P46893 (PPSA_STAMF) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 87.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable phosphoenolpyruvate synthase Short name=PEP synthase EC=2.7.9.2 Alternative name(s): Pyruvate, water dikinase | ||||
| Gene names |
| ||||
| Organism | Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 399550 [NCBI] | ||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Staphylothermus › ![]() |
Protein attributes
| Sequence length | 834 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 | |
| Subunit structure | Homooligomer. Forms a large complex of about 2000 kDa. |
| 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. |
| Post-translational modification | The N-terminus is blocked. |
| 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 Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-UniPathway pyruvate metabolic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal 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 – 834 | 834 | Probable phosphoenolpyruvate synthase | PRO_0000147038 | |||||
Sites | |||||||||
| Active site | 447 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 772 | 1 | Proton donor By similarity | ||||||
| Metal binding | 699 | 1 | Magnesium By similarity | ||||||
| Metal binding | 723 | 1 | Magnesium By similarity | ||||||
| Binding site | 550 | 1 | Substrate By similarity | ||||||
| Binding site | 598 | 1 | Substrate By similarity | ||||||
| Binding site | 699 | 1 | Substrate By similarity | ||||||
| Binding site | 720 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 721 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 722 | 1 | Substrate By similarity | ||||||
| Binding site | 723 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary structure of a multimeric protein, homologous to the PEP-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium." Cicicopol C., Peters J., Kellermann J., Baumeister W. FEBS Lett. 356:345-350(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 296-320; 528-546; 625-636; 638-647; 657-661; 682-694; 698-720 AND 742-752. |
| [2] | "The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota." Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N. BMC Genomics 10:145-145(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43588 / DSM 3639 / F1. |
| [3] | "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1." Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C. Stand. Genomic Sci. 1:183-188(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43588 / DSM 3639 / F1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | S74619 Genomic DNA. Translation: AAB32888.1. CP000575 Genomic DNA. Translation: ABN69254.1. |
| PIR | S51006. |
| RefSeq | YP_001040162.1. NC_009033.1. |
3D structure databases | |
| ProteinModelPortal | P46893. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 399550.Smar_0141. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABN69254; ABN69254; Smar_0141. |
| GeneID | 4907183. |
| KEGG | smr:Smar_0141. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0574. |
| HOGENOM | HOG000230912. |
| KO | K01007. |
| OMA | NVMERYL. |
| ProtClustDB | PRK06464. |
Enzyme and pathway databases | |
| BioCyc | SMAR399550:GHK2-186-MONOMER. |
| UniPathway | UPA00138. |
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. [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_STAMF | ||||||||
| Accession | Primary (citable) accession number: P46893 Secondary accession number(s): A3DKU4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
