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B9MQ85 (GATB_CALBD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:Athe_0762
OrganismCaldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum) [Complete proteome] [HAMAP]
Taxonomic identifier521460 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length480 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 – 480480Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_1000122503

Sequences

Sequence LengthMass (Da)Tools
B9MQ85 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 2A3BD0019AEEF92C

FASTA48054,776
        10         20         30         40         50         60 
MEYEVVIGLE VHAELATKSK IFCSCTTEFG GEPNTHCCPI CTGMPGVLPV LNKKAVEYAI 

        70         80         90        100        110        120 
MAGLATNCQI ARYSKQDRKN YFYPDLPKAY QISQYDLPLC YNGYIDIEVN GQKKRIGIKR 

       130        140        150        160        170        180 
IHIEEDAGKL LHDQWEEGSL VDFNRCGVPL IEIVTEPDLR SSEETRIFLE KLKAILQYTE 

       190        200        210        220        230        240 
VSDCKMQEGS LRVDVNLSVR PKGSKEFGTR TEMKNLNSFR SVVRAIEYEA RRQIEVLESG 

       250        260        270        280        290        300 
GVVVQETRRW DDPKGISLSM RTKEEAHDYR YFPEPDLPPI VVDDSWIEEI RKRIPELPDQ 

       310        320        330        340        350        360 
KKERYIKEYG LPEYDAGVLT SSKAIANYFE ECIKYTQNIK AASNWMMGEI MRILNDKGLE 

       370        380        390        400        410        420 
PEEINNIKIK PNQLASLINL VDNKTISNTI AKQVFEEMFE TGKDPEVIVK EKGLVQITDR 

       430        440        450        460        470        480 
NVILEAVKQA IANNPKSVED YKNGKDKAFG FLVGQVMKIT KGKANPQLVN EILREELEKI 

« Hide

References

[1]"Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1888 / DSM 6725 / Z-1320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001393 Genomic DNA. Translation: ACM59877.1.
RefSeqYP_002572650.1. NC_012034.1.

3D structure databases

ProteinModelPortalB9MQ85.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521460.Athe_0762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM59877; ACM59877; Athe_0762.
GeneID7407949.
KEGGate:Athe_0762.
PATRIC20898593. VBIAnaThe135187_0813.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223742.
KOK02434.
OrthoDBEOG6RJV5B.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycCBES521460:GH8H-779-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. SSF89095. 1 hit.
TIGRFAMsTIGR00133. gatB. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATB_CALBD
AccessionPrimary (citable) accession number: B9MQ85
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
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