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UniProtKB - P9WFX1 (MBTI_MYCTU)
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>sp|P9WFX1|MBTI_MYCTU Salicylate synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=mbtI PE=1 SV=1 MSELSVATGAVSTASSSIPMPAGVNPADLAAELAAVVTESVDEDYLLYECDGQWVLAAGV QAMVELDSDELRVIRDGVTRRQQWSGRPGAALGEAVDRLLLETDQAFGWVAFEFGVHRYG LQQRLAPHTPLARVFSPRTRIMVSEKEIRLFDAGIRHREAIDRLLATGVREVPQSRSVDV SDDPSGFRRRVAVAVDEIAAGRYHKVILSRCVEVPFAIDFPLTYRLGRRHNTPVRSFLLQ LGGIRALGYSPELVTAVRADGVVITEPLAGTRALGRGPAIDRLARDDLESNSKEIVEHAI SVRSSLEEITDIAEPGSAAVIDFMTVRERGSVQHLGSTIRARLDPSSDRMAALEALFPAV TASGIPKAAGVEAIFRLDECPRGLYSGAVVMLSADGGLDAALTLRAAYQVGGRTWLRAGA GIIEESEPEREFEETCEKLSTLTPYLVARQCommunity curation ()Add a publicationFeedback
Protein
Salicylate synthase
Gene
mbtI
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
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.
5 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin."
Quadri L.E.N., Sello J., Keating T.A., Weinreb P.H., Walsh C.T.
Chem. Biol. 5:631-645(1998) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY. - Ref.5"Roles of trpE2, entC and entD in salicylic acid biosynthesis in Mycobacterium smegmatis."
Nagachar N., Ratledge C.
FEMS Microbiol. Lett. 308:159-165(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE. - Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT. - Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- chorismateEC:5.4.4.2
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Manual assertion based on experiment ini
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT. - Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
- Search proteins in UniProtKB for this EC number.
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Manual assertion based on experiment ini
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT. - Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
Source: Rhea- Search for this reaction in UniProtKB.
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chorismate- Search proteins in UniProtKB for this molecule.
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=isochorismate- Search proteins in UniProtKB for this molecule.
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- isochorismateEC:4.2.99.21
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Manual assertion based on experiment ini
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT. - Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
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Manual assertion based on experiment ini
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT. - Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
Source: Rhea- Search for this reaction in UniProtKB.
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isochorismate- Search proteins in UniProtKB for this molecule.
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=pyruvate- Search proteins in UniProtKB for this molecule.
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+salicylate- Search proteins in UniProtKB for this molecule.
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- chorismateEC:5.4.99.5
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Manual assertion based on experiment ini
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
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Manual assertion based on experiment ini
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
Source: Rhea- Search for this reaction in UniProtKB.
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chorismate- Search proteins in UniProtKB for this molecule.
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=prephenate- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Mg2+
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Manual assertion based on experiment ini
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT. - Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
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).2 Publications
Manual assertion based on experiment ini
- Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT. - Ref.10"Implications of binding mode and active site flexibility for inhibitor potency against the salicylate synthase from Mycobacterium tuberculosis."
Chi G., Manos-Turvey A., O'Connor P.D., Johnston J.M., Evans G.L., Baker E.N., Payne R.J., Lott J.S., Bulloch E.M.
Biochemistry 51:4868-4879(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ACTIVITY REGULATION, SUBUNIT.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
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).1 Publication
Manual assertion based on experiment ini
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- KM=2.6 µM for isochorismate (for isochorismate pyruvate lyase activity at pH 8 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- KM=6 µM for isochorismate (for salicylate synthase activity at pH 8 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- KM=21 µM for isochorismate (for salicylate synthase activity at pH 8 and 25 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
- KM=26 µM for chorismate (for chorismate mutase activity without magnesium at pH 7.5 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- KM=34 µM for chorismate (for isochorismate synthase activity at pH 7 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
pH dependencei
At pH below 7.5, MtbI produces isochorismate and at pH 8 it produces salicylate.1 Publication
Manual assertion based on experiment ini
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: mycobactin biosynthesis
This protein is involved in the pathway mycobactin biosynthesis, which is part of Siderophore biosynthesis.1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.2"Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin."
Quadri L.E.N., Sello J., Keating T.A., Weinreb P.H., Walsh C.T.
Chem. Biol. 5:631-645(1998) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY.
