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Q65MP8 (GATA_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:BLi00731, BL00601
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length485 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 – 485485Glutamyl-tRNA(Gln) amidotransferase subunit A HAMAP-Rule MF_00120
PRO_0000241071

Sites

Active site791Charge relay system By similarity
Active site1541Charge relay system By similarity
Active site1781Acyl-ester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65MP8 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 4D3F944611FFDEE3

FASTA48552,882
        10         20         30         40         50         60 
MSLFDHKISE LKRLIHNKEI SISDLVDESY KRIHEVDGKV QAFLQLDEEK ARAYAKELDE 

        70         80         90        100        110        120 
ALDTRDEHGL LFGMPIGIKD NIVTKDLRTT CASKILENFD PIYDATVVER LHEAEAVTIG 

       130        140        150        160        170        180 
KLNMDEFAMG SSTENSGFKK TKNPWNLETV PGGSSGGSAA AVAAGEVPFS LGSDTGGSIR 

       190        200        210        220        230        240 
QPASFCGVVG LKPTYGRVSR YGLVAFASSL DQIGPITRSV EDNAYLLQAI SGVDKMDSTS 

       250        260        270        280        290        300 
ANVDVPDYLS ALTGDIKGLK IAVPKEYLGE GVSEEAKQSV LEALKVLESL GATWEEVSLP 

       310        320        330        340        350        360 
HSKYALATYY LLSSSEASAN LARFDGIRYG YRTDNADNLI DLYKQTRSEG FGNEVKRRIM 

       370        380        390        400        410        420 
LGTFALSSGY YDAYYKKAQK VRTLIKKDFE DVFANYDVII GPTTPTPAFK IGEKTSDPLT 

       430        440        450        460        470        480 
MYANDILTIP VNLAGVPGIS VPCGFANGLP LGLQIIGKHF DESTVYRVAH AFEQATDHHK 


AKPEL 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU39666.1.
CP000002 Genomic DNA. Translation: AAU22316.1.
RefSeqYP_006712136.1. NC_006322.1.
YP_077954.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65MP8.
SMRQ65MP8. Positions 1-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL00601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU22316; AAU22316; BL00601.
AAU39666; AAU39666; BLi00731.
GeneID3031305.
3101495.
KEGGbld:BLi00731.
bli:BL00601.
PATRIC18946993. VBIBacLic203714_0721.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0154.
HOGENOMHOG000116699.
KOK02433.
OMARDSTSID.
OrthoDBEOG61P6R9.
ProtClustDBPRK00012.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-724-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_BACLD
AccessionPrimary (citable) accession number: Q65MP8
Secondary accession number(s): Q62Y42
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 25, 2004
Last modified: March 19, 2014
This is version 66 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