P9WFX1 · MBTI_MYCTU

Function

function

Involved in the incorporation of salicylate into the virulence-conferring salicylate-based siderophore mycobactin. Catalyzes the initial conversion of chorismate to yield the intermediate isochorismate (isochorismate synthase activity), and the subsequent elimination of the enolpyruvyl side chain to give salicylate (isochorismate pyruvate-lyase activity). In the absence of magnesium, MbtI displays a chorismate mutase activity and converts chorismate to prephenate.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Inhibited by (E)-3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid (AMT), 3-(1-carboxy-2-phenylvinyloxy)-2-hydroxybenzoic acid (phenyl-AMT), 3-(1-carboxy-3-methylbut-1-enyloxy)-2-hydroxybenzoic acid, 3-(1-carboxybut-1-enyloxy)-2-hydroxybenzoic acid (ethyl-AMT), 3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid (methyl-AMT), 3-(1-carboxy-2-cyclopropylethenyloxy)-2-hydroxybenzoic acid (cyclopropyl-AMT) and 3-(1-carboxy-3-methylbut-1-enyloxy)-2-hydroxybenzoic acid (isopropyl-AMT).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.6 μMisochorismate837for isochorismate pyruvate lyase activity
6 μMisochorismate837for salicylate synthase activity
21 μMisochorismate825for salicylate synthase activity
26 μMchorismate7.537for chorismate mutase activity without magnesium
34 μMchorismate737for isochorismate synthase activity
kcat is 2.6 min-1 for isochorismate pyruvate lyase activity (at pH 8 and 37 degrees Celsius). kcat is 2.8 min-1 for salicylate synthase activity (at pH 8 and 37 degrees Celsius). kcat is 3.1 min-1 for isochorismate synthase activity (at pH 7 and 37 degrees Celsius). kcat is 4.5 min-1 for chorismate mutase activity (without magnesium at pH 7.5 and 37 degrees Celsius).

pH Dependence

At pH below 7.5, MtbI produces isochorismate and at pH 8 it produces salicylate.

Pathway

Siderophore biosynthesis; mycobactin biosynthesis.

Features

Showing features for active site, site, binding site.

TypeIDPosition(s)Description
Active site252Proton donor
Site268Could activate a water molecule for attack at the C2 of chorismate and involved in recognition/elimination of the C4 hydroxyl
Binding site270-271substrate
Binding site297Mg2+ (UniProtKB | ChEBI)
Binding site385substrate
Binding site405substrate
Binding site419-421substrate
Binding site431Mg2+ (UniProtKB | ChEBI)
Binding site434Mg2+ (UniProtKB | ChEBI)
Binding site438substrate

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionchorismate mutase activity
Molecular Functionisochorismate pyruvate lyase activity
Molecular Functionisochorismate synthase activity
Molecular Functionmagnesium ion binding
Molecular Functionoxo-acid-lyase activity
Biological Processcatechol-containing siderophore biosynthetic process
Biological Processcellular response to iron ion starvation
Biological Processresponse to host immune response
Biological Processsalicylic acid biosynthetic process
Biological Processtryptophan biosynthetic process

Keywords

Enzyme and pathway databases

Chemistry

Names & Taxonomy

Protein names

  • Recommended name
    Salicylate synthase
  • Alternative names
    • Chorismate mutase
      (CM
      ) (EC:5.4.99.5
      ) . EC:5.4.99.5 (UniProtKB | ENZYME | Rhea)
    • Isochorismate synthase/isochorismate lyase
      (EC:4.2.99.21
      , EC:5.4.4.2
      ) . EC:4.2.99.21 (UniProtKB | ENZYME | Rhea)
      , EC:5.4.4.2 (UniProtKB | ENZYME | Rhea)
    • Mycobactin synthase protein

Gene names

    • Name
      mbtI
    • Synonyms
      trpE2
    • Ordered locus names
      Rv2386c

Organism names

Accessions

  • Primary accession
    P9WFX1
  • Secondary accessions
    • L0T9G8
    • Q79FE7
    • Q7D785

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene display a reduction in salicylic acid biosynthesis and a drastic decrease in production of mycobactin compared with the wild-type strain.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis205Only the chorismate mutase activity is observed.
Mutagenesis252No activity is observed.
Mutagenesis268Only the chorismate mutase activity is observed.
Mutagenesis271Only the chorismate mutase activity is observed.
Mutagenesis334Only the chorismate mutase activity is observed.
Mutagenesis405Only the chorismate mutase activity is observed.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002620861-450Salicylate synthase

Proteomic databases

Expression

Induction

Induced by iron starvation conditions and during infection of human THP-1 macrophages. Transcriptionally repressed by IdeR and iron.

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    450
  • Mass (Da)
    48,754
  • Last updated
    2014-04-16 v1
  • Checksum
    79D95307E025D28A
MSELSVATGAVSTASSSIPMPAGVNPADLAAELAAVVTESVDEDYLLYECDGQWVLAAGVQAMVELDSDELRVIRDGVTRRQQWSGRPGAALGEAVDRLLLETDQAFGWVAFEFGVHRYGLQQRLAPHTPLARVFSPRTRIMVSEKEIRLFDAGIRHREAIDRLLATGVREVPQSRSVDVSDDPSGFRRRVAVAVDEIAAGRYHKVILSRCVEVPFAIDFPLTYRLGRRHNTPVRSFLLQLGGIRALGYSPELVTAVRADGVVITEPLAGTRALGRGPAIDRLARDDLESNSKEIVEHAISVRSSLEEITDIAEPGSAAVIDFMTVRERGSVQHLGSTIRARLDPSSDRMAALEALFPAVTASGIPKAAGVEAIFRLDECPRGLYSGAVVMLSADGGLDAALTLRAAYQVGGRTWLRAGAGIIEESEPEREFEETCEKLSTLTPYLVARQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP45174.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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