Q9HHA0 (PROB_METAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 86.
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 | Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 188937 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina › ![]() |
Protein attributes
| Sequence length | 385 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. |
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 – 385 | 385 | Glutamate 5-kinase HAMAP-Rule MF_00456 | PRO_0000109765 | |||||
Regions | |||||||||
| Domain | 291 – 367 | 77 | PUA | ||||||
| Nucleotide binding | 185 – 186 | 2 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 17 | 1 | ATP By similarity | ||||||
| Binding site | 64 | 1 | Substrate By similarity | ||||||
| Binding site | 151 | 1 | Substrate By similarity | ||||||
| Binding site | 165 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Directed mutagenesis and plasmid-based complementation in the methanogenic archaeon Methanosarcina acetivorans C2A demonstrated by genetic analysis of proline biosynthesis." Zhang J.K., White A.K., Kuettner H.C., Boccazzi P., Metcalf W.W. J. Bacteriol. 184:1449-1454(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A. |
| [2] | "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. Birren B.Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF305580 Genomic DNA. Translation: AAG22032.1. AE010299 Genomic DNA. Translation: AAM07449.1. |
| RefSeq | NP_618969.1. NC_003552.1. |
3D structure databases | |
| ProteinModelPortal | Q9HHA0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 188937.MA4101. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAM07449; AAM07449; MA_4101. |
| GeneID | 1475995. |
| KEGG | mac:MA4101. |
Phylogenomic databases | |
| eggNOG | COG0263. |
| KO | K00931. |
| OMA | DHLQLRG. |
| ProtClustDB | PRK05429. |
Enzyme and pathway databases | |
| BioCyc | MACE188937:GI2O-4166-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_METAC | ||||||||
| Accession | Primary (citable) accession number: Q9HHA0 | ||||||||
| 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
