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Q6F1V4 (GATB_MESFL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:Mfl163
OrganismMesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1) (Acholeplasma florum) [Reference proteome] [HAMAP]
Taxonomic identifier265311 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesEntomoplasmatalesEntomoplasmataceaeMesoplasma

Protein attributes

Sequence length479 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
Reference 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 – 479479Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_0000241237

Sequences

Sequence LengthMass (Da)Tools
Q6F1V4 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: B24DFA899127259B

FASTA47954,705
        10         20         30         40         50         60 
MRNFEIVIGI ENHVELKTKS KMFSSAPVSY GETPNTNVNE TDMAYPGSLP TINKKGIELA 

        70         80         90        100        110        120 
IRTCNALNME IDTLVKFDRK NYFYPDLTKG YQITQQYNPI GKNGKLNINV NGLTKEVDIE 

       130        140        150        160        170        180 
RLHMEEDTAK QIHKDDLTYI DYNRAGTGLV EIVTRPVLRS ADEACAYVEK LREVLLFLKV 

       190        200        210        220        230        240 
SDVKMNEGSL RTDVNISIRP FGTQEFSNKV EVKNLNSISN IKKAIEFEVE RQTKLMLNNE 

       250        260        270        280        290        300 
IIIQETRRFD DTTNSTVSMR SKSDALDYKY FREPNIMPIQ LKKEWVEDCI KNSPELADIK 

       310        320        330        340        350        360 
RIKYVNDYKI SINDANIILT SIEMTEFFEE TIKFTNNYTK VANILISDIQ AQLNNENTTI 

       370        380        390        400        410        420 
DKLALLPSHL AEMINLVDQS VISSKHTKTI LPIIMKDSSK SVIEIVEELN IKMISDENEI 

       430        440        450        460        470 
ANLVNPIIES NLELLEQYSE RPERVTKTIM GQLMKVTGGN VNPEAGMNII IKLVENKIK 

« Hide

References

[1]Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S., Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33453 / NBRC 100688 / NCTC 11704 / L1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017263 Genomic DNA. Translation: AAT75519.1.
RefSeqYP_053403.1. NC_006055.1.

3D structure databases

ProteinModelPortalQ6F1V4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265311.Mfl163.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT75519; AAT75519; Mfl163.
GeneID2897853.
KEGGmfl:Mfl163.
PATRIC22473035. VBIMesFlo3168_0164.

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223742.
KOK02434.
OMAESADYRY.
OrthoDBEOG6RJV5B.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycMFLO265311:GHIB-184-MONOMER.

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_MESFL
AccessionPrimary (citable) accession number: Q6F1V4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: August 16, 2004
Last modified: February 19, 2014
This is version 54 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