Reviewed,
UniProtKB/Swiss-Prot O29548 (PPSA_ARCFU)
Last modified
November 3, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 | Archaeoglobus fulgidus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2234 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus |
Protein attributes
| Sequence length | 753 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 – 753 | 753 | Probable phosphoenolpyruvate synthase | PRO_0000147041 | |||||
Sites | |||||||||
| Active site | 398 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 703 | 1 | Proton donor By similarity | ||||||
| Metal binding | 631 | 1 | Magnesium By similarity | ||||||
| Metal binding | 656 | 1 | Magnesium By similarity | ||||||
| Binding site | 488 | 1 | Substrate By similarity | ||||||
| Binding site | 535 | 1 | Substrate By similarity | ||||||
| Binding site | 631 | 1 | Substrate By similarity | ||||||
| Binding site | 653 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 654 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 655 | 1 | Substrate By similarity | ||||||
| Binding site | 656 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. Venter J.C.Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126. |
Cross-references
Sequence databases | |
|---|---|
| AE000782 Genomic DNA. Translation: AAB90532.1. | |
| PIR | F69338. |
| RefSeq | NP_069544.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1H6Z based on UniProtKB O76283. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1483928. |
| GenomeReviews | Gene locus AF_0710 in contig AE000782_GR. |
| KEGG | afu:AF0710. |
| NMPDR | fig|224325.1.peg.703. |
| TIGR | AF_0710. |
Phylogenomic databases | |
| HOGENOM | O29548. |
| OMA | RAEHMIL. |
Enzyme and pathway databases | |
| BioCyc | AFUL224325:AF_0710-MON. |
| BRENDA | 2.7.9.2. 7576. |
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. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view] |
| Gene3D | G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 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_ARCFU | ||||||||
| Accession | Primary (citable) accession number: O29548 | ||||||||
| 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 |

Clusters with


