Reviewed,
UniProtKB/Swiss-Prot Q9HZ67 (PHEA_PSEAE)
Last modified
February 9, 2010.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: P-protein Including the following 2 domains: 1- Recommended name: Chorismate mutase Short name=CM EC=5.4.99.5 2- Recommended name: Prephenate dehydratase Short name=PDT EC=4.2.1.51 | ||||
| Gene names |
| ||||
| Organism | Pseudomonas aeruginosa [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 287 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 365 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Chorismate = prephenate. Prephenate = phenylpyruvate + H2O + CO2. |
| Pathway | Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Contains 1 ACT domain. Contains 1 chorismate mutase domain. Contains 1 prephenate dehydratase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Aromatic amino acid biosynthesis Phenylalanine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Isomerase Lyase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | L-phenylalanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | amino acid binding Inferred from electronic annotation. Source: InterPro chorismate mutase activityInferred from electronic annotation. Source: EC prephenate dehydratase activityInferred 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 – 365 | 365 | P-protein | PRO_0000287803 | |||||
Regions | |||||||||
| Domain | 1 – 96 | 96 | Chorismate mutase | ||||||
| Domain | 97 – 272 | 176 | Prephenate dehydratase | ||||||
| Domain | 283 – 359 | 77 | ACT | ||||||
| Region | 273 – 365 | 93 | Regulatory (Phe-binding) By similarity | ||||||
Sites | |||||||||
| Site | 265 | 1 | Essential for prephenate dehydratase activity Potential | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE004091 Genomic DNA. Translation: AAG06554.1. |
| PIR | G83250. |
| RefSeq | NP_251856.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PHZ based on UniProtKB P04176. |
| SMR | Q9HZ67. Positions 5-89, 95-363. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 882699. |
| GenomeReviews | Gene locus PA3166 in contig AE004091_GR. |
| KEGG | pae:PA3166. |
Organism-specific databases | |
| PseudoCAP | PA3166. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG693866. |
| OMA | GLGNYFF. |
Enzyme and pathway databases | |
| BioCyc | PAER208964:PA3166-MONOMER. |
| BRENDA | 4.2.1.51. 354. 5.4.99.5. 354. |
Family and domain databases | |
| InterPro | IPR002912. ACT_bd. IPR008242. Chor_mutase/pphenate_deHydtase. IPR002701. Chorismate_mutase. IPR020822. Chorismate_mutase_type_II. IPR010957. G/b/e-P-prot_chorismate_mutase. IPR001086. Preph_deHydtase. IPR018528. Preph_deHydtase_CS. [Graphical view] |
| Pfam | PF01842. ACT. 1 hit. PF01817. CM_2. 1 hit. PF00800. PDT. 1 hit. [Graphical view] |
| PIRSF | PIRSF001500. Chor_mut_pdt_Ppr. 1 hit. |
| SMART | SM00830. CM_2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01807. CM_P2. 1 hit. |
| PROSITE | PS51168. CHORISMATE_MUT_2. 1 hit. PS00857. PREPHENATE_DEHYDR_1. 1 hit. PS00858. PREPHENATE_DEHYDR_2. 1 hit. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PHEA_PSEAE | ||||||||
| Accession | Primary (citable) accession number: Q9HZ67 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


