SAMT_CLABR
ID SAMT_CLABR Reviewed; 359 AA.
AC Q9SPV4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Salicylate carboxymethyltransferase;
DE EC=2.1.1.274 {ECO:0000269|PubMed:12897246};
DE AltName: Full=S-adenosyl-L-methionine:salicylate acid carboxylmethyltransferase;
DE Short=CbSAMT;
DE AltName: Full=Salicylate O-methyltransferase;
GN Name=SAMT;
OS Clarkia breweri (Fairy fans) (Eucharidium breweri).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX NCBI_TaxID=36903;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10375393; DOI=10.1006/abbi.1999.1255;
RA Ross J.R., Nam K.H., D'Auria J.C., Pichersky E.;
RT "S-Adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an
RT enzyme involved in floral scent production and plant defense, represents a
RT new class of plant methyltransferases.";
RL Arch. Biochem. Biophys. 367:9-16(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND SALICYLIC ACID, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-147; MET-150;
RP ILE-225 AND PHE-347.
RX PubMed=12897246; DOI=10.1105/tpc.014548;
RA Zubieta C., Ross J.R., Koscheski P., Yang Y., Pichersky E., Noel J.P.;
RT "Structural basis for substrate recognition in the salicylic acid carboxyl
RT methyltransferase family.";
RL Plant Cell 15:1704-1716(2003).
CC -!- FUNCTION: Catalyzes the methylation of the free carboxyl end of the
CC plant hormone salicylic acid (SA). Converts SA to SA methyl ester
CC (MSA). The volatile compound MSA is hypothesized to act as an airborne
CC signal that triggers defense responses in uninfected plants. MSA is an
CC important chemoattractant for moth pollinated flowering plants.
CC {ECO:0000269|PubMed:12897246}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + salicylate = methyl salicylate + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:36095, ChEBI:CHEBI:30762,
CC ChEBI:CHEBI:31832, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.274; Evidence={ECO:0000269|PubMed:12897246};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for salicylate {ECO:0000269|PubMed:12897246};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. SABATH
CC family. {ECO:0000305}.
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DR EMBL; AF133053; AAF00108.1; -; mRNA.
DR PDB; 1M6E; X-ray; 3.00 A; X=1-359.
DR PDBsum; 1M6E; -.
DR AlphaFoldDB; Q9SPV4; -.
DR SMR; Q9SPV4; -.
DR KEGG; ag:AAF00108; -.
DR BRENDA; 2.1.1.273; 1437.
DR BRENDA; 2.1.1.274; 1437.
DR SABIO-RK; Q9SPV4; -.
DR EvolutionaryTrace; Q9SPV4; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..359
FT /note="Salicylate carboxymethyltransferase"
FT /id="PRO_0000406604"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12897246,
FT ECO:0007744|PDB:1M6E"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 21..25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12897246,
FT ECO:0007744|PDB:1M6E"
FT BINDING 59..61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12897246,
FT ECO:0007744|PDB:1M6E"
FT BINDING 59..60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 96..99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12897246,
FT ECO:0007744|PDB:1M6E"
FT BINDING 129..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12897246,
FT ECO:0007744|PDB:1M6E"
FT BINDING 146..148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 147..151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12897246,
FT ECO:0007744|PDB:1M6E"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12897246,
FT ECO:0007744|PDB:1M6E"
FT MUTAGEN 147
FT /note="Y->S: Decreases activity 2-fold and switch in
FT specificity for jasmonic acid as substrate; when associated
FT with H-150; Q-225 and Y-347."
FT /evidence="ECO:0000269|PubMed:12897246"
FT MUTAGEN 150
FT /note="M->H: Decreases activity 2-fold and switch in
FT specificity for jasmonic acid as substrate; when associated
FT with S-147; Q-225 and Y-347."
FT /evidence="ECO:0000269|PubMed:12897246"
FT MUTAGEN 225
FT /note="I->Q: Decreases activity 2-fold and switch in
FT specificity for jasmonic acid as substrate; when associated
FT with S-147; H-150 and Y-347."
FT /evidence="ECO:0000269|PubMed:12897246"
FT MUTAGEN 347
FT /note="F->Y: Decreases activity 2-fold and switch in
FT specificity for jasmonic acid as substrate; when associated
FT with S-147; H-150 and Q-225."
FT /evidence="ECO:0000269|PubMed:12897246"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1M6E"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1M6E"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1M6E"
FT TURN 109..113
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1M6E"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 181..198
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:1M6E"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1M6E"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:1M6E"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:1M6E"
FT TURN 297..302
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 303..320
FT /evidence="ECO:0007829|PDB:1M6E"
FT HELIX 322..341
FT /evidence="ECO:0007829|PDB:1M6E"
FT STRAND 346..356
FT /evidence="ECO:0007829|PDB:1M6E"
SQ SEQUENCE 359 AA; 40289 MW; B0FE3E41AEBEDB51 CRC64;
MDVRQVLHMK GGAGENSYAM NSFIQRQVIS ITKPITEAAI TALYSGDTVT TRLAIADLGC
SSGPNALFAV TELIKTVEEL RKKMGRENSP EYQIFLNDLP GNDFNAIFRS LPIENDVDGV
CFINGVPGSF YGRLFPRNTL HFIHSSYSLM WLSQVPIGIE SNKGNIYMAN TCPQSVLNAY
YKQFQEDHAL FLRCRAQEVV PGGRMVLTIL GRRSEDRAST ECCLIWQLLA MALNQMVSEG
LIEEEKMDKF NIPQYTPSPT EVEAEILKEG SFLIDHIEAS EIYWSSCTKD GDGGGSVEEE
GYNVARCMRA VAEPLLLDHF GEAIIEDVFH RYKLLIIERM SKEKTKFINV IVSLIRKSD
