67990.1; AT1G67990.1; AT1G67990.
DR GeneID; 843127; -.
DR Gramene; AT1G67990.1; AT1G67990.1; AT1G67990.
DR KEGG; ath:AT1G67990; -.
DR Araport; AT1G67990; -.
DR TAIR; locus:2200256; AT1G67990.
DR eggNOG; KOG1663; Eukaryota.
DR HOGENOM; CLU_067676_5_0_1; -.
DR InParanoid; Q9C9W4; -.
DR OMA; NYANAYE; -.
DR OrthoDB; 1116724at2759; -.
DR PhylomeDB; Q9C9W4; -.
DR BioCyc; ARA:AT1G67990-MON; -.
DR BioCyc; MetaCyc:AT1G67990-MON; -.
DR UniPathway; UPA00711; -.
DR PRO; PR:Q9C9W4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9W4; baseline and differential.
DR Genevisible; Q9C9W4; AT.
DR GO; GO:0080076; F:caffeoyl CoA:S-adenosyl-L-methionine O-methyltransferase activity; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0080078; F:tricaffeoyl spermidine:S-adenosyl-L-methionine O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0080012; F:trihydroxyferuloyl spermidine O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0080077; F:trihydroxyferuloyl spermidine:S-adenosyl-L-methionine O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0080088; P:spermidine hydroxycinnamate conjugate biosynthetic process; IDA:TAIR.
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 1: Evidence at protein level;
KW Lignin biosynthesis; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..233
FT /note="Tapetum-specific methyltransferase 1"
FT /id="PRO_0000165677"
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 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ SEQUENCE 233 AA; 26350 MW; 24C1D44F91B9168D CRC64;
MDGRLPDKGI LKSEALKQYI METTAYPREH ELLKELREAT IQRYGNLSEM GVPVDESLFL
SMLVKIINAK NTIEIGVFTG YSLFTVALAL PEDGRITAID IDQAGYNLGL EFMKKAGVDH
KINFIQSDAV RGLDQLLNGE KQEYDFAFVD ADKTNYVYFL EKLLKLVKVG GIIAFDNTLW
FGTLIQKENE VPGHMRAYRE ALLEFNKILA RDPRVEIAQI SIGDGLTLCR RLI
