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Q7WEV0 (GATB_BORBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 55. 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:
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:BB4532
OrganismBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier257310 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella ›

Protein attributes

Sequence length484 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.

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: 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 – 484484Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_0000148765

Sequences

Sequence LengthMass (Da)Tools
Q7WEV0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 8C30ACBADD6D5E38

FASTA48452,260
        10         20         30         40         50         60 
MNWEIVIGLE THTQLSTDSK IFSGSSTRFG AAPNTQANAV DLALPGSLPV MNRGAAERAI 

        70         80         90        100        110        120 
LFGLAVGGKV APRSVFARKN YFYPDLPKGY QISQYELPVV EGGTLSFFVG EEEKTVNLTR 

       130        140        150        160        170        180 
AHLEEDAGKS LHDEFSLASG APASGIDLNR AGTPLLEIVT EPEMRSAAEA VAYARALHSL 

       190        200        210        220        230        240 
VVWLGICDGN MQEGSFRCDA NVSVRPVGQK EFGTRTEIKN VNSFRFLERA ILFEARRQIE 

       250        260        270        280        290        300 
LIEDGGTVVQ ETRLYDADRD ETRSMRSKED AHDYRYFPDP DLPPLVIGQD WVDAVRAGMP 

       310        320        330        340        350        360 
ELPAAQRARF EADYGLPAYD AAQLTVSRAM ADYFEAVARA LPAGQAKLAA NWIMGEVAAT 

       370        380        390        400        410        420 
LNREEKDIDA APVSAAALAA LINRIIDGTI SNKIARDVFA AMWAGENGGD ADAIIAARGL 

       430        440        450        460        470        480 
KQISDSGAIG AMIDEVLAAN PAIVEEYRAG KQKAFNSLVG QIMKAAKGKA NPQQVNELLK 


EKLG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX640450 Genomic DNA. Translation: CAE34895.1.
RefSeqNP_891066.1. NC_002927.3.

3D structure databases

ProteinModelPortalQ7WEV0.
ModBaseSearch...

Protein-protein interaction databases

STRING257310.BB4532.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE34895; CAE34895; BB4532.
GeneID2659343.
KEGGbbr:BB4532.
PATRIC21142536. VBIBorBro124907_4613.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223742.
KOK02434.
OMAKNYFYAD.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycBBRO257310:BB4532-MONOMER.

Family and domain databases

Gene3D1.10.10.410. 1 hit.
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.
IPR023168. GatB_Yqey_C.
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. GatB_Yqey. 1 hit.
TIGRFAMsTIGR00133. gatB. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATB_BORBR
AccessionPrimary (citable) accession number: Q7WEV0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: May 1, 2013
This is version 55 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

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