Q99YJ7 (PROB_STRP1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 79.
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 | Streptococcus pyogenes serotype M1 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 301447 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › ![]() |
Protein attributes
| Sequence length | 273 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. |
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 |
| 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 | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 273 | 273 | Glutamate 5-kinase HAMAP-Rule MF_00456 | PRO_0000109734 | |||||
Regions | |||||||||
| Nucleotide binding | 178 – 179 | 2 | ATP By similarity | ||||||
| Nucleotide binding | 220 – 226 | 7 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 15 | 1 | ATP By similarity | ||||||
| Binding site | 55 | 1 | Substrate By similarity | ||||||
| Binding site | 142 | 1 | Substrate By similarity | ||||||
| Binding site | 158 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of an M1 strain of Streptococcus pyogenes." Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. McLaughlin R.E.Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700294 / SF370 / Serotype M1. |
| [2] | "Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events." Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M. J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-947 / MGAS5005 / Serotype M1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE004092 Genomic DNA. Translation: AAK34430.1. CP000017 Genomic DNA. Translation: AAZ51989.1. |
| RefSeq | NP_269709.1. NC_002737.1. YP_282734.1. NC_007297.1. |
3D structure databases | |
| ProteinModelPortal | Q99YJ7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 160490.SPy_1672. |
Proteomic databases | |
| PaxDb | Q99YJ7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAK34430; AAK34430; SPy_1672. AAZ51989; AAZ51989; M5005_Spy1371. |
| GeneID | 3571525. 901919. |
| KEGG | spy:SPy_1672. spz:M5005_Spy_1371. |
| PATRIC | 19716806. VBIStrPyo79812_1455. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0263. |
| HOGENOM | HOG000246368. |
| KO | K00931. |
| OMA | VYTGNPK. |
| ProtClustDB | PRK12314. |
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. [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 | PROB_STRP1 | ||||||||
| Accession | Primary (citable) accession number: Q99YJ7 Secondary accession number(s): Q48XD6 | ||||||||
| 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
