Q3KN18 (GATB_CHLTA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 50.
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 | Chlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 315277 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia › ![]() |
Protein attributes
| Sequence length | 488 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-Rule MF_00121 |
| Catalytic activity | ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP-Rule MF_00121 ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. HAMAP-Rule MF_00121 |
| Subunit structure | Heterotrimer of A, B and C subunits By similarity. HAMAP-Rule 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 – 488 | 488 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121 | PRO_0000241208 | |||
Sequences
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References
| [1] | "Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains." Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D. Infect. Immun. 73:6407-6418(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HAR-13 / ATCC VR-571B. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000051 Genomic DNA. Translation: AAX50254.1. |
| RefSeq | YP_327802.1. NC_007429.1. |
3D structure databases | |
| ProteinModelPortal | Q3KN18. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 315277.CTA_0005. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAX50254; AAX50254; CTA_0005. |
| GeneID | 3688099. |
| KEGG | cta:CTA_0005. |
| PATRIC | 32021852. VBIChlTra31516_0007. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0064. |
| HOGENOM | HOG000223742. |
| KO | K02434. |
| OMA | KNYFYAD. |
| ProtClustDB | PRK05477. |
Enzyme and pathway databases | |
| BioCyc | CTRA315277:GI4C-5-MONOMER. |
Family and domain databases | |
| Gene3D | 1.10.10.410. 1 hit. |
| HAMAP | MF_00121. GatB. |
| InterPro | IPR004413. Apn/Gln-ADT_bsu. 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. IPR023168. GatB_Yqey_C. IPR017958. Gln-tRNA_amidoTrfase_suB_CS. [Graphical view] |
| PANTHER | PTHR11659. PTHR11659. 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_CHLTA | ||||||||
| Accession | Primary (citable) accession number: Q3KN18 | ||||||||
| 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 |

Clusters with
