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Protein

Intracellular chorismate mutase

Gene

Rv0948c

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. Probably involved in the aromatic amino acid biosynthesis.3 Publications

Catalytic activityi

Chorismate = prephenate.

Enzyme regulationi

The formation of the complex with AroG activates the chorismate mutase activity by more than two orders of magnitude to a catalytic efficiency (kcat/Km) typical for chorismate mutase. This activation is primarily caused by a more than 30-fold-decreased Km value, but also by a four-fold increase in kcat. The activity of the complex is inhibited by phenylalanine and tyrosine by about 70 and 40%, respectively.1 Publication

Kineticsi

  1. KM=500 µM for chorismate (at 30 degrees Celsius and at pH 7.5)1 Publication
  2. KM=1140 µM for chorismate (at 30 degrees Celsius and at pH 7.5)1 Publication
  3. KM=1500 µM for chorismate (at 30 degrees Celsius and at pH 7.5)1 Publication
  1. Vmax=1.2 µmol/min/mg enzyme (at 30 degrees Celsius and at pH 7.5)1 Publication

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 sitei33SubstrateSequence analysis1
Binding sitei50Substrate1
Binding sitei54Substrate1
Binding sitei61SubstrateSequence analysis1
Sitei61Important for catalysis1
Sitei101Important for activation via AroG1
Sitei102Important for activation via AroG1
Sitei103Important for activation via AroG1

GO - Molecular functioni

  • chorismate mutase activity Source: MTBBASE

GO - Biological processi

  • aromatic amino acid family biosynthetic process, prephenate pathway Source: MTBBASE
  • cellular amino acid biosynthetic process Source: UniProtKB-KW
  • chorismate metabolic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-5103-MONOMER.
UniPathwayiUPA00120; UER00203.

Names & Taxonomyi

Protein namesi
Recommended name:
Intracellular chorismate mutase (EC:5.4.99.5)
Short name:
CM
Gene namesi
Ordered Locus Names:Rv0948c
ORF Names:MTCY10D7.26
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0948c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi61R → K: It is catalytically catastrophic, but strongly activated by AroG. 1 Publication1
Mutagenesisi101G → A: The catalytic efficiency and the affinity are 5 and 3-fold lower than the wild-type. The activation by AroG is 10-fold lower than the wild-type. 1 Publication1
Mutagenesisi102R → A: The catalytic efficiency and the affinity are slightly modified. The activation by AroG is 2-fold lower than the wild-type. 1 Publication1
Mutagenesisi103 – 105Missing : The catalytic efficiency and the affinity are higher than the wild-type. The activation by AroG is 20-fold lower than the wild-type. 3
Mutagenesisi103L → A: The catalytic efficiency and the affinity are identical to the wild-type. The activation by AroG is 10-fold lower than the wild type. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2069157.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001192001 – 105Intracellular chorismate mutaseAdd BLAST105

Proteomic databases

PaxDbiP9WIC1.

Interactioni

Subunit structurei

Homodimer. Interacts with AroG.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
aroGO535122EBI-5241850,EBI-5241825

Protein-protein interaction databases

IntActiP9WIC1. 1 interactor.
STRINGi83332.Rv0948c.

Chemistry databases

BindingDBiP9WIC1.

Structurei

Secondary structure

1105
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 64Combined sources36
Turni70 – 72Combined sources3
Helixi73 – 82Combined sources10
Helixi86 – 98Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QBVX-ray2.00A16-105[»]
2VKLX-ray1.65A16-105[»]
2W19X-ray2.15C/D16-105[»]
2W1AX-ray2.35C/D16-105[»]
5CKXX-ray2.70C/D16-105[»]
ProteinModelPortaliP9WIC1.
SMRiP9WIC1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 105Chorismate mutasePROSITE-ProRule annotationAdd BLAST83

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni73 – 74Substrate binding2
Regioni100 – 101Substrate bindingSequence analysis2

Sequence similaritiesi

Contains 1 chorismate mutase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105W7X. Bacteria.
COG1605. LUCA.
KOiK04093.
OMAiIIGRTRM.
PhylomeDBiP9WIC1.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002701. Chorismate_mutase.
IPR010958. Chorismate_mutase_highGC-bac.
IPR020822. Chorismate_mutase_type_II.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
[Graphical view]
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01808. CM_M_hiGC-arch. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WIC1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPEPPHHEN AELAAMNLEM LESQPVPEID TLREEIDRLD AEILALVKRR
60 70 80 90 100
AEVSKAIGKA RMASGGTRLV HSREMKVIER YSELGPDGKD LAILLLRLGR

GRLGH
Length:105
Mass (Da):11,771
Last modified:April 16, 2014 - v1
Checksum:i6A387E4A53CC9F6D
GO

Mass spectrometryi

Molecular mass is 11771 Da from positions 1 - 105. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43696.1.
PIRiB70716.
RefSeqiNP_215463.1. NC_000962.3.
WP_003404838.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP43696; CCP43696; Rv0948c.
GeneIDi885485.
KEGGimtu:Rv0948c.
mtv:RVBD_0948c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43696.1.
PIRiB70716.
RefSeqiNP_215463.1. NC_000962.3.
WP_003404838.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QBVX-ray2.00A16-105[»]
2VKLX-ray1.65A16-105[»]
2W19X-ray2.15C/D16-105[»]
2W1AX-ray2.35C/D16-105[»]
5CKXX-ray2.70C/D16-105[»]
ProteinModelPortaliP9WIC1.
SMRiP9WIC1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP9WIC1. 1 interactor.
STRINGi83332.Rv0948c.

Chemistry databases

BindingDBiP9WIC1.
ChEMBLiCHEMBL2069157.

Proteomic databases

PaxDbiP9WIC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43696; CCP43696; Rv0948c.
GeneIDi885485.
KEGGimtu:Rv0948c.
mtv:RVBD_0948c.

Organism-specific databases

TubercuListiRv0948c.

Phylogenomic databases

eggNOGiENOG4105W7X. Bacteria.
COG1605. LUCA.
KOiK04093.
OMAiIIGRTRM.
PhylomeDBiP9WIC1.

Enzyme and pathway databases

UniPathwayiUPA00120; UER00203.
BioCyciMTBH37RV:G185E-5103-MONOMER.

Miscellaneous databases

PROiP9WIC1.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002701. Chorismate_mutase.
IPR010958. Chorismate_mutase_highGC-bac.
IPR020822. Chorismate_mutase_type_II.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
[Graphical view]
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01808. CM_M_hiGC-arch. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHMU_MYCTU
AccessioniPrimary (citable) accession number: P9WIC1
Secondary accession number(s): L0T5D6, P64767, P71562
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.