Q9KPT8 (PROB_VIBCH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 76.
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: Glutamate 5-kinase EC=2.7.2.11 Alternative name(s): Gamma-glutamyl kinase Short name=GK | ||||
| Gene names |
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| Organism | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 243277 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › ![]() |
Protein attributes
| Sequence length | 377 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline By similarity. HAMAP-Rule MF_00456 |
| Catalytic activity | ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP-Rule MF_00456 |
| Pathway | Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP-Rule MF_00456 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the glutamate 5-kinase family. Contains 1 PUA domain. |
| Sequence caution | The sequence AAF95418.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Proline biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway proline biosynthetic processInferred from sequence or structural similarity Ref.1. Source: TIGR |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA bindingInferred from electronic annotation. Source: InterPro glutamate 5-kinase activityInferred from sequence or structural similarity Ref.1. Source: TIGR |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 377 | 377 | Glutamate 5-kinase HAMAP-Rule MF_00456 | PRO_0000109751 | |||||
Regions | |||||||||
| Domain | 283 – 361 | 79 | PUA | ||||||
| Nucleotide binding | 176 – 177 | 2 | ATP By similarity | ||||||
| Nucleotide binding | 218 – 224 | 7 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 17 | 1 | ATP By similarity | ||||||
| Binding site | 57 | 1 | Substrate By similarity | ||||||
| Binding site | 144 | 1 | Substrate By similarity | ||||||
| Binding site | 156 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. Fraser C.M.Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE003852 Genomic DNA. Translation: AAF95418.1. Different initiation. |
| PIR | F82095. |
| RefSeq | NP_231905.2. NC_002505.1. |
3D structure databases | |
| ProteinModelPortal | Q9KPT8. |
| SMR | Q9KPT8. Positions 12-373. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 243277.VC2274. |
Protocols and materials databases | |
| DNASU | 2613196. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAF95418; AAF95418; VC_2274. |
| GeneID | 2613196. |
| KEGG | vch:VC2274. |
| PATRIC | 20083589. VBIVibCho83274_2169. |
Phylogenomic databases | |
| eggNOG | COG0263. |
| KO | K00931. |
| OMA | DHLQLRG. |
| ProtClustDB | PRK05429. |
Enzyme and pathway databases | |
| UniPathway | UPA00098; UER00359. |
Family and domain databases | |
| Gene3D | 3.40.1160.10. 1 hit. |
| HAMAP | MF_00456. ProB. |
| InterPro | IPR001048. Asp/Glu/Uridylate_kinase. IPR001057. Glu/AcGlu_kinase. IPR011529. Glu_5kinase. IPR005715. Glu_5kinase/COase_Synthase. IPR019797. Glutamate_5-kinase_CS. IPR002478. PUA. IPR015947. PUA-like_domain. [Graphical view] |
| Pfam | PF00696. AA_kinase. 1 hit. PF01472. PUA. 1 hit. [Graphical view] |
| PIRSF | PIRSF000729. GK. 1 hit. |
| PRINTS | PR00474. GLU5KINASE. |
| SMART | SM00359. PUA. 1 hit. [Graphical view] |
| SUPFAM | SSF53633. Aa_kinase. 1 hit. SSF88697. PUA-like. 1 hit. |
| TIGRFAMs | TIGR01027. proB. 1 hit. |
| PROSITE | PS00902. GLUTAMATE_5_KINASE. 1 hit. PS50890. PUA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PROB_VIBCH | ||||||||
| Accession | Primary (citable) accession number: Q9KPT8 | ||||||||
| 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
