O53258 (GATA_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 85.
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: Glutamyl-tRNA(Gln) amidotransferase subunit A Short name=Glu-ADT subunit A EC=6.3.5.- | ||||||
| Gene names |
| ||||||
| Organism | Mycobacterium tuberculosis [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex![]() |
Protein attributes
| Sequence length | 494 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) By similarity. HAMAP-Rule MF_00120 |
| Catalytic activity | ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP-Rule MF_00120 |
| Subunit structure | Heterotrimer of A, B and C subunits By similarity. |
| Sequence similarities | Belongs to the amidase family. GatA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE translationInferred from electronic annotation. Source: HAMAP |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutaminyl-tRNA synthase (glutamine-hydrolyzing) 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 – 494 | 494 | Glutamyl-tRNA(Gln) amidotransferase subunit A HAMAP-Rule MF_00120 | PRO_0000105181 | |||||
Sites | |||||||||
| Active site | 81 | 1 | Charge relay system By similarity | ||||||
| Active site | 156 | 1 | Charge relay system By similarity | ||||||
| Active site | 180 | 1 | Acyl-ester intermediate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 420 | 1 | M → L in AAK47420. Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842581 Genomic DNA. Translation: CAA16096.1. AE000516 Genomic DNA. Translation: AAK47420.1. |
| PIR | F70856. |
| RefSeq | NP_337606.1. NC_002755.2. |
3D structure databases | |
| ProteinModelPortal | O53258. |
| SMR | O53258. Positions 9-486. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 83332.Rv3011c. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAK47420; AAK47420; MT3091. |
| GeneID | 923318. |
| KEGG | mtc:MT3091. mtu:Rv3011c. |
| PATRIC | 18128562. VBIMycTub22151_3379. |
Organism-specific databases | |
| TubercuList | Rv3011c. |
Phylogenomic databases | |
| eggNOG | COG0154. |
| HOGENOM | HOG000116699. |
| KO | K02433. |
| OMA | RYDGVKY. |
| ProtClustDB | PRK00012. |
Family and domain databases | |
| Gene3D | 3.90.1300.10. 1 hit. |
| HAMAP | MF_00120. GatA. |
| InterPro | IPR000120. Amidase. IPR020556. Amidase_CS. IPR023631. Amidase_dom. IPR004412. GatA. [Graphical view] |
| PANTHER | PTHR11895. PTHR11895. 1 hit. |
| Pfam | PF01425. Amidase. 1 hit. [Graphical view] |
| SUPFAM | SSF75304. Amidase_sig_enz. 1 hit. |
| TIGRFAMs | TIGR00132. gatA. 1 hit. |
| PROSITE | PS00571. AMIDASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GATA_MYCTU | ||||||||
| Accession | Primary (citable) accession number: O53258 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
