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A5VZ22 (GATA_PSEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 39. 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:
Glutamyl-tRNA(Gln) amidotransferase subunit A

Short name=Glu-ADT subunit A
EC=6.3.5.-
Gene names
Name:gatA
Ordered Locus Names:Pput_0971
OrganismPseudomonas putida (strain F1 / ATCC 700007) [Complete proteome] [HAMAP]
Taxonomic identifier351746 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length483 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.

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: 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 – 483483Glutamyl-tRNA(Gln) amidotransferase subunit A HAMAP-Rule MF_00120
PRO_1000015889

Sites

Active site761Charge relay system By similarity
Active site1511Charge relay system By similarity
Active site1751Acyl-ester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VZ22 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: A715AD24E4FB7FF4

FASTA48351,531
        10         20         30         40         50         60 
MHQLTLAEIA RGLADKSFSS EELTGALLAR IKQLDPQINS FISITDDLAL AQARAADARR 

        70         80         90        100        110        120 
AAGETGVLLG APIAHKDLFC TNGVRTSCGS KMLDNFKAPY DATVVAKLAE AGMVTLGKTN 

       130        140        150        160        170        180 
MDEFAMGSAN ESSHYGAVKN PWNLEHVPGG SSGGSAAAVA ARLLPATTGT DTGGSIRQPA 

       190        200        210        220        230        240 
ALTNLTGLKP TYGRVSRWGM IAYASSLDQG GPLARTAEDC ALLLQGMAGF DAKDSTSIEE 

       250        260        270        280        290        300 
PVPDYSASLN ASLQGLRIGL PKEYFGAGLD PRIADLVQAS VKELEKLGAV VKEISLPNMQ 

       310        320        330        340        350        360 
HAIPAYYVIA PAEASSNLSR FDGVRFGYRC EEPKDLTDLY KRSRGEGFGV EVQRRIMVGT 

       370        380        390        400        410        420 
YALSAGYYDA YYVKAQQIRR LIKNDFMAAF NDVDLILGPT TPNPAWKLGA KSSDPVAAYL 

       430        440        450        460        470        480 
EDVYTITANL AGLPGLSMPA GFVDGLPVGV QLLAPYFQEG RLLNVAHRYQ QVTDWHTRAP 


NGF 

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References

[1]"Complete sequence of Pseudomonas putida F1."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F1 / ATCC 700007.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000712 Genomic DNA. Translation: ABQ77132.1.
RefSeqYP_001266316.1. NC_009512.1.

3D structure databases

ProteinModelPortalA5VZ22.
ModBaseSearch...

Protein-protein interaction databases

STRING351746.Pput_0971.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ77132; ABQ77132; Pput_0971.
GeneID5192698.
KEGGppf:Pput_0971.
PATRIC19917951. VBIPsePut56420_0974.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0154.
HOGENOMHOG000116699.
KOK02433.
OMARYDGVKY.
ProtClustDBPRK00012.

Enzyme and pathway databases

BioCycPPUT351746:GI26-1067-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. Amidase_sig_enz. 1 hit.
TIGRFAMsTIGR00132. gatA. 1 hit.
PROSITEPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATA_PSEP1
AccessionPrimary (citable) accession number: A5VZ22
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: May 1, 2013
This is version 39 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