Q8P8K2 (PROB_XANCP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 72.
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 |
| ||||
| Organism | Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 190485 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › ![]() |
Protein attributes
| Sequence length | 362 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 HAMAP-Rule MF_00456. |
| Sequence similarities | Belongs to the glutamate 5-kinase family. Contains 1 PUA domain. |
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 |
| 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 electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 362 | 362 | Glutamate 5-kinase HAMAP-Rule MF_00456 | PRO_0000109758 | |||||
Regions | |||||||||
| Domain | 267 – 348 | 82 | PUA | ||||||
| Nucleotide binding | 160 – 161 | 2 | ATP By similarity | ||||||
| Nucleotide binding | 202 – 208 | 7 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 3 | 1 | ATP By similarity | ||||||
| Binding site | 43 | 1 | Substrate By similarity | ||||||
| Binding site | 128 | 1 | Substrate By similarity | ||||||
| Binding site | 140 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. Kitajima J.P.Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE008922 Genomic DNA. Translation: AAM41518.1. |
| RefSeq | NP_637594.2. NC_003902.1. |
3D structure databases | |
| ProteinModelPortal | Q8P8K2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 190485.XCC2239. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAM41518; AAM41518; XCC2239. |
| GeneID | 998826. |
| KEGG | xcc:XCC2239. |
| PATRIC | 24075383. VBIXanCam115730_2389. |
Phylogenomic databases | |
| eggNOG | COG0263. |
| HOGENOM | HOG000246368. |
| KO | K00931. |
| OMA | DHLQLRG. |
| ProtClustDB | PRK05429. |
Enzyme and pathway databases | |
| BioCyc | XCAM190485:GIXZ-2237-MONOMER. |
| UniPathway | UPA00098; UER00359. |
Family and domain databases | |
| Gene3D | 2.30.130.10. 1 hit. 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_XANCP | ||||||||
| Accession | Primary (citable) accession number: Q8P8K2 | ||||||||
| Entry history |
| ||||||||
| 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
