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Protein

Secreted chorismate mutase

Gene

Rv1885c

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.2 Publications

Catalytic activityi

Chorismate = prephenate.

Enzyme regulationi

Tyrosine, phenylalanine, and tryptophan moderately enhance chorismate mutase activity at low concentrations, but allosterically inhibit the enzyme at higher concentrations.1 Publication

Kineticsi

  1. KM=120 µM for chorismate (at pH 7.5 and 37 degrees Celsius)1 Publication
  2. KM=180 µM for chorismate (at pH 7.5 and 30 degrees Celsius)1 Publication
  3. KM=500 µM for chorismate (with 27.5 nM of protein at pH 7.5 and 37 degrees Celsius)1 Publication
  4. KM=670 µM for chorismate (with 8 nM of protein at pH 7.5 and 37 degrees Celsius)1 Publication
  1. Vmax=74 µmol/min/mg enzyme (at pH 7.5 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.5. The activity is dramatically affected under alkaline conditions (pH 9.5).2 Publications

Temperature dependencei

Optimum temperature is between 37 to 50 degrees Celsius. An increase in temperature does increase enzyme activity, and complete reversible denaturation of the enzyme occurs at a temperature close to 60 degrees Celsius.2 Publications

Pathwayi: prephenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes prephenate from chorismate.
Proteins known to be involved in this subpathway in this organism are:
  1. Intracellular chorismate mutase (Rv0948c), Secreted chorismate mutase (Rv1885c), Chorismate mutase (LH57_10265)
This subpathway is part of the pathway prephenate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes prephenate from chorismate, the pathway prephenate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491Substrate
Binding sitei60 – 601Substrate
Binding sitei69 – 691Substrate
Binding sitei76 – 761Substrate
Binding sitei134 – 1341Substrate

GO - Molecular functioni

  • chorismate mutase activity Source: MTBBASE

GO - Biological processi

  • chorismate metabolic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

UniPathwayiUPA00120; UER00203.

Names & Taxonomyi

Protein namesi
Recommended name:
Secreted chorismate mutase (EC:5.4.99.5)
Short name:
*MtCM
Short name:
CM
Gene namesi
Ordered Locus Names:Rv1885c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1885c.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491R → A: Less than 1% of the wild-type enzyme activity. 1 Publication
Mutagenesisi60 – 601K → A: Less than 1% of the wild-type enzyme activity. 1 Publication
Mutagenesisi69 – 691D → A: No effect on the enzyme activity. 1 Publication
Mutagenesisi72 – 721R → A: Less than 1% of the wild-type enzyme activity. 1 Publication
Mutagenesisi105 – 1051T → A: 20% of the wild-type enzyme activity. 1 Publication
Mutagenesisi109 – 1091E → A: 10% of the wild-type enzyme activity. 1 Publication
Mutagenesisi109 – 1091E → Q: 40% of the wild-type enzyme activity at pH 7.5 and 27% of the wild-type enzyme activity at pH 4. 1 Publication
Mutagenesisi134 – 1341R → A: Less than 1% of the wild-type enzyme activity. 1 Publication

Chemistry

ChEMBLiCHEMBL6066.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Add
BLAST
Chaini34 – 199166Secreted chorismate mutasePRO_0000414906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi160 ↔ 193

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP9WIB9.

Interactioni

Subunit structurei

Homodimer.5 Publications

Protein-protein interaction databases

STRINGi83332.Rv1885c.

Chemistry

BindingDBiP9WIB9.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5112Combined sources
Helixi53 – 6311Combined sources
Helixi70 – 8617Combined sources
Helixi91 – 11828Combined sources
Helixi120 – 1223Combined sources
Helixi131 – 15020Combined sources
Helixi152 – 1554Combined sources
Helixi160 – 17415Combined sources
Helixi179 – 18810Combined sources
Turni189 – 1913Combined sources
Helixi192 – 1943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AO2X-ray2.07A/B/C35-199[»]
2F6LX-ray1.70A/B34-199[»]
2FP1X-ray1.55A/B34-199[»]
2FP2X-ray1.64A/B34-199[»]
ProteinModelPortaliP9WIB9.
SMRiP9WIB9. Positions 35-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 11380Chorismate mutasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 765Substrate binding
Regioni105 – 1095Substrate binding

