Reviewed,
UniProtKB/Swiss-Prot Q9PK61 (KPYK_CHLMU)
Last modified
June 16, 2009.
Version 55.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pyruvate kinase Short name=PK EC=2.7.1.40 | ||||
| Gene names |
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| Organism | Chlamydia muridarum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83560 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia |
Protein attributes
| Sequence length | 481 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | ATP + pyruvate = ADP + phosphoenolpyruvate. |
| Cofactor | Magnesium. Potassium. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the pyruvate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW potassium ion bindingInferred from electronic annotation. Source: InterPro pyruvate kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. Fraser C.M.Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg. |
Cross-references
Sequence databases | |
|---|---|
| AE002160 Genomic DNA. Translation: AAF39440.1. | |
| PIR | F81684. |
| RefSeq | NP_296985.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1E0T based on UniProtKB P14178. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1245971. |
| GenomeReviews | Gene locus TC_0609 in contig AE002160_GR. |
| KEGG | cmu:TC0609. |
| TIGR | TC_0609. |
Phylogenomic databases | |
| HOGENOM | Q9PK61. |
| OMA | Q9PK61. DSECAVK. |
Enzyme and pathway databases | |
| BioCyc | CMUR243161:TC_0609-MON. |
| BRENDA | 2.7.1.40. 256349. |
Family and domain databases | |
| InterPro | IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. [Graphical view] |
| Gene3D | G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit. G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit. |
| PANTHER | PTHR11817. Pyruvate_kinase. 1 hit. |
| Pfam | PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view] |
| PRINTS | PR01050. PYRUVTKNASE. |
| ProDom | PD001009. Pyruvate_kinase. 2 hits. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01064. pyruv_kin. 1 hit. |
| PROSITE | PS00110. PYRUVATE_KINASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KPYK_CHLMU | ||||||||
| Accession | Primary (citable) accession number: Q9PK61 | ||||||||
| 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


