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Q2YKL3 (GATA_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit A

Short name=Glu-ADT subunit A
EC=6.3.5.7
Gene names
Name:gatA
Ordered Locus Names:BAB2_0646
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_00120

Sequence similarities

Belongs to the amidase family. GatA 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: UniProtKB-HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Glutamyl-tRNA(Gln) amidotransferase subunit A HAMAP-Rule MF_00120
PRO_0000241078

Sites

Active site791Charge relay system By similarity
Active site1591Charge relay system By similarity
Active site1831Acyl-ester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YKL3 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 9830C28DEC567BD2

FASTA49352,399
        10         20         30         40         50         60 
MSELTALTIA EARDKLKAKA ITATELTDAY LSAIDAANDA INAYVAVTHD QARSMAKASD 

        70         80         90        100        110        120 
ERIAKGEAGA LEGIPLGVKD LFATKGVHTQ ACSHILDGFK PEYESTVTAN LWADGAVMLG 

       130        140        150        160        170        180 
KLNMDEVAMG SSNETSYYGP VKNPWRAKGS NADLVPGGSS GGSAAAVAAH LCAGATATDT 

       190        200        210        220        230        240 
GGSIRQPAAF TGTVGIKPTY GRVSRWGTVA FASSLDQAGP IARDVRDAAI LMKSMASLDL 

       250        260        270        280        290        300 
KDTTSVDLPV PDYEAALGRS VKGMKIGIPR EYRVDGMPGE IEELWQKGIQ YLKDAGAEIV 

       310        320        330        340        350        360 
DISLPHTKYA LPAYYIVAPA EASSNLARYD GVRYGLRVPG KDIADMYEQT RAAGFGKEVK 

       370        380        390        400        410        420 
RRIMIGTYVL SAGYYDAYYL RAQKVRTLIK KDFEDVFAKG VDAILTPATP SAAFGLADEV 

       430        440        450        460        470        480 
LANDPVKMYL NDIFTVTVNM AGLPGIAVPA GLNGQGLPLG LQLIGRPFEE ETLFQAAHVI 

       490 
EQAAGRFTPA KWW 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040265 Genomic DNA. Translation: CAJ12812.1.
RefSeqYP_418821.1. NC_007624.1.

3D structure databases

ProteinModelPortalQ2YKL3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB2_0646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ12812; CAJ12812; BAB2_0646.
GeneID3828230.
KEGGbmf:BAB2_0646.
PATRIC17848835. VBIBruMel86222_2940.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0154.
HOGENOMHOG000116699.
KOK02433.
OMASKQYRER.
OrthoDBEOG61P6R9.
ProtClustDBPRK00012.

Enzyme and pathway databases

BioCycBABO359391:GKDV-2896-MONOMER.
BMEL359391:GJOQ-2896-MONOMER.

Family and domain databases

Gene3D3.90.1300.10. 1 hit.
HAMAPMF_00120. GatA.
InterProIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR004412. GatA.
[Graphical view]
PANTHERPTHR11895. PTHR11895. 1 hit.
PfamPF01425. Amidase. 1 hit.
[Graphical view]
SUPFAMSSF75304. SSF75304. 1 hit.
TIGRFAMsTIGR00132. gatA. 1 hit.
PROSITEPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATA_BRUA2
AccessionPrimary (citable) accession number: Q2YKL3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 7, 2006
Last modified: March 19, 2014
This is version 52 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

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names