Q9Z9X0 (GATB_BACHD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 69.
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: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B Short name=Asp/Glu-ADT subunit B EC=6.3.5.- | ||||
| Gene names |
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| Organism | Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272558 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 476 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) By similarity. HAMAP MF_00121 |
| Catalytic activity | ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP MF_00121 ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. HAMAP MF_00121 |
| Subunit structure | Heterotrimer of A, B and C subunits By similarity. HAMAP MF_00121 |
| Sequence similarities | Belongs to the GatB/GatE family. GatB subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | translation Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-nitrogen ligase activity, with glutamine as amido-N-donorInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 476 | 476 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP MF_00121 | PRO_0000148760 | |||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequencing of three lambda clones from the genome of alkaliphilic Bacillus sp. strain C-125." Takami H., Nakasone K., Ogasawara N., Hirama C., Nakamura Y., Masui N., Fuji F., Takaki Y., Inoue A., Horikoshi K. Extremophiles 3:29-34(1999) [PubMed: 10086842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125. |
| [2] | "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB011836 Genomic DNA. Translation: BAA75312.1. BA000004 Genomic DNA. Translation: BAB04386.1. |
| PIR | T44293. |
| RefSeq | NP_241533.1. NC_002570.2. |
3D structure databases | |
| ProteinModelPortal | Q9Z9X0. |
| SMR | Q9Z9X0. Positions 2-412. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000052034; EBBACP00000050673; EBBACG00000052025. |
| GeneID | 893061. |
| GenomeReviews | Gene locus BH0667 in contig BA000004_GR. |
| KEGG | bha:BH0667. |
| NMPDR | fig|272558.1.peg.667. |
| PATRIC | 18938322. VBIBacHal18977_0699. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000002603. |
| HOGENOM | HBG395951. |
| OMA | KNYFYAD. |
| PhylomeDB | Q9Z9X0. |
| ProtClustDB | PRK05477. |
Enzyme and pathway databases | |
| BioCyc | BHAL272558:BH0667-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00121. GatB. [Tree] |
| InterPro | IPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E. IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat. IPR018027. Asn/Gln_amidotransferase. IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel. IPR004413. Gln-tRNA_amidoTrfase_bsu. IPR017958. Gln-tRNA_amidoTrfase_suB_CS. [Graphical view] |
| KO | K02434. |
| PANTHER | PTHR11659. GatB. 1 hit. |
| Pfam | PF02934. GatB_N. 1 hit. PF02637. GatB_Yqey. 1 hit. [Graphical view] |
| SMART | SM00845. GatB_Yqey. 1 hit. [Graphical view] |
| SUPFAM | SSF89095. GatB_Yqey. 1 hit. |
| TIGRFAMs | TIGR00133. GatB. 1 hit. |
| PROSITE | PS01234. GATB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GATB_BACHD | ||||||||
| Accession | Primary (citable) accession number: Q9Z9X0 Secondary accession number(s): Q9JPV7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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