Sequence similaritiesi

Contains 1 chorismate mutase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105WWF. Bacteria.
COG1605. LUCA.
KOiK04093.
OMAiRSAPDCP.
PhylomeDBiP9WIB9.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002701. Chorismate_mutase.
IPR008240. Chorismate_mutase_periplasmic.
IPR020822. Chorismate_mutase_type_II.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF026640. Peripl_chor_mut. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01806. CM_mono2. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WIB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTRPREIYL ATAVSIGILL SLIAPLGPPL ARADGTSQLA ELVDAAAERL
60 70 80 90 100
EVADPVAAFK WRAQLPIEDS GRVEQQLAKL GEDARSQHID PDYVTRVFDD
110 120 130 140 150
QIRATEAIEY SRFSDWKLNP ASAPPEPPDL SASRSAIDSL NNRMLSQIWS
160 170 180 190
HWSLLSAPSC AAQLDRAKRD IVRSRHLDSL YQRALTTATQ SYCQALPPA
Length:199
Mass (Da):21,945
Last modified:April 16, 2014 - v1
Checksum:iBC5DFB776FC3FA1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44651.1.
PIRiB70516.
RefSeqiNP_216401.1. NC_000962.3.
WP_003899064.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44651; CCP44651; Rv1885c.
GeneIDi885772.
KEGGimtu:Rv1885c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44651.1.
PIRiB70516.
RefSeqiNP_216401.1. NC_000962.3.
WP_003899064.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AO2X-ray2.07A/B/C35-199[»]
2F6LX-ray1.70A/B34-199[»]
2FP1X-ray1.55A/B34-199[»]
2FP2X-ray1.64A/B34-199[»]
ProteinModelPortaliP9WIB9.
SMRiP9WIB9. Positions 35-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1885c.

Chemistry

BindingDBiP9WIB9.
ChEMBLiCHEMBL6066.

Proteomic databases

PaxDbiP9WIB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44651; CCP44651; Rv1885c.
GeneIDi885772.
KEGGimtu:Rv1885c.

Organism-specific databases

TubercuListiRv1885c.

Phylogenomic databases

eggNOGiENOG4105WWF. Bacteria.
COG1605. LUCA.
KOiK04093.
OMAiRSAPDCP.
PhylomeDBiP9WIB9.

Enzyme and pathway databases

UniPathwayiUPA00120; UER00203.

Miscellaneous databases

PROiP9WIB9.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002701. Chorismate_mutase.
IPR008240. Chorismate_mutase_periplasmic.
IPR020822. Chorismate_mutase_type_II.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF026640. Peripl_chor_mut. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01806. CM_mono2. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis."
    Sasso S., Ramakrishnan C., Gamper M., Hilvert D., Kast P.
    FEBS J. 272:375-389(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CHORISMATE MUTASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: ATCC 25618 / H37Rv.
  3. "Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity."
    Prakash P., Aruna B., Sardesai A.A., Hasnain S.E.
    J. Biol. Chem. 280:19641-19648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CHORISMATE MUTASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, SUBUNIT.
    Strain: ATCC 25618 / H37Rv.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  5. "1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed."
    Okvist M., Dey R., Sasso S., Grahn E., Kast P., Krengel U.
    J. Mol. Biol. 357:1483-1499(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 34-199 IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
    Strain: ATCC 25618 / H37Rv.
  6. "The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions."
    Qamra R., Prakash P., Aruna B., Hasnain S.E., Mande S.C.
    Biochemistry 45:6997-7005(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 35-199, SUBUNIT.
    Strain: ATCC 25618 / H37Rv.
  7. "Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids."
    Kim S.K., Reddy S.K., Nelson B.C., Vasquez G.B., Davis A., Howard A.J., Patterson S., Gilliland G.L., Ladner J.E., Reddy P.T.
    J. Bacteriol. 188:8638-8648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 34-199, MUTAGENESIS OF ARG-49; LYS-60; ASP-69; ARG-72; THR-105; GLU-109 AND ARG-134, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: ATCC 25618 / H37Rv.
  8. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
    Raman K., Yeturu K., Chandra N.
    BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSCMU_MYCTU
AccessioniPrimary (citable) accession number: P9WIB9
Secondary accession number(s): L0T9J1, O07746, Q7D7U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: June 8, 2016
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a high-confidence drug target.1 Publication
In the presence of high concentrations of tyrosine, phenylalanine, and tryptophan, the enzyme is completely protected from proteolytic degradation.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.