P19080 (AROH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chorismate mutase AroH
Short name=CM
EC=5.4.99.5

Gene names

Name:	aroH
Ordered Locus Names:	BSU22690

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	127 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.1
Catalytic activity	Chorismate = prephenate.
Pathway	Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subunit structure	Homotrimer. Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm Potential.
Miscellaneous	This enzyme is monofunctional, and its activity is unaffected by the end-product aromatic amino acids.
Sequence similarities	Contains 1 chorismate mutase aroH-type domain.
Biophysicochemical properties	Kinetic parameters: KM=67 µM for chorismate (at pH 7.5 and at 30 degrees Celsius, Ref.10) Ref.1 Ref.4 Ref.10 KM=87 µM for chorismate (at pH 7.5 and at 30 degrees Celsius) KM=100 µM for chorismate (at pH 7.5 and at 30 degrees Celsius, Ref.1)

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW chorismate metabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chorismate mutase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 127

127

Chorismate mutase AroH

PRO_0000119203

Regions

Domain

3 – 121

119

Chorismate mutase aroH-type

Region

47 – 78

32

Substrate binding By similarity

Sites

Binding site

7

1

Substrate

Binding site

90

1

Substrate

Experimental info

Mutagenesis

78

1

E → A: No chorismate mutase activity. Ref.5

Mutagenesis

90

1

R → A: No chorismate mutase activity. Ref.10

Mutagenesis

90

1

R → G: 2-fold decrease in affinity and very low decrease in catalytic efficiency. Ref.10

Mutagenesis

90

1

R → K: Low decrease in catalytic efficiency and in affinity. Ref.10

Sequence conflict

112

1

V → A in AAA22249. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

127

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Beta strand

13 – 15

3

Helix

17 – 35

19

Helix

39 – 41

3

Beta strand

42 – 49

8

Helix

59 – 63

5

Beta strand

65 – 67

3

Beta strand

73 – 77

5

Beta strand

86 – 97

12

Helix

101 – 103

3

Helix

110 – 115

6

Helix

121 – 124

4

Sequences

	Sequence		Length	Mass (Da)
	P19080 [UniParc]. Last modified October 19, 2002. Version 2. Checksum: 5A803614FE1F402E	FASTA	127	14,517
	10 20 30 40 50 60 MMIRGIRGAT TVERDTEEEI LQKTKQLLEK IIEENHTKPE DVVQMLLSAT PDLHAVFPAK 70 80 90 100 110 120 AVRELSGWQY VPVTCMQEMD VTGGLKKCIR VMMTVQTDVP QDQIRHVYLE KVVVLRPDLS LTKNTEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli." Gray J.V., Golinelli-Pimpaneau B., Knowles J.R. Biochemistry 29:376-383(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-35, FUNCTION AS A CHORISMATE MUTASE, BIOPHYSICOCHEMICAL PROPERTIES. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]	"Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR, aro(B,E,F,H), trp(A-F), hisH, and tyrA genes." Henner D.J. Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Mutagenesis study of active site residues in chorismate mutase from Bacillus subtilis." Cload S.T., Liu D.R., Pastor R.M., Schultz P.G. J. Am. Chem. Soc. 118:1787-1788(1996) Cited for: MUTAGENESIS, BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Electrostatic catalysis of the Claisen rearrangement: probing the role of Glu78 in Bacillus subtilis chorismate mutase by genetic selection." Kast P., Hartgerink J.D., Asif-Ullah M., Hilvert D. J. Am. Chem. Soc. 118:3069-3070(1996) Cited for: MUTAGENESIS OF GLU-78.
[6]	"13C NMR studies of the enzyme-product complex of Bacillus subtilis chorismate mutase." Rajagopalan J.S., Taylor K.M., Jaffe E.K. Biochemistry 32:3965-3972(1993) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[7]	"Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog." Chook Y.M., Ke H., Lipscomb W.N. Proc. Natl. Acad. Sci. U.S.A. 90:8600-8603(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.
[8]	"The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction." Chook Y.M., Gray J.V., Ke H., Lipscomb W.N. J. Mol. Biol. 240:476-500(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
[9]	"The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer." Ladner J.E., Reddy P., Davis A., Tordova M., Howard A.J., Gilliland G.L. Acta Crystallogr. D 56:673-683(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), SUBUNIT.
[10]	"A strategically positioned cation is crucial for efficient catalysis by chorismate mutase." Kast P., Grisostomi C., Chen I.A., Li S., Krengel U., Xue Y., Hilvert D. J. Biol. Chem. 275:36832-36838(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT SER-88/LYS-90 AND LYS-88/SER-90, MUTAGENESIS OF ARG-90, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32278 Genomic DNA. Translation: AAA22249.1.
M80245 Genomic DNA. Translation: AAA20861.1.
AL009126 Genomic DNA. Translation: CAB14185.1.

PIR

A33894.

RefSeq

NP_390150.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1COM	X-ray	2.20	A/B/C/D/E/F/G/H/I/J/K/L	1-127	[»]
1DBF	X-ray	1.30	A/B/C	1-127	[»]
1FNJ	X-ray	1.90	A	1-127	[»]
1FNK	X-ray	2.00	A	1-127	[»]
2CHS	X-ray	1.90	A/B/C/D/E/F/G/H/I/J/K/L	1-127	[»]
2CHT	X-ray	2.20	A/B/C/D/E/F/G/H/I/J/K/L	1-127	[»]

ProteinModelPortal

P19080.

SMR

P19080. Positions 1-127.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU22690.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14185; CAB14185; BSU22690.

GeneID

939005.

KEGG

bsu:BSU22690.

PATRIC

18976347. VBIBacSub10457_2364.

Organism-specific databases

GenoList

BSU22690. [Micado]

Phylogenomic databases

HOGENOM

HOG000043606.

KO

K06208.

OMA

CIRVMMT.

ProtClustDB

CLSK887499.

Enzyme and pathway databases

BioCyc

BSUB:BSU22690-MONOMER.

BRENDA

5.4.99.5. 700.

SABIO-RK

P19080.

UniPathway

UPA00120; UER00203.

Family and domain databases

Gene3D

3.30.1330.40. 1 hit.

InterPro

IPR008243. Chorismate_mutase_AroH.
IPR013813. Endoribo_LPSP/chorism_mut-like.
[Graphical view]

PANTHER

PTHR21164. PTHR21164. 1 hit.

Pfam

PF07736. CM_1. 1 hit.
[Graphical view]

PIRSF

PIRSF005965. Chor_mut_AroH. 1 hit.

ProDom

PD031888. Chorismate_mutase_AroH. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF55298. YjgF/chorismate_mutase-like. 1 hit.

TIGRFAMs

TIGR01796. CM_mono_aroH. 1 hit.

PROSITE

PS51167. CHORISMATE_MUT_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P19080.

Entry information

Entry name

AROH_BACSU

Accession

Primary (citable) accession number: P19080

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	October 19, 2002
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program