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Q9Z9X0 (GATB_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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:
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:BH0667
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length476 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 MF_00121

Catalytic activity

ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP MF_00121

ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. HAMAP MF_00121

Subunit structure

Heterotrimer of A, B and C subunits By similarity. HAMAP 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 – 476476Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP MF_00121
PRO_0000148760

Sequences

Sequence LengthMass (Da)Tools
Q9Z9X0 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C212B522413C579B

FASTA47653,415
        10         20         30         40         50         60 
MNFETVIGLE VHVELKTESK IFSASPNHFG AEPNANTSVI DLGYPGVLPV LNKAAVEFAM 

        70         80         90        100        110        120 
KAAMALNCEV ATDTKFDRKN YFYPDNPKAY QISQFDKPIG ENGWIEIEVD GTKKKIGITR 

       130        140        150        160        170        180 
LHLEEDAGKL THSGNGYSLV DFNRQGTPLI EIVSEPDIRT PQEAYAYLEK LKSIIQYTGV 

       190        200        210        220        230        240 
SDCKMEEGSL RCDANISLRP VGQEEFGTKT ELKNLNSFNF VRKGLEYEEK RQAQVLLSGG 

       250        260        270        280        290        300 
EILQETRRYD EAANKTVLMR VKEGSDDYRY FPEPDLVALH IDDEWKARIR SEIPELPDAR 

       310        320        330        340        350        360 
KKRYVEELGL PAYDAMVLTL TKEMSDFFEE TIAKGADPKL ASNWLMGEVS GYLNAEQKEL 

       370        380        390        400        410        420 
DEVALTPDGL AKMIQLIEKG TISSKIAKKV FKDLIEKGGD PEEIVKAKGL VQISDEGELR 

       430        440        450        460        470 
KYVVEVLDNN QQSIDDFKNG KDRAIGFLVG QIMKATKGKA NPPMVNKLLL EEINKR 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of three lambda clones from the genome of alkaliphilic Bacillus sp. strain C-125."
Takami H., Nakasone K., Ogasawara N., Hirama C., Nakamura Y., Masui N., Fuji F., Takaki Y., Inoue A., Horikoshi K.
Extremophiles 3:29-34(1999) [PubMed: 10086842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
[2]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011836 Genomic DNA. Translation: BAA75312.1.
BA000004 Genomic DNA. Translation: BAB04386.1.
PIRT44293.
RefSeqNP_241533.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9Z9X0.
SMRQ9Z9X0. Positions 2-412.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000052034; EBBACP00000050673; EBBACG00000052025.
GeneID893061.
GenomeReviewsGene locus BH0667 in contig BA000004_GR.
KEGGbha:BH0667.
NMPDRfig|272558.1.peg.667.
PATRIC18938322. VBIBacHal18977_0699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002603.
HOGENOMHBG395951.
OMAKNYFYAD.
PhylomeDBQ9Z9X0.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycBHAL272558:BH0667-MONOMER.

Family and domain databases

HAMAPMF_00121. GatB.
[Tree]
InterProIPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E.
IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat.
IPR018027. Asn/Gln_amidotransferase.
IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel.
IPR004413. Gln-tRNA_amidoTrfase_bsu.
IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
[Graphical view]
KOK02434.
PANTHERPTHR11659. GatB. 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_BACHD
AccessionPrimary (citable) accession number: Q9Z9X0
Secondary accession number(s): Q9JPV7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 69 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