Reviewed,
UniProtKB/Swiss-Prot P19080 (CHMU_BACSU)
Last modified
June 16, 2009.
Version 85.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Chorismate mutase Short name=CM EC=5.4.99.5 | ||||
| Gene names |
| ||||
| 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 | |
| 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 | ||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||
| 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
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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: 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. 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 | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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 | |||||||||||||||||||||||||||||||||||||||||||
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| 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 |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