View all proteins of this organism that are known to be involved in the pathway mycobactin biosynthesis and in Siderophore biosynthesis.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 252 | Proton donorBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 268 | Could activate a water molecule for attack at the C2 of chorismate and involved in recognition/elimination of the C4 hydroxyl1 Publication Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 297 | Magnesium1 Publication Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 385 | Substrate3 Publications Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 405 | Substrate3 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 431 | Magnesium1 Publication Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 434 | Magnesium1 Publication Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 438 | Substrate3 Publications Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- chorismate mutase activity Source: MTBBASE
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- isochorismate pyruvate lyase activity Source: MTBBASEInferred from direct assayi
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- isochorismate synthase activity Source: MTBBASEInferred from direct assayi
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- magnesium ion binding Source: MTBBASEInferred from direct assayi
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
- oxo-acid-lyase activity Source: InterPro
GO - Biological processi
- catechol-containing siderophore biosynthetic process Source: MTBBASEInferred from direct assayi
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
- cellular response to iron ion starvation Source: MTBBASE
<p>Inferred from Expression Pattern</p>
<p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p>
Inferred from expression patterni
- Ref.3"The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages."
Gold B., Rodriguez G.M., Marras S.A.E., Pentecost M., Smith I.
Mol. Microbiol. 42:851-865(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
- response to host immune response Source: MTBBASEInferred from expression patterni
- Ref.3"The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages."
Gold B., Rodriguez G.M., Marras S.A.E., Pentecost M., Smith I.
Mol. Microbiol. 42:851-865(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
- salicylic acid biosynthetic process Source: MTBBASEInferred from direct assayi
- Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
- tryptophan biosynthetic process Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Isomerase, Lyase |
| Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 4.2.99.21, 3445 5.4.4.2, 3445 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00011 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000001285 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Salicylate synthase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Alternative name(s): Chorismate mutase1 Publication Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: CM1 Publication Manual assertion based on opinion ini
Isochorismate synthase/isochorismate lyase1 Publication Manual assertion based on opinion ini
Manual assertion based on experiment ini
Manual assertion based on experiment ini
Mycobactin synthase protein1 Publication Manual assertion inferred by curator fromi
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:mbtI1 Publication Manual assertion based on opinion ini
Synonyms:trpE21 Publication Manual assertion based on opinion ini
Ordered Locus Names:Rv2386c |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83332 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Terrabacteria group › Actinobacteria › Actinomycetia › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium tuberculosis |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Mycobacterium tuberculosis strain H37Rv genome database More...TubercuListi | Rv2386c |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma Membrane
- plasma membrane Source: MTBBASEInferred from high throughput direct assayi
- "Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling."
Mawuenyega K.G., Forst C.V., Dobos K.M., Belisle J.T., Chen J., Bradbury E.M., Bradbury A.R., Chen X.
Mol Biol Cell 16:396-404(2005) [PubMed] [Europe PMC] [Abstract]
- plasma membrane Source: MTBBASEInferred from high throughput direct assayi
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
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.1 Publication
Manual assertion based on experiment ini
- Ref.5"Roles of trpE2, entC and entD in salicylic acid biosynthesis in Mycobacterium smegmatis."
Nagachar N., Ratledge C.
FEMS Microbiol. Lett. 308:159-165(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 205 | K → A: Only the chorismate mutase activity is observed. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 252 | E → Q: No activity is observed. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 268 | L → A: Only the chorismate mutase activity is observed. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 271 | T → A: Only the chorismate mutase activity is observed. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 334 | H → M: Only the chorismate mutase activity is observed. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 405 | R → A: Only the chorismate mutase activity is observed. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000262086 | 1 – 450 | Salicylate synthaseAdd BLAST | 450 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P9WFX1 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Induced by iron starvation conditions and during infection of human THP-1 macrophages. Transcriptionally repressed by IdeR and iron.1 Publication
Manual assertion based on experiment ini
- Ref.3"The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages."
Gold B., Rodriguez G.M., Marras S.A.E., Pentecost M., Smith I.
Mol. Microbiol. 42:851-865(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Monomer.
5 PublicationsManual assertion based on experiment ini
- Ref.4"Crystallization and preliminary X-ray crystallographic analysis of MbtI, a protein essential for siderophore biosynthesis in Mycobacterium tuberculosis."
