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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)DescriptionActionsGraphical viewLength
Binding sitei49Substrate1
Binding sitei60Substrate1
Binding sitei69Substrate1
Binding sitei76Substrate1
Binding sitei134Substrate1

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

BioCyciMTBH37RV:G185E-6080-MONOMER.
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)DescriptionActionsGraphical viewLength
Mutagenesisi49R → A: Less than 1% of the wild-type enzyme activity. 1 Publication1
Mutagenesisi60K → A: Less than 1% of the wild-type enzyme activity. 1 Publication1
Mutagenesisi69D → A: No effect on the enzyme activity. 1 Publication1
Mutagenesisi72R → A: Less than 1% of the wild-type enzyme activity. 1 Publication1
Mutagenesisi105T → A: 20% of the wild-type enzyme activity. 1 Publication1
Mutagenesisi109E → A: 10% of the wild-type enzyme activity. 1 Publication1
Mutagenesisi109E → Q: 40% of the wild-type enzyme activity at pH 7.5 and 27% of the wild-type enzyme activity at pH 4. 1 Publication1
Mutagenesisi134R → A: Less than 1% of the wild-type enzyme activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL6066.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Add BLAST33
ChainiPRO_000041490634 – 199Secreted chorismate mutaseAdd BLAST166

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi160 ↔ 193

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP9WIB9.

Interactioni

Subunit structurei

Homodimer.5 Publications

Protein-protein interaction databases

STRINGi83332.Rv1885c.

Chemistry databases

BindingDBiP9WIB9.

Structurei

Secondary structure

1199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 51Combined sources12
Helixi53 – 63Combined sources11
Helixi70 – 86Combined sources17
Helixi91 – 118Combined sources28
Helixi120 – 122Combined sources3
Helixi131 – 150Combined sources20
Helixi152 – 155Combined sources4
Helixi160 – 174Combined sources15
Helixi179 – 188Combined sources10
Turni189 – 191Combined sources3
Helixi192 – 194Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 113Chorismate mutasePROSITE-ProRule annotationAdd BLAST80

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni72 – 76Substrate binding5
Regioni105 – 109Substrate binding5

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1885c.

Chemistry databases

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.
BioCyciMTBH37RV:G185E-6080-MONOMER.

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...

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: November 2, 2016
This is version 19 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.