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Protein

Chorismate mutase AroH

Gene

aroH

Organism
Bacillus subtilis (strain 168)
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.1 Publication

Catalytic activityi

Chorismate = prephenate.

Kineticsi

  1. KM=67 µM for chorismate (at pH 7.5 and at 30 degrees Celsius, PubMed:10960481)3 Publications
  2. KM=87 µM for chorismate (at pH 7.5 and at 30 degrees Celsius)3 Publications
  3. KM=100 µM for chorismate (at pH 7.5 and at 30 degrees Celsius, PubMed:2105742)3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Substrate
Binding sitei90 – 901Substrate

GO - Molecular functioni

  1. chorismate mutase activity Source: UniProtKB

GO - Biological processi

  1. aromatic amino acid family biosynthetic process Source: UniProtKB-KW
  2. chorismate metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU22690-MONOMER.
BRENDAi5.4.99.5. 658.
SABIO-RKP19080.
UniPathwayiUPA00120; UER00203.

Names & Taxonomyi

Protein namesi
Recommended name:
Chorismate mutase AroH (EC:5.4.99.5)
Short name:
CM
Gene namesi
Name:aroH
Ordered Locus Names:BSU22690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU22690. [Micado]

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781E → A: No chorismate mutase activity. 1 Publication
Mutagenesisi90 – 901R → A: No chorismate mutase activity. 1 Publication
Mutagenesisi90 – 901R → G: 2-fold decrease in affinity and very low decrease in catalytic efficiency. 1 Publication
Mutagenesisi90 – 901R → K: Low decrease in catalytic efficiency and in affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Chorismate mutase AroHPRO_0000119203Add
BLAST

Interactioni

Subunit structurei

Homotrimer.3 Publications

Protein-protein interaction databases

STRINGi224308.BSU22690.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1110Combined sources
Beta strandi13 – 153Combined sources
Helixi17 – 3519Combined sources
Helixi39 – 413Combined sources
Beta strandi42 – 498Combined sources
Helixi59 – 635Combined sources
Beta strandi65 – 673Combined sources
Beta strandi73 – 775Combined sources
Beta strandi86 – 9712Combined sources
Helixi101 – 1033Combined sources
Helixi110 – 1156Combined sources
Helixi121 – 1244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP19080. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19080.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 121119Chorismate mutase aroH-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 7832Substrate bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 chorismate mutase aroH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000043606.
InParanoidiP19080.
KOiK06208.
OMAiCIRVMMT.
OrthoDBiEOG6WT8J3.
PhylomeDBiP19080.

Family and domain databases

Gene3Di3.30.1330.40. 1 hit.
InterProiIPR008243. Chorismate_mutase_AroH.
IPR013813. Endoribo_LPSP/chorism_mut-like.
[Graphical view]
PANTHERiPTHR21164. PTHR21164. 1 hit.
PfamiPF07736. CM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005965. Chor_mut_AroH. 1 hit.
ProDomiPD031888. Chorismate_mutase_AroH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55298. SSF55298. 1 hit.
TIGRFAMsiTIGR01796. CM_mono_aroH. 1 hit.
PROSITEiPS51167. CHORISMATE_MUT_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19080-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMIRGIRGAT TVERDTEEEI LQKTKQLLEK IIEENHTKPE DVVQMLLSAT
60 70 80 90 100
PDLHAVFPAK AVRELSGWQY VPVTCMQEMD VTGGLKKCIR VMMTVQTDVP
110 120
QDQIRHVYLE KVVVLRPDLS LTKNTEL
Length:127
Mass (Da):14,517
Last modified:October 18, 2002 - v2
Checksum:i5A803614FE1F402E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121V → A in AAA22249 (PubMed:2105742).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32278 Genomic DNA. Translation: AAA22249.1.
M80245 Genomic DNA. Translation: AAA20861.1.
AL009126 Genomic DNA. Translation: CAB14185.1.
PIRiA33894.
RefSeqiNP_390150.1. NC_000964.3.
WP_009967606.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14185; CAB14185; BSU22690.
GeneIDi939005.
KEGGibsu:BSU22690.
PATRICi18976347. VBIBacSub10457_2364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32278 Genomic DNA. Translation: AAA22249.1.
M80245 Genomic DNA. Translation: AAA20861.1.
AL009126 Genomic DNA. Translation: CAB14185.1.
PIRiA33894.
RefSeqiNP_390150.1. NC_000964.3.
WP_009967606.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP19080. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU22690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14185; CAB14185; BSU22690.
GeneIDi939005.
KEGGibsu:BSU22690.
PATRICi18976347. VBIBacSub10457_2364.

Organism-specific databases

GenoListiBSU22690. [Micado]

Phylogenomic databases

HOGENOMiHOG000043606.
InParanoidiP19080.
KOiK06208.
OMAiCIRVMMT.
OrthoDBiEOG6WT8J3.
PhylomeDBiP19080.

Enzyme and pathway databases

UniPathwayiUPA00120; UER00203.
BioCyciBSUB:BSU22690-MONOMER.
BRENDAi5.4.99.5. 658.
SABIO-RKP19080.

Miscellaneous databases

EvolutionaryTraceiP19080.

Family and domain databases

Gene3Di3.30.1330.40. 1 hit.
InterProiIPR008243. Chorismate_mutase_AroH.
IPR013813. Endoribo_LPSP/chorism_mut-like.
[Graphical view]
PANTHERiPTHR21164. PTHR21164. 1 hit.
PfamiPF07736. CM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005965. Chor_mut_AroH. 1 hit.
ProDomiPD031888. Chorismate_mutase_AroH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55298. SSF55298. 1 hit.
TIGRFAMsiTIGR01796. CM_mono_aroH. 1 hit.
PROSITEiPS51167. CHORISMATE_MUT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1989) [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 (DEC-1991) 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(1996) [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(1995)
    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(1995)
    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(1992) [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(1992) [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(1993) [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(1999) [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(1999) [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.

Entry informationi

Entry nameiAROH_BACSU
AccessioniPrimary (citable) accession number: P19080
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1990
Last sequence update: October 18, 2002
Last modified: March 31, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This enzyme is monofunctional, and its activity is unaffected by the end-product aromatic amino acids.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.