P23538 (PPSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 117.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 792 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. Ref.7 |
| Catalytic activity | ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate. Ref.6 Ref.7 |
| Cofactor | Magnesium. Ref.7 |
| Enzyme regulation | Activated by a Pi-dependent pyrophosphorylation and inactivated by an ADP-dependent phosphorylation on a regulatory threonine. Both reactions are mediated by the bifunctional serine/threonine kinase and phosphorylase PpsR. Ref.10 |
| Pathway | |
| Subunit structure | Homodimer. Ref.8 |
| 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. |
| Biophysicochemical properties | Kinetic parameters: KM=0.083 mM for pyruvate Ref.7 KM=0.028 mM for ATP KM=10.4 mM for phosphate |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | gluconeogenesis Inferred from mutant phenotype PubMed 4383555. Source: EcoCyc pyruvate metabolic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from direct assay PubMed 4383554. Source: EcoCyc pyruvate, water dikinase activityInferred from direct assay PubMed 4383554. Source: EcoCyc |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| rplB | P60422 | 1 | EBI-1114517,EBI-543515 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 792 | 791 | Phosphoenolpyruvate synthase | PRO_0000147034 | |||||
Sites | |||||||||
| Active site | 421 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 751 | 1 | Proton donor By similarity | ||||||
| Metal binding | 680 | 1 | Magnesium By similarity | ||||||
| Metal binding | 704 | 1 | Magnesium By similarity | ||||||
| Binding site | 511 | 1 | Substrate By similarity | ||||||
| Binding site | 578 | 1 | Substrate By similarity | ||||||
| Binding site | 680 | 1 | Substrate By similarity | ||||||
| Binding site | 701 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 702 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 703 | 1 | Substrate By similarity | ||||||
| Binding site | 704 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 194 – 195 | 2 | RM → AGL in AAA24319. Ref.1 | ||||||
| Sequence conflict | 341 – 360 | 20 | RSRGQ…GKIIA → AHAVRSWSVIRCIHRVRLSP in AAA24319. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The cloning and sequence of the E. coli pps gene." Holzschu D.L., McElver J.A., Liao C.C., Berry A. Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase." Niersbach M., Kreuzaler F., Geerse R.H., Postma P.W., Hirsch H.J. Mol. Gen. Genet. 231:332-336(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21. Strain: K12. |
| [3] | "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T.DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [6] | "The mechanism of the phosphoenolpyruvate synthase reaction." Cooper R.A., Kornberg H.L. Biochim. Biophys. Acta 141:211-213(1967) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY. |
| [7] | "Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions." Berman K.M., Cohn M. J. Biol. Chem. 245:5309-5318(1970) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. |
| [8] | "Phosphoenolypyruvate synthetase of Escherichia coli: molecular weight, subunit composition, and identification of phosphohistidine in phosphoenzyme intermediate." Narindrasorasak S., Bridger W.A. J. Biol. Chem. 252:3121-3127(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHOINTERMEDIATE OF REACTION, SUBUNIT, AMINO-ACID COMPOSITION. |
| [9] | "Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL. |
| [10] | "Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria." Burnell J.N. BMC Biochem. 11:1-1(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M69116 Genomic DNA. Translation: AAA24319.1. X59381 Genomic DNA. Translation: CAA42024.1. U00096 Genomic DNA. Translation: AAC74772.1. AP009048 Genomic DNA. Translation: BAA15471.1. |
| PIR | S20554. |
| RefSeq | NP_416217.1. NC_000913.2. YP_489964.1. NC_007779.1. |
3D structure databases | |
| ProteinModelPortal | P23538. |
| SMR | P23538. Positions 10-788. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-10552N. |
| IntAct | P23538. 6 interactions. |
| STRING | 511145.b1702. |
PTM databases | |
| PhosSite | P0810424. |
2D gel databases | |
| SWISS-2DPAGE | P23538. |
Proteomic databases | |
| PaxDb | P23538. |
| PRIDE | P23538. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC74772; AAC74772; b1702. BAA15471; BAA15471; BAA15471. |
| GeneID | 12933090. 946209. |
| KEGG | ecj:Y75_p1677. eco:b1702. |
| PATRIC | 32118710. VBIEscCol129921_1773. |
Organism-specific databases | |
| EchoBASE | EB0752. |
| EcoGene | EG10759. pps. |
Phylogenomic databases | |
| eggNOG | COG0574. |
| HOGENOM | HOG000230913. |
| KO | K01007. |
| OMA | NVMERYL. |
| ProtClustDB | PRK06464. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:PEPSYNTH-MONOMER. ECOL316407:JW1692-MONOMER. MetaCyc:PEPSYNTH-MONOMER. |
| BRENDA | 2.7.9.2. 2026. |
| SABIO-RK | P23538. |
| UniPathway | UPA00138. |
Gene expression databases | |
| Genevestigator | P23538. |
Family and domain databases | |
| Gene3D | 3.20.20.60. 1 hit. 3.30.1490.20. 1 hit. 3.30.470.20. 1 hit. |
| InterPro | IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR008279. PEP-util_enz_mobile_dom. IPR006319. PEP_synth. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR002192. PPDK_PEP-bd. IPR015813. Pyrv/PenolPyrv_Kinase-like_dom. [Graphical view] |
| Pfam | PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF01326. PPDK_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000854. PEP_synthase. 1 hit. |
| SUPFAM | SSF52009. PEP_mobile. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| TIGRFAMs | TIGR01418. PEP_synth. 1 hit. |
| PROSITE | PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PPSA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P23538 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
