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P19080 (AROH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chorismate mutase AroH

Short name=CM
EC=5.4.99.5
Gene names
Name:aroH
Ordered Locus Names:BSU22690
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaromatic amino acid family biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

chorismate metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchorismate mutase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 127127Chorismate mutase AroH
PRO_0000119203

Regions

Domain3 – 121119Chorismate mutase aroH-type
Region47 – 7832Substrate binding By similarity

Sites

Binding site71Substrate
Binding site901Substrate

Experimental info

Mutagenesis781E → A: No chorismate mutase activity. Ref.5
Mutagenesis901R → A: No chorismate mutase activity. Ref.10
Mutagenesis901R → G: 2-fold decrease in affinity and very low decrease in catalytic efficiency. Ref.10
Mutagenesis901R → K: Low decrease in catalytic efficiency and in affinity. Ref.10
Sequence conflict1121V → A in AAA22249. Ref.1

Secondary structure

........................ 127
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19080 [UniParc].

Last modified October 19, 2002. Version 2.
Checksum: 5A803614FE1F402E

FASTA12714,517
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.

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.
PIRA33894.
RefSeqNP_390150.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1COMX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
1DBFX-ray1.30A/B/C1-127[»]
1FNJX-ray1.90A1-127[»]
1FNKX-ray2.00A1-127[»]
2CHSX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
2CHTX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
3ZO8X-ray1.59A/B/C/D/E/F1-127[»]
3ZOPX-ray1.61A/B/C/D/E/F1-127[»]
3ZP4X-ray1.80A/B/C/D/E/F1-127[»]
3ZP7X-ray1.70A/B/C/D/E/F1-127[»]
ProteinModelPortalP19080.
SMRP19080. Positions 1-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU22690.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14185; CAB14185; BSU22690.
GeneID939005.
KEGGbsu:BSU22690.
PATRIC18976347. VBIBacSub10457_2364.

Organism-specific databases

GenoListBSU22690. [Micado]

Phylogenomic databases

HOGENOMHOG000043606.
KOK06208.
OMAGWTYVPV.
OrthoDBEOG6WT8J3.
PhylomeDBP19080.

Enzyme and pathway databases

BioCycBSUB:BSU22690-MONOMER.
BRENDA5.4.99.5. 700.
SABIO-RKP19080.
UniPathwayUPA00120; UER00203.

Family and domain databases

Gene3D3.30.1330.40. 1 hit.
InterProIPR008243. Chorismate_mutase_AroH.
IPR013813. Endoribo_LPSP/chorism_mut-like.
[Graphical view]
PANTHERPTHR21164. PTHR21164. 1 hit.
PfamPF07736. CM_1. 1 hit.
[Graphical view]
PIRSFPIRSF005965. Chor_mut_AroH. 1 hit.
ProDomPD031888. Chorismate_mutase_AroH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF55298. SSF55298. 1 hit.
TIGRFAMsTIGR01796. CM_mono_aroH. 1 hit.
PROSITEPS51167. CHORISMATE_MUT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19080.

Entry information

Entry nameAROH_BACSU
AccessionPrimary (citable) accession number: P19080
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 19, 2002
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList