Reviewed,
UniProtKB/Swiss-Prot Q9ZMV4 (PPSA_HELPJ)
Last modified
November 3, 2009.
Version 61.
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 |
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| Organism | Helicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 85963 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter |
Protein attributes
| Sequence length | 812 AA. |
| Sequence status | Complete. |
| 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 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from electronic annotation. Source: InterPro phosphorylationInferred 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 812 | 812 | Phosphoenolpyruvate synthase | PRO_0000147037 | |||||
Sites | |||||||||
| Active site | 430 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 761 | 1 | Proton donor By similarity | ||||||
| Metal binding | 690 | 1 | Magnesium By similarity | ||||||
| Metal binding | 714 | 1 | Magnesium By similarity | ||||||
| Binding site | 520 | 1 | Substrate By similarity | ||||||
| Binding site | 588 | 1 | Substrate By similarity | ||||||
| Binding site | 690 | 1 | Substrate By similarity | ||||||
| Binding site | 711 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 712 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 713 | 1 | Substrate By similarity | ||||||
| Binding site | 714 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. Trust T.J.Nature 397:176-180(1999) [PubMed: 9923682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AE001439 Genomic DNA. Translation: AAD05690.1. | |
| PIR | E71972. |
| RefSeq | NP_222832.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1H6Z based on UniProtKB O76283. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9ZMV4. |
Genome annotation databases | |
| GeneID | 889485. |
| GenomeReviews | Gene locus jhp_0111 in contig AE001439_GR. |
| KEGG | hpj:jhp0111. |
| NMPDR | fig|85963.1.peg.110. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9ZMV4. |
| OMA | NKYVGIC. |
Enzyme and pathway databases | |
| BioCyc | HPYL85963:JHP0111-MON. |
| BRENDA | 2.7.9.2. 295085. |
Family and domain databases | |
| InterPro | IPR013815. ATP_grasp_subdomain_1. IPR008279. PEP_mobile. IPR018274. PEP_mobile_CS. IPR006318. PEP_P_trans. IPR006319. PEP_synth. IPR000121. PEP_utilizers. IPR002192. PPDK_PEP_bd. [Graphical view] |
| Gene3D | G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. |
| Pfam | PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF01326. PPDK_N. 1 hit. [Graphical view] |
| PRINTS | PR01736. PHPHTRNFRASE. |
| ProDom | PD000940. PEP_utilizers. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| 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_HELPJ | ||||||||
| Accession | Primary (citable) accession number: Q9ZMV4 | ||||||||
| 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 |

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