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Protein

Salicylate carboxymethyltransferase

Gene

SAMT

Organism
Clarkia breweri (Fairy fans) (Eucharidium breweri)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the methylation of the free carboxyl end of the plant hormone salicylic acid (SA). Converts SA to SA methyl ester (MSA). The volatile compound MSA is hypothesized to act as an airborne signal that triggers defense responses in uninfected plants. MSA is an important chemoattractant for moth pollinated flowering plants.

Catalytic activityi

S-adenosyl-L-methionine + salicylate = S-adenosyl-L-homocysteine + methyl salicylate.1 Publication

Kineticsi

  1. KM=23 µM for salicylate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei18 – 181S-adenosyl-L-methionine
    Binding sitei25 – 251Substrate
    Binding sitei98 – 981S-adenosyl-L-methionine
    Binding sitei151 – 1511Substrate
    Metal bindingi162 – 1621Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi248 – 2481Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi250 – 2501Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi251 – 2511MagnesiumBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    Magnesium, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.274. 1437.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Salicylate carboxymethyltransferase (EC:2.1.1.274)
    Alternative name(s):
    S-adenosyl-L-methionine:salicylate acid carboxylmethyltransferase
    Short name:
    CbSAMT
    Salicylate O-methyltransferase
    Gene namesi
    Name:SAMT
    OrganismiClarkia breweri (Fairy fans) (Eucharidium breweri)
    Taxonomic identifieri36903 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsMyrtalesOnagraceaeOnagroideaeOnagreaeClarkia

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi147 – 1471Y → S: Decreases activity 2-fold and switch in specificity for jasmonic acid as substrate; when associated with H-150; Q-225 and Y-347. 1 Publication
    Mutagenesisi150 – 1501M → H: Decreases activity 2-fold and switch in specificity for jasmonic acid as substrate; when associated with S-147; Q-225 and Y-347. 1 Publication
    Mutagenesisi225 – 2251I → Q: Decreases activity 2-fold and switch in specificity for jasmonic acid as substrate; when associated with S-147; H-150 and Y-347. 1 Publication
    Mutagenesisi347 – 3471F → Y: Decreases activity 2-fold and switch in specificity for jasmonic acid as substrate; when associated with S-147; H-150 and Q-225. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Salicylate carboxymethyltransferasePRO_0000406604Add
    BLAST

    Structurei

    Secondary structure

    1
    359
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74Combined sources
    Turni16 – 194Combined sources
    Helixi23 – 319Combined sources
    Helixi33 – 4412Combined sources
    Beta strandi45 – 539Combined sources
    Beta strandi56 – 594Combined sources
    Turni64 – 685Combined sources
    Helixi69 – 713Combined sources
    Helixi74 – 829Combined sources
    Beta strandi83 – 853Combined sources
    Beta strandi91 – 988Combined sources
    Helixi104 – 1085Combined sources
    Turni109 – 1135Combined sources
    Beta strandi121 – 1288Combined sources
    Beta strandi130 – 1323Combined sources
    Beta strandi143 – 1475Combined sources
    Turni163 – 1664Combined sources
    Beta strandi170 – 1723Combined sources
    Helixi181 – 19818Combined sources
    Beta strandi204 – 2118Combined sources
    Beta strandi213 – 2197Combined sources
    Turni220 – 2223Combined sources
    Turni224 – 2263Combined sources
    Helixi227 – 23812Combined sources
    Helixi248 – 2503Combined sources
    Helixi260 – 2689Combined sources
    Turni269 – 2713Combined sources
    Beta strandi275 – 2839Combined sources
    Turni297 – 3026Combined sources
    Helixi303 – 32018Combined sources
    Helixi322 – 34120Combined sources
    Beta strandi346 – 35611Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M6EX-ray3.00X1-359[»]
    ProteinModelPortaliQ9SPV4.
    SMRiQ9SPV4. Positions 1-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9SPV4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni59 – 613S-adenosyl-L-methionine binding
    Regioni129 – 1313S-adenosyl-L-methionine binding

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.150. 2 hits.
    InterProiIPR005299. MeTrfase_7.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PfamiPF03492. Methyltransf_7. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9SPV4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDVRQVLHMK GGAGENSYAM NSFIQRQVIS ITKPITEAAI TALYSGDTVT
    60 70 80 90 100
    TRLAIADLGC SSGPNALFAV TELIKTVEEL RKKMGRENSP EYQIFLNDLP
    110 120 130 140 150
    GNDFNAIFRS LPIENDVDGV CFINGVPGSF YGRLFPRNTL HFIHSSYSLM
    160 170 180 190 200
    WLSQVPIGIE SNKGNIYMAN TCPQSVLNAY YKQFQEDHAL FLRCRAQEVV
    210 220 230 240 250
    PGGRMVLTIL GRRSEDRAST ECCLIWQLLA MALNQMVSEG LIEEEKMDKF
    260 270 280 290 300
    NIPQYTPSPT EVEAEILKEG SFLIDHIEAS EIYWSSCTKD GDGGGSVEEE
    310 320 330 340 350
    GYNVARCMRA VAEPLLLDHF GEAIIEDVFH RYKLLIIERM SKEKTKFINV

    IVSLIRKSD
    Length:359
    Mass (Da):40,289
    Last modified:May 1, 2000 - v1
    Checksum:iB0FE3E41AEBEDB51
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF133053 mRNA. Translation: AAF00108.1.

    Genome annotation databases

    KEGGiag:AAF00108.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF133053 mRNA. Translation: AAF00108.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M6EX-ray3.00X1-359[»]
    ProteinModelPortaliQ9SPV4.
    SMRiQ9SPV4. Positions 1-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAF00108.

    Enzyme and pathway databases

    BRENDAi2.1.1.274. 1437.

    Miscellaneous databases

    EvolutionaryTraceiQ9SPV4.

    Family and domain databases

    Gene3Di3.40.50.150. 2 hits.
    InterProiIPR005299. MeTrfase_7.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PfamiPF03492. Methyltransf_7. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "S-Adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme involved in floral scent production and plant defense, represents a new class of plant methyltransferases."
      Ross J.R., Nam K.H., D'Auria J.C., Pichersky E.
      Arch. Biochem. Biophys. 367:9-16(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family."
      Zubieta C., Ross J.R., Koscheski P., Yang Y., Pichersky E., Noel J.P.
      Plant Cell 15:1704-1716(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND SALICYLIC ACID, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-147; MET-150; ILE-225 AND PHE-347.

    Entry informationi

    Entry nameiSAMT_CLABR
    AccessioniPrimary (citable) accession number: Q9SPV4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: May 1, 2000
    Last modified: April 13, 2016
    This is version 50 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.