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A1WVR6 (GATB_HALHL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 41. 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:Hhal_1002
OrganismHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) [Complete proteome] [HAMAP]
Taxonomic identifier349124 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeHalorhodospira

Protein attributes

Sequence length479 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 – 479479Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_1000015972

Sequences

Sequence LengthMass (Da)Tools
A1WVR6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 7E147F88B89920FB

FASTA47953,120
        10         20         30         40         50         60 
MKWETVIGLE IHAQLATRTK IFSGAPTAYG AEPNTQACPV DLGLPGVLPV LNREVVRMAI 

        70         80         90        100        110        120 
KFGLAVDARI APRSVFARKN YFYPDLPKGY QISQYDLPIV EGGHLDIELE DGASKRIGIT 

       130        140        150        160        170        180 
RAHLEEDAGK SLHEDFHGMT GVDLNRAGTP LMEIVSEPDL RSPAEAAAYM KKLHALVRYL 

       190        200        210        220        230        240 
EICDGNMQEG SFRCDANVSV RPVGQEAFGT RAELKNLNSF RFVERALEYE VERQIDLLES 

       250        260        270        280        290        300 
GGEVVQETRL YDVDKGVTRS MRTKEEANDY RYFPEPDLLP VEVDAALVDE VRETLPELPD 

       310        320        330        340        350        360 
EKRRRFEEEY GLPAYDAGVL TATRDMADFF EHAVSESGGF AKRTANLLMS ELLAYLNKDG 

       370        380        390        400        410        420 
LEIAESPVTP EMLGKLVARV EDETLSSRGA KDVFEAMWAG EGEPDEVIEK KGLKQVTDTS 

       430        440        450        460        470 
AIEALVDEAI ANNPQQLEQY RAGKEKLFGF FVGQVMKASG GKANPQQVNE LLKKKLDGS 

« Hide

References

[1]"Complete sequence of Halorhodospira halophila SL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 244 / SL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000544 Genomic DNA. Translation: ABM61778.1.
RefSeqYP_001002580.1. NC_008789.1.

3D structure databases

ProteinModelPortalA1WVR6.
SMRA1WVR6. Positions 2-403.
ModBaseSearch...

Protein-protein interaction databases

STRING349124.Hhal_1002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM61778; ABM61778; Hhal_1002.
GeneID4709576.
KEGGhha:Hhal_1002.
PATRIC22096311. VBIHalHal112047_0997.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223743.
KOK02434.
OMAKNYFYAD.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycHHAL349124:GI3I-1056-MONOMER.

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_HALHL
AccessionPrimary (citable) accession number: A1WVR6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 41 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