P64767 (CHMU_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Intracellular chorismate mutase
Short name=CM
EC=5.4.99.5

Gene names

Ordered Locus Names:	Rv0948c, MT0975
ORF Names:	MTCY10D7.26

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	105 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. Ref.3 Ref.4 Ref.5
Catalytic activity	Chorismate = prephenate.
Enzyme regulation	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. Ref.5
Pathway	Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subunit structure	Homodimer. Interacts with AroG. Ref.4
Subcellular location	Cytoplasm Potential.
Sequence similarities	Contains 1 chorismate mutase domain.
Biophysicochemical properties	Kinetic parameters: KM=500 µM for chorismate (at 30 degrees Celsius and at pH 7.5, Ref.3) Ref.3 Ref.4 Ref.5 KM=1140 µM for chorismate (at 30 degrees Celsius and at pH 7.5, Ref.5) KM=1500 µM for chorismate (at 30 degrees Celsius and at pH 7.5, Ref.4) Vmax=1.2 µmol/min/mg enzyme (at 30 degrees Celsius and at pH 7.5, Ref.3)
Mass spectrometry	Molecular mass is 11771 Da from positions 1 - 105. Determined by MALDI. Ref.4
Sequence caution	The sequence AAK45223.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aromatic amino acid family biosynthetic process, prephenate pathway Inferred from direct assay Ref.4. Source: MTBBASE chorismate metabolic process Inferred from direct assay Ref.4. Source: MTBBASE
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 15525680. Source: MTBBASE
Molecular_function	chorismate mutase activity Inferred from direct assay Ref.3PubMed 17965159Ref.4. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 105

105

Intracellular chorismate mutase

PRO_0000119200

Regions

Domain

23 – 105

83

Chorismate mutase

Region

73 – 74

2

Substrate binding

Region

100 – 101

2

Substrate binding Potential

Sites

Binding site

33

1

Substrate Potential

Binding site

50

1

Substrate

Binding site

54

1

Substrate

Binding site

61

1

Substrate Potential

Site

61

1

Important for catalysis

Site

101

1

Important for activation via AroG

Site

102

1

Important for activation via AroG

Site

103

1

Important for activation via AroG

Experimental info

Mutagenesis

61

1

R → K: It is catalytically catastrophic, but strongly activated by AroG. Ref.5

Mutagenesis

101

1

G → 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. Ref.5

Mutagenesis

102

1

R → A: The catalytic efficiency and the affinity are slightly modify. The activation by AroG is 2-fold lower than the wild-type. Ref.5

Mutagenesis

103 – 105

3

Missing: The catalytic efficiency and the affinity are higher than the wild-type. The activation by AroG is 20-fold lower than the wild-type. Ref.5

Mutagenesis

103

1

L → 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. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

105

Helix Strand Turn

Details...

Helix

29 – 64

36

Turn

70 – 72

3

Helix

73 – 82

10

Helix

86 – 98

13

Sequences

	Sequence		Length	Mass (Da)
	P64767 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 6A387E4A53CC9F6D	FASTA	105	11,771
	10 20 30 40 50 60 MRPEPPHHEN AELAAMNLEM LESQPVPEID TLREEIDRLD AEILALVKRR AEVSKAIGKA 70 80 90 100 RMASGGTRLV HSREMKVIER YSELGPDGKD LAILLLRLGR GRLGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[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. Strain: ATCC 25618 / H37Rv.
[4]	"A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis." Kim S.K., Reddy S.K., Nelson B.C., Robinson H., Reddy P.T., Ladner J.E. FEBS J. 275:4824-4835(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-105, FUNCTION AS A CHORISMATE MUTASE, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Strain: ATCC 25618 / H37Rv.
[5]	"Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner." Sasso S., Okvist M., Roderer K., Gamper M., Codoni G., Krengel U., Kast P. EMBO J. 28:2128-2142(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 16-105 IN COMPLEX WITH SUBSTRATE ANALOGS AND WITH AROG, FUNCTION AS A CHORISMATE MUTASE, MASS SPECTROMETRY, ENZYME REGULATION, MUTAGENESIS OF ARG-61; GLY-101; ARG-102 AND LEU-103, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842575 Genomic DNA. Translation: CAB02002.1.
AE000516 Genomic DNA. Translation: AAK45223.1. Different initiation.
AL123456 Genomic DNA. Translation: CCP43696.1.

PIR

B70716.

RefSeq

NP_215463.1. NC_000962.3.
NP_335409.2. NC_002755.2.
YP_006514305.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QBV	X-ray	2.00	A	16-105	[»]
2VKL	X-ray	1.65	A	16-105	[»]
2W19	X-ray	2.15	C/D	16-105	[»]
2W1A	X-ray	2.35	C/D	16-105	[»]

ProteinModelPortal

P64767.

SMR

P64767. Positions 28-100.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv0948c.

Proteomic databases

PRIDE

P64767.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK45223; AAK45223; MT0975.

GeneID

13319505.
885485.
926366.

KEGG

mtc:MT0975.
mtu:Rv0948c.
mtv:RVBD_0948c.

PATRIC

18123888. VBIMycTub22151_1067.

Organism-specific databases

TubercuList

Rv0948c.

Phylogenomic databases

eggNOG

COG1605.

HOGENOM

HOG000019826.

KO

K04093.

OMA

ILLRMGR.

ProtClustDB

PRK07857.

Enzyme and pathway databases

UniPathway

UPA00120; UER00203.

Family and domain databases

Gene3D

1.20.59.10. 1 hit.

InterPro

IPR002701. Chorismate_mutase.
IPR010958. Chorismate_mutase_highGC-bac.
IPR020822. Chorismate_mutase_type_II.
[Graphical view]

Pfam

PF01817. CM_2. 1 hit.
[Graphical view]

SMART

SM00830. CM_2. 1 hit.
[Graphical view]

SUPFAM

SSF48600. Chorismate_mut. 1 hit.

TIGRFAMs

TIGR01808. CM_M_hiGC-arch. 1 hit.

PROSITE

PS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P64767.

Entry information

Entry name

CHMU_MYCTU

Accession

Primary (citable) accession number: P64767
Secondary accession number(s): L0T5D6, P71562

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program