O05118 (KPYK_METEA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 75.
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: Pyruvate kinase Short name=PK EC=2.7.1.40 | ||||||
| Gene names |
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| Organism | Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 272630 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium › ![]() |
Protein attributes
| Sequence length | 478 AA. |
| Sequence status | Complete. |
| 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. |
| Sequence caution | The sequence AAB66498.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: InterPro potassium ion bindingInferred from electronic annotation. Source: InterPro pyruvate kinase 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 – 478 | 478 | Pyruvate kinase | PRO_0000112078 | |||||
Sites | |||||||||
| Metal binding | 37 | 1 | Potassium By similarity | ||||||
| Metal binding | 39 | 1 | Potassium By similarity | ||||||
| Metal binding | 69 | 1 | Potassium By similarity | ||||||
| Metal binding | 219 | 1 | Magnesium By similarity | ||||||
| Metal binding | 243 | 1 | Magnesium By similarity | ||||||
| Binding site | 35 | 1 | Substrate By similarity | ||||||
| Binding site | 242 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 243 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 275 | 1 | Substrate By similarity | ||||||
| Site | 217 | 1 | Transition state stabilizer By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 60 | 1 | A → G in AAB66498. Ref.1 | ||||||
| Sequence conflict | 165 | 1 | V → A in AAB66498. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Chistoserdova L., Lidstrom M.E. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources." Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. Lidstrom M.E.PLoS ONE 4:E5584-E5584(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14718 / DSM 1338 / AM1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U87316 Genomic DNA. Translation: AAB66498.1. Different initiation. CP001510 Genomic DNA. Translation: ACS40693.1. |
| RefSeq | YP_002963970.1. NC_012808.1. |
3D structure databases | |
| ProteinModelPortal | O05118. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACS40693; ACS40693; MexAM1_META1p2941. |
| GeneID | 7992827. |
| KEGG | mea:Mex_1p2941. |
| PATRIC | 22511616. VBIMetExt101010_2874. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0469. |
| HOGENOM | HOG000021558. |
| KO | K00873. |
| OMA | SSISFRR. |
| ProtClustDB | CLSK2331328. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00188. |
Family and domain databases | |
| Gene3D | 2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit. |
| InterPro | IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. IPR011037. Pyrv_Knase-like_insert_dom. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. IPR015795. Pyrv_Knase_C. IPR015806. Pyrv_Knase_insert_dom. [Graphical view] |
| PANTHER | PTHR11817. PTHR11817. 1 hit. |
| Pfam | PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view] |
| PRINTS | PR01050. PYRUVTKNASE. |
| SUPFAM | SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| TIGRFAMs | TIGR01064. pyruv_kin. 1 hit. |
| PROSITE | PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KPYK_METEA | ||||||||
| Accession | Primary (citable) accession number: O05118 Secondary accession number(s): C5AUT3 | ||||||||
| 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
