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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)DescriptionActionsGraphical viewLength
    Binding sitei18S-adenosyl-L-methionine1
    Binding sitei25Substrate1
    Binding sitei98S-adenosyl-L-methionine1
    Binding sitei151Substrate1
    Metal bindingi162Magnesium; via carbonyl oxygenBy similarity1
    Metal bindingi248Magnesium; via carbonyl oxygenBy similarity1
    Metal bindingi250Magnesium; via carbonyl oxygenBy similarity1
    Metal bindingi251MagnesiumBy similarity1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi147Y → 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 Publication1
    Mutagenesisi150M → 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 Publication1
    Mutagenesisi225I → 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 Publication1
    Mutagenesisi347F → 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 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004066041 – 359Salicylate carboxymethyltransferaseAdd BLAST359

    Structurei

    Secondary structure

    1359
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 7Combined sources4
    Turni16 – 19Combined sources4
    Helixi23 – 31Combined sources9
    Helixi33 – 44Combined sources12
    Beta strandi45 – 53Combined sources9
    Beta strandi56 – 59Combined sources4
    Turni64 – 68Combined sources5
    Helixi69 – 71Combined sources3
    Helixi74 – 82Combined sources9
    Beta strandi83 – 85Combined sources3
    Beta strandi91 – 98Combined sources8
    Helixi104 – 108Combined sources5
    Turni109 – 113Combined sources5
    Beta strandi121 – 128Combined sources8
    Beta strandi130 – 132Combined sources3
    Beta strandi143 – 147Combined sources5
    Turni163 – 166Combined sources4
    Beta strandi170 – 172Combined sources3
    Helixi181 – 198Combined sources18
    Beta strandi204 – 211Combined sources8
    Beta strandi213 – 219Combined sources7
    Turni220 – 222Combined sources3
    Turni224 – 226Combined sources3
    Helixi227 – 238Combined sources12
    Helixi248 – 250Combined sources3
    Helixi260 – 268Combined sources9
    Turni269 – 271Combined sources3
    Beta strandi275 – 283Combined sources9
    Turni297 – 302Combined sources6
    Helixi303 – 320Combined sources18
    Helixi322 – 341Combined sources20
    Beta strandi346 – 356Combined sources11

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9SPV4.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni59 – 61S-adenosyl-L-methionine binding3
    Regioni129 – 131S-adenosyl-L-methionine binding3

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1M6EX-ray3.00X1-359[»]
    ProteinModelPortaliQ9SPV4.
    SMRiQ9SPV4.
    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...

    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: November 2, 2016
    This is version 52 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.