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P64198 (GATB_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:
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:BR0899, BS1330_I0895
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length500 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. HAMAP-Rule MF_00121

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: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbon-nitrogen ligase activity, with glutamine as amido-N-donor

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_0000148771

Sequences

Sequence LengthMass (Da)Tools
P64198 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: FEBA3251275BE195

FASTA50054,714
        10         20         30         40         50         60 
MSIIDTRTPE PKRFISGATG DWEVVIGMEV HAQVTSESKL FSGASTAFGA EPNSNVSLVD 

        70         80         90        100        110        120 
AAMPGMLPVI NLECVRQAVR TGIGLNAQIN LKSVFDRKNY FYPDLPQGYQ ISQFKQPIVG 

       130        140        150        160        170        180 
EGKIMISVGP DNKGQFEDVE IGIERLHLEQ DAGKSMHDQH PTMSYVDLNR SGVALMEIVS 

       190        200        210        220        230        240 
KPDLRSSDEA RAYLTKLRTI VRYLGTCDGN MDEGSMRADV NVSVRRPGGE FGTRCEIKNV 

       250        260        270        280        290        300 
NSIRFVGQAI EYEARRQIAI LEDGGVIDQE TRLFDPVKGE TRSMRSKEEA HDYRYFPDPD 

       310        320        330        340        350        360 
LLPLEFDQAF VDALAAKLPE LPDVKKQRLV ETLGISVYDA SILVTEKAIA DYYEAVAEGR 

       370        380        390        400        410        420 
DGKAAANWVI NDLLGALNKA GKDIEESPIS PAQLGAIIDL IKEGTISGKI AKDLFEIVWN 

       430        440        450        460        470        480 
EGGDPKKLVE ERGMKQVTDT GAIEKAVDDV IAANPDKVEQ AKAKPTLAGW FVGQVMKATG 

       490        500 
GKANPQAVNE LVKSKLGIEE 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN29827.1.
CP002997 Genomic DNA. Translation: AEM18244.1.
RefSeqNP_697912.1. NC_004310.3.
YP_005615736.1. NC_017251.1.

3D structure databases

ProteinModelPortalP64198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BR0899.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN29827; AAN29827; BR0899.
AEM18244; AEM18244; BS1330_I0895.
GeneID1166568.
12137222.
KEGGbms:BR0899.
bsi:BS1330_I0895.
PATRIC17790106. VBIBruSui107850_0913.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223743.
KOK02434.
OMASNWIMTE.
OrthoDBEOG6RJV5B.

Family and domain databases

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.
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. SSF89095. 1 hit.
TIGRFAMsTIGR00133. gatB. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATB_BRUSU
AccessionPrimary (citable) accession number: P64198
Secondary accession number(s): G0K9C7, Q8YGT9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 56 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 suis

Brucella suis (strain 1330): entries and gene names