Harrison A.J., Ramsay R.J., Baker E.N., Lott J.S.
Acta Crystallogr. F 61:121-123(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CRYSTALLIZATION, SUBUNIT. - Ref.7"The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase."
Harrison A.J., Yu M., Gardenborg T., Middleditch M., Ramsay R.J., Baker E.N., Lott J.S.
J. Bacteriol. 188:6081-6091(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. - Ref.8"Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis."
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
Biochemistry 46:954-964(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-205; GLU-252; LEU-268; THR-271; HIS-334 AND ARG-405, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT. - Ref.9"Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)."
Manos-Turvey A., Bulloch E.M., Rutledge P.J., Baker E.N., Lott J.S., Payne R.J.
ChemMedChem 5:1067-1079(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT. - Ref.10"Implications of binding mode and active site flexibility for inhibitor potency against the salicylate synthase from Mycobacterium tuberculosis."
Chi G., Manos-Turvey A., O'Connor P.D., Johnston J.M., Evans G.L., Baker E.N., Payne R.J., Lott J.S., Bulloch E.M.
Biochemistry 51:4868-4879(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ACTIVITY REGULATION, SUBUNIT.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 83332.Rv2386c |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1 – 5 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 6 – 9 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 10 – 14 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 16 – 19 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 26 – 41 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 16 | |
| Beta strandi | 45 – 50 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 53 – 67 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 70 – 75 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 78 – 82 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 88 – 102 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 104 – 110 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 112 – 115 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 117 – 119 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 122 – 124 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 130 – 143 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 145 – 152 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 155 – 167 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 187 – 199 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 204 – 213 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 220 – 228 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 234 – 241 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 244 – 250 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 252 – 257 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 261 – 265 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 268 – 273 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 278 – 290 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 292 – 310 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 19 | |
| Beta strandi | 319 – 329 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 332 – 343 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 349 – 355 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 360 – 362 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 363 – 366 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 367 – 377 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Turni | 383 – 386 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 387 – 393 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 398 – 402 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 405 – 410 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 413 – 422 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 428 – 439 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Turni | 440 – 442 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 443 – 445 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
AlphaFold Protein Structure Database More...AlphaFoldDBi | P9WFX1 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P9WFX1 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 270 – 271 | Substrate binding2 Publications Manual assertion based on experiment ini
| 2 | |
| Regioni | 419 – 421 | Substrate binding3 Publications Manual assertion based on experiment ini
| 3 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG1169, Bacteria |
Identification of Orthologs from Complete Genome Data More...OMAi | VTDFMTV |
Database for complete collections of gene phylogenies More...PhylomeDBi | P9WFX1 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.60.120.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005801, ADC_synthase IPR019999, Anth_synth_I-like IPR015890, Chorismate_C IPR019996, Salicylate_synthase |
