Reviewed,
UniProtKB/Swiss-Prot O54457 (PPSA_ENTAG)
Last modified
June 16, 2009.
Version 45.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (2) |
 Third-party data |
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Names and origin
| Protein names | Recommended name: Phosphoenolpyruvate synthase Short name=PEP synthase EC=2.7.9.2 Alternative name(s): Pyruvate, water dikinase | ||
| Gene names |
| ||
| Organism | Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans) | ||
| Taxonomic identifier | 549 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pantoea |
Protein attributes
| Sequence length | 61 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate By similarity. |
| Catalytic activity | ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate. |
| Cofactor | Magnesium By similarity. |
| Pathway | |
| Domain | The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity. |
| Miscellaneous | The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity. |
| Sequence similarities | Belongs to the PEP-utilizing enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | phosphorylation Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW pyruvate, water dikinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases." Subramaniam P.S., Xie G., Xia T., Jensen R.A. J. Bacteriol. 180:119-127(1998) [PubMed: 9422601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| U93355 Genomic DNA. Translation: AAB96398.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.7.9.2. 3054. |
Family and domain databases | |
| InterPro | IPR013815. ATP_grasp_subdomain_1. IPR018274. PEP_mobile_CS. IPR000121. PEP_utilizers. IPR002192. PPDK_PEP_bd. [Graphical view] |
| Gene3D | G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. |
| Pfam | PF01326. PPDK_N. 1 hit. [Graphical view] |
| PROSITE | PS00742. PEP_ENZYMES_2. Partial match. PS00370. PEP_ENZYMES_PHOS_SITE. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PPSA_ENTAG | ||||||||
| Accession | Primary (citable) accession number: O54457 | ||||||||
| Entry history |
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| 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 |
