D2P4H0 (D2P4H0_LISM2) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 24.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Glutamate 5-kinase HAMAP-Rule MF_00456 EC=2.7.2.11 HAMAP-Rule MF_00456 Alternative name(s): Gamma-glutamyl kinase HAMAP-Rule MF_00456 | ||||
| Gene names |
| ||||
| Organism | Listeria monocytogenes serotype 1/2a (strain 08-5923) [Complete proteome] [HAMAP] EMBL ADB71193.1 | ||||
| Taxonomic identifier | 637381 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › ![]() |
Protein attributes
| Sequence length | 276 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 SAAS SAAS011529 |
| 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 SAAS SAAS011529 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00456 SAAS SAAS011529. |
| Sequence similarities | Belongs to the glutamate 5-kinase family. HAMAP-Rule MF_00456 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Proline biosynthesis HAMAP-Rule MF_00456 SAAS SAAS011529 |
| Cellular component | Cytoplasm HAMAP-Rule MF_00456 SAAS SAAS011529 |
| Ligand | ATP-binding HAMAP-Rule MF_00456 SAAS SAAS011529 Nucleotide-binding |
| Molecular function | Kinase HAMAP-Rule MF_00456 SAAS SAAS011529 EMBL ADB71193.1 Transferase |
| Technical term | Complete 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 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 | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 177 – 178 | 2 | ATP By similarity HAMAP-Rule MF_00456 | ||||||
| Nucleotide binding | 219 – 225 | 7 | ATP By similarity HAMAP-Rule MF_00456 | ||||||
Sites | |||||||||
| Binding site | 14 | 1 | ATP By similarity HAMAP-Rule MF_00456 | ||||||
| Binding site | 54 | 1 | Substrate By similarity HAMAP-Rule MF_00456 | ||||||
| Binding site | 141 | 1 | Substrate By similarity HAMAP-Rule MF_00456 | ||||||
| Binding site | 157 | 1 | Substrate; via amide nitrogen By similarity HAMAP-Rule MF_00456 | ||||||
Sequences
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References
| [1] | "High-throughput genome sequencing of two Listeria monocytogenes clinical isolates during a large foodborne outbreak." Gilmour M.W., Graham M., Van Domselaar G., Tyler S., Kent H., Trout-Yakel K.M., Larios O., Allen V., Lee B., Nadon C. BMC Genomics 11:120-120(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 08-5923 EMBL ADB71193.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001604 Genomic DNA. Translation: ADB71193.1. |
| RefSeq | YP_003416555.1. NC_013768.1. |
3D structure databases | |
| ProteinModelPortal | D2P4H0. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADB71193; ADB71193; LM5923_1351. |
| GeneID | 8758146. |
| KEGG | lmy:LM5923_1351. |
| PATRIC | 32256474. VBILisMon5116_1366. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000246368. |
| KO | K00931. |
| OMA | VYTGNPK. |
Enzyme and pathway databases | |
| BioCyc | LMON637381:GH7Z-1348-MONOMER. |
| 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. [Graphical view] |
| Pfam | PF00696. AA_kinase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000729. GK. 1 hit. |
| PRINTS | PR00474. GLU5KINASE. |
| SUPFAM | SSF53633. Aa_kinase. 1 hit. |
| TIGRFAMs | TIGR01027. proB. 1 hit. |
| PROSITE | PS00902. GLUTAMATE_5_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | D2P4H0_LISM2 | ||||||||
| Accession | Primary (citable) accession number: D2P4H0 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
