Reviewed, UniProtKB/Swiss-Prot P19080 (CHMU_BACSU)

Names and origin

Protein names

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

Gene names

Name:	aroH
Ordered Locus Names:	BSU22690

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	127 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Chorismate = prephenate.
Enzyme regulation	This enzyme is monofunctional, and its activity is unaffected by the end-product aromatic amino acids.
Pathway	Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subunit structure	Homotrimer.
Subcellular location	Cytoplasm.
Sequence similarities	Contains 1 chorismate mutase aroH-type domain.

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
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chorismate mutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 127

127

Chorismate mutase

PRO_0000119203

Regions

Domain

3 – 121

119

Chorismate mutase aroH-type

Experimental info

Sequence conflict

112

1

V → A in AAA22249. Ref.1

Secondary structure

1

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127

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Helix

17 – 35

19

Helix

39 – 41

3

Beta strand

42 – 49

8

Helix

59 – 63

5

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)
	P19080-1 [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: 2105742] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-35. Strain: 168 / Marburg.
[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: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"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: 8471608] [Abstract] Cited for: STRUCTURE BY NMR.
[5]	"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: 8378335] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]	"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: 8046752] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[7]	"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: 10818343] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

PIR

A33894.

RefSeq

NP_390150.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

939005.

GenomeReviews

Gene locus BSU22690 in contig AL009126_GR.

KEGG

bsu:BSU22690.

NMPDR

fig|224308.1.peg.2273.

Organism-specific databases

SubtiList

BG10286. aroH. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P19080.

OMA

P19080. HVYLRGA.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU2268-MON.

BRENDA

5.4.99.5. 150.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.30.1330.40. Endoribo_LPSP/chorism_mut-like. 1 hit.

PANTHER

PTHR21164. Chor_mut_AroH. 1 hit.

Pfam

PF07736. CM_1. 1 hit.
[Graphical view]

PIRSF

PIRSF005965. Chor_mut_AroH. 1 hit.

TIGRFAMs

TIGR01796. CM_mono_aroH. 1 hit.

PROSITE

PS51167. CHORISMATE_MUT_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CHMU_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:	June 16, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)