A0R148 (PROB_MYCS2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 56.
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 | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 246196 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › ![]() |
Protein attributes
| Sequence length | 370 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
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. |
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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.3 | ||||||
| Chain | 2 – 370 | 369 | Glutamate 5-kinase HAMAP-Rule MF_00456 | PRO_1000081076 | |||||
Regions | |||||||||
| Domain | 282 – 360 | 79 | PUA | ||||||
| Nucleotide binding | 176 – 177 | 2 | ATP By similarity | ||||||
| Nucleotide binding | 220 – 226 | 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] | Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [2] | "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?" Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M. Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [3] | "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol." Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O. Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE. Strain: ATCC 700084 / mc(2)155. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000480 Genomic DNA. Translation: ABK71775.1. CP001663 Genomic DNA. Translation: AFP40959.1. |
| RefSeq | YP_006569254.1. NC_018289.1. YP_888886.1. NC_008596.1. |
3D structure databases | |
| ProteinModelPortal | A0R148. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 246196.MSMEG_4621. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABK71775; ABK71775; MSMEG_4621. |
| GeneID | 13429725. 4531097. |
| KEGG | msg:MSMEI_4505. msm:MSMEG_4621. |
| PATRIC | 18081557. VBIMycSme59918_4517. |
Phylogenomic databases | |
| eggNOG | COG0263. |
| HOGENOM | HOG000246368. |
| KO | K00931. |
| OMA | DHLQLRG. |
| ProtClustDB | PRK05429. |
Enzyme and pathway databases | |
| BioCyc | MSME246196:GJ4Y-4621-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. 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_MYCS2 | ||||||||
| Accession | Primary (citable) accession number: A0R148 Secondary accession number(s): I7GDU5 | ||||||||
| 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
