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Q8RC39 (GATB_THETN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B

Short name=Asp/Glu-ADT subunit B
EC=6.3.5.-
Gene names
Name:gatB
Ordered Locus Names:TTE0608
OrganismThermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Caldanaerobacter subterraneus subsp. tengcongensis) [Complete proteome] [HAMAP]
Taxonomic identifier273068 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCaldanaerobacter

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence similarities

Belongs to the GatB/GatE family. GatB subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_0000148859

Sequences

Sequence LengthMass (Da)Tools
Q8RC39 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: D24D52CE1C4F49F7

FASTA47553,803
        10         20         30         40         50         60 
MKYEAVIGLE VHAELLTDSK IFCGCSTKFG SEPNTQVCPV CLGLPGTLPV LNKKVVEYAV 

        70         80         90        100        110        120 
RAGLALNCTI ANFSKMDRKN YFYPDLPKAY QISQYDLPLC SNGYIEIEVE GGTKRIGIKR 

       130        140        150        160        170        180 
IHIEEDAGKL LHEGTDGSLV DYNRAGVPLI EIVSEPDIST PEEAYQYLVK LKSILEYTEV 

       190        200        210        220        230        240 
SDCKMQEGSL RVDTNVSVRP VGTTELGTKI ELKNLNSFKA VQKALEYEIK RQIKVLEEGG 

       250        260        270        280        290        300 
TIVQETRRWN EAKGITEPMR TKEEAHDYRY FPEPDLVPII VTEEWKEEIR KTLPEMPDAK 

       310        320        330        340        350        360 
RERFITQYGL PEYDAKVITS SKKMADFFEK CASNYHSPKI VSNWLMGEFA RLLNDTGKEI 

       370        380        390        400        410        420 
DEVPITPDML IELLKLVDDN VISGSIAKTV FEEMFFTGKN PQIIVEEKGL RQIADEGELR 

       430        440        450        460        470 
RIVRKVIEEN PKSVEDYKKG KEKALGFLVG QVMKETKGKA NPQLTNQLLR EELSK 

« Hide

References

[1]"A complete sequence of the T. tengcongensis genome."
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R. expand/collapse author list , Wang J., Yu J., Yang H.
Genome Res. 12:689-700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15242 / JCM 11007 / NBRC 100824 / MB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008691 Genomic DNA. Translation: AAM23878.1.
RefSeqNP_622274.1. NC_003869.1.

3D structure databases

ProteinModelPortalQ8RC39.
SMRQ8RC39. Positions 2-400.
ModBaseSearch...

Protein-protein interaction databases

STRING273068.TTE0608.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM23878; AAM23878; TTE0608.
GeneID996458.
KEGGtte:TTE0608.
PATRIC23895876. VBITheTen82880_0609.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223743.
KOK02434.
OMAKNYFYAD.
ProtClustDBPRK05477.

Family and domain databases

Gene3D1.10.10.410. 1 hit.
HAMAPMF_00121. GatB.
InterProIPR004413. 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]
PANTHERPTHR11659. PTHR11659. 1 hit.
PfamPF02934. GatB_N. 1 hit.
PF02637. GatB_Yqey. 1 hit.
[Graphical view]
SMARTSM00845. GatB_Yqey. 1 hit.
[Graphical view]
SUPFAMSSF89095. GatB_Yqey. 1 hit.
TIGRFAMsTIGR00133. gatB. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATB_THETN
AccessionPrimary (citable) accession number: Q8RC39
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families