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Q98M95 (GATA_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:
Glutamyl-tRNA(Gln) amidotransferase subunit A

Short name=Glu-ADT subunit A
EC=6.3.5.-
Gene names
Name:gatA
Ordered Locus Names:mll0675
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) By similarity. HAMAP MF_00120

Catalytic activity

ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP MF_00120

Subunit structure

Heterotrimer of A, B and C subunits By similarity. HAMAP MF_00120

Sequence similarities

Belongs to the amidase family. GatA 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 – 521521Glutamyl-tRNA(Gln) amidotransferase subunit A HAMAP MF_00120
PRO_0000105193

Sites

Active site791Charge relay system By similarity
Active site1871Charge relay system By similarity
Active site2111Acyl-ester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98M95 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 7D416666B589F0C9

FASTA52155,665
        10         20         30         40         50         60 
MSDLTRLTIS QARAKLRGKE ITATEITEAY LSAIDRANPA LNAYVAVTGD RARDMAKASD 

        70         80         90        100        110        120 
ARLVKGEGGA LEGIPLGIKD LFGTEGVHTQ ACSHVLDGFK PLYESTVTAN LWADGAVMLG 

       130        140        150        160        170        180 
KLNMDEFAMG SSNETSYYGP VINPWRRSRL DTVVMPTTHQ GDGGFVSAGG TKTQRSLDNA 

       190        200        210        220        230        240 
QLVPGGSSGG SATAVSAFLC AGATATDTGG SIRQPAAFTG TVGIKPTYGR CSRWGIVAFA 

       250        260        270        280        290        300 
SSLDQAGPIA RDVRDAAILL KSMASVDPKD TTSVