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Protein

Salicylic acid-binding protein 2

Gene

SABP2

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required to convert methyl salicylate (MeSA) to salicylic acid (SA) as part of the signal transduction pathways that activate systemic acquired resistance in systemic tissue. MeSA is believed to be an inactive form that needs to be demethylated to exert a biological effect. Also able to catalyze the conversion of acibenzolar-S-methyl into acibenzolar to induce systemic acquired resistance.6 Publications

Enzyme regulationi

Esterase activity is down-regulated by salicylic acid (SA) or by tetraFA, a synthetic SA analog.2 Publications

Kineticsi

  1. KM=8.6 µM for methyl salicylate (MeSA)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei81 – 811Acyl-ester intermediate
    Active sitei210 – 2101Charge relay system
    Active sitei238 – 2381Charge relay system

    GO - Molecular functioni

    • lipase activity Source: UniProtKB
    • methyl salicylate esterase activity Source: UniProtKB

    GO - Biological processi

    • metabolic process Source: UniProtKB
    • systemic acquired resistance, salicylic acid mediated signaling pathway Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Immunity, Innate immunity, Plant defense

    Protein family/group databases

    ESTHERinicta-SABP2. Hydroxynitrile_lyase.
    MEROPSiS33.A63.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Salicylic acid-binding protein 2 (EC:3.1.1.-)
    Short name:
    NtSABP2
    Alternative name(s):
    Methyl salicylate esterase
    Gene namesi
    Name:SABP2
    OrganismiNicotiana tabacum (Common tobacco)
    Taxonomic identifieri4097 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121G → T: Abolishes methyl salicylate esterase activity and favors hydroxynitrile lyase activity; in association with K-239.
    Mutagenesisi13 – 131A → L: Abolishes salicylic acid-binding. 1 Publication
    Mutagenesisi81 – 811S → A: Abolishes methyl salicylate esterase activity. 2 Publications
    Mutagenesisi238 – 2381H → A: Abolishes salicylic acid-binding and methyl salicylate esterase activity. 1 Publication
    Mutagenesisi239 – 2391M → K: Abolishes methyl salicylate esterase activity and favors hydroxynitrile lyase activity; in association with T-12.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 260260Salicylic acid-binding protein 2PRO_0000418175Add
    BLAST

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105Combined sources
    Helixi17 – 204Combined sources
    Helixi23 – 297Combined sources
    Beta strandi33 – 364Combined sources
    Helixi49 – 513Combined sources
    Helixi55 – 6713Combined sources
    Beta strandi71 – 733Combined sources
    Beta strandi75 – 806Combined sources
    Helixi83 – 9311Combined sources
    Helixi95 – 973Combined sources
    Beta strandi98 – 1058Combined sources
    Beta strandi111 – 1133Combined sources
    Helixi117 – 1248Combined sources
    Turni128 – 1336Combined sources
    Beta strandi135 – 1384Combined sources
    Beta strandi142 – 1443Combined sources
    Beta strandi147 – 1504Combined sources
    Helixi153 – 1597Combined sources
    Helixi166 – 17510Combined sources
    Helixi183 – 1886Combined sources
    Turni194 – 1963Combined sources
    Helixi197 – 1993Combined sources
    Beta strandi202 – 2076Combined sources
    Turni211 – 2144Combined sources
    Helixi215 – 22511Combined sources
    Beta strandi228 – 2336Combined sources
    Helixi240 – 2434Combined sources
    Helixi245 – 25814Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XKLX-ray2.00A/B/C/D1-260[»]
    1Y7HX-ray2.52A/B/C/D/E/F/G/H1-260[»]
    1Y7IX-ray2.10A/B1-260[»]
    ProteinModelPortaliQ6RYA0.
    SMRiQ6RYA0. Positions 2-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6RYA0.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6RYA0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKEGKHFVLV HGACHGGWSW YKLKPLLEAA GHKVTALDLA ASGTDLRKIE
    60 70 80 90 100
    ELRTLYDYTL PLMELMESLS ADEKVILVGH SLGGMNLGLA MEKYPQKIYA
    110 120 130 140 150
    AVFLAAFMPD SVHNSSFVLE QYNERTPAEN WLDTQFLPYG SPEEPLTSMF
    160 170 180 190 200
    FGPKFLAHKL YQLCSPEDLA LASSLVRPSS LFMEDLSKAK YFTDERFGSV
    210 220 230 240 250
    KRVYIVCTED KGIPEEFQRW QIDNIGVTEA IEIKGADHMA MLCEPQKLCA
    260
    SLLEIAHKYN
    Length:260
    Mass (Da):29,304
    Last modified:July 5, 2004 - v1
    Checksum:i9AA49E6423361145
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY485932 mRNA. Translation: AAR87711.1.
    UniGeneiNta.4007.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY485932 mRNA. Translation: AAR87711.1.
    UniGeneiNta.4007.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XKLX-ray2.00A/B/C/D1-260[»]
    1Y7HX-ray2.52A/B/C/D/E/F/G/H1-260[»]
    1Y7IX-ray2.10A/B1-260[»]
    ProteinModelPortaliQ6RYA0.
    SMRiQ6RYA0. Positions 2-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERinicta-SABP2. Hydroxynitrile_lyase.
    MEROPSiS33.A63.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6RYA0.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSABP2_TOBAC
    AccessioniPrimary (citable) accession number: Q6RYA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2012
    Last sequence update: July 5, 2004
    Last modified: September 7, 2016
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Two amino acid substitutions near the catalytic pocket are sufficient to switch from an esterase to a hydroxynitrile lyase activity.

    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.