The PANTHER Classification System More...PANTHERi | PTHR11236, PTHR11236, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00425, Chorismate_bind, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00095, ANTSNTHASEI |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56322, SSF56322, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR03494, salicyl_syn, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
P9WFX1-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MSELSVATGA VSTASSSIPM PAGVNPADLA AELAAVVTES VDEDYLLYEC
60 70 80 90 100
DGQWVLAAGV QAMVELDSDE LRVIRDGVTR RQQWSGRPGA ALGEAVDRLL
110 120 130 140 150
LETDQAFGWV AFEFGVHRYG LQQRLAPHTP LARVFSPRTR IMVSEKEIRL
160 170 180 190 200
FDAGIRHREA IDRLLATGVR EVPQSRSVDV SDDPSGFRRR VAVAVDEIAA
210 220 230 240 250
GRYHKVILSR CVEVPFAIDF PLTYRLGRRH NTPVRSFLLQ LGGIRALGYS
260 270 280 290 300
PELVTAVRAD GVVITEPLAG TRALGRGPAI DRLARDDLES NSKEIVEHAI
310 320 330 340 350
SVRSSLEEIT DIAEPGSAAV IDFMTVRERG SVQHLGSTIR ARLDPSSDRM
360 370 380 390 400
AALEALFPAV TASGIPKAAG VEAIFRLDEC PRGLYSGAVV MLSADGGLDA
410 420 430 440 450
ALTLRAAYQV GGRTWLRAGA GIIEESEPER EFEETCEKLS TLTPYLVARQ
Length:450
Mass (Da):48,754
Last modified:April 16, 2014 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i79D95307E025D28A
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AL123456 Genomic DNA Translation: CCP45174.1 |
NCBI Reference Sequences More...RefSeqi | WP_003412287.1, NZ_NVQJ01000029.1 YP_177877.1, NC_000962.3 |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 885823 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | mtu:Rv2386c |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P9WFX1 | Salicylate synthase | 450 | UniRef100_Q7TYQ1 | |||
| Salicylate synthase | 450 | |||||
| Isochorismate synthase | 450 | |||||
| Isochorismate synthase mbtI | 450 | |||||
| Isochorismate synthase mbtI | 450 | |||||
| +18 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P9WFX1 | Salicylate synthase | 450 | UniRef90_Q7TYQ1 | |||
| Salicylate synthase | 450 | |||||
| Isochorismate synthase | 450 | |||||
| Isochorismate synthase mbtI | 450 | |||||
| Isochorismate synthase mbtI | 450 | |||||
| +104 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P9WFX1 | Salicylate synthase | 450 | UniRef50_Q73XV3 | |||
| Salicylate synthase | 450 | |||||
| Salicylate synthase | 450 | |||||
| Salicylate synthase | 450 | |||||
| Salicylate synthase | 450 | |||||
| +773 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45174.1 |
| RefSeqi | WP_003412287.1, NZ_NVQJ01000029.1 YP_177877.1, NC_000962.3 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2G5F | X-ray | 1.80 | A/B/C/D | 2-450 | [»] | |
| 2I6Y | X-ray | 2.50 | A | 2-450 | [»] | |
| 3LOG | X-ray | 1.73 | A/B/C/D | 1-449 | [»] | |
| 3RV6 | X-ray | 2.04 | A/B | 2-450 | [»] | |
| 3RV7 | X-ray | 2.50 | A/B/C/D | 2-450 | [»] | |
| 3RV8 | X-ray | 2.29 | A/B/C/D | 1-450 | [»] | |
| 3RV9 | X-ray | 2.14 | A/B/C/D | 2-450 | [»] | |
| 3ST6 | X-ray | 1.75 | A/B/C/D | 1-450 | [»] | |
| 3VEH | X-ray | 2.00 | A/B/C/D | 1-449 | [»] | |
| 6ZA4 | X-ray | 2.09 | A/B/C/D | 1-450 | [»] | |
| 6ZA5 | X-ray | 2.11 | A/B/C/D | 1-450 | [»] | |
| 6ZA6 | X-ray | 1.80 | A/B/C/D | 1-450 | [»] | |
| AlphaFoldDBi | P9WFX1 | |||||
| SMRi | P9WFX1 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 83332.Rv2386c |
Chemistry databases
| SwissLipidsi | SLP:000001285 |
Proteomic databases
| PaxDbi | P9WFX1 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 885823 |
Genome annotation databases
| GeneIDi | 885823 |
| KEGGi | mtu:Rv2386c |
Organism-specific databases
| TubercuListi | Rv2386c |
Phylogenomic databases
| eggNOGi | COG1169, Bacteria |
| OMAi | VTDFMTV |
| PhylomeDBi | P9WFX1 |
Enzyme and pathway databases
| UniPathwayi | UPA00011 |
| BRENDAi | 4.2.99.21, 3445 5.4.4.2, 3445 |
Miscellaneous databases
Protein Ontology More...PROi | PR:P9WFX1 |
Family and domain databases
| Gene3Di | 3.60.120.10, 1 hit |
| InterProi | View protein in InterPro IPR005801, ADC_synthase IPR019999, Anth_synth_I-like IPR015890, Chorismate_C IPR019996, Salicylate_synthase |
| PANTHERi | PTHR11236, PTHR11236, 1 hit |
| Pfami | View protein in Pfam PF00425, Chorismate_bind, 1 hit |
| PRINTSi | PR00095, ANTSNTHASEI |
| SUPFAMi | SSF56322, SSF56322, 1 hit |
| TIGRFAMsi | TIGR03494, salicyl_syn, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | MBTI_MYCTU | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P9WFX1Primary (citable) accession number: P9WFX1 Secondary accession number(s): L0T9G8, Q79FE7, Q7D785 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
| Last sequence update: | April 16, 2014 | |
| Last modified: | May 25, 2022 | |
| This is version 40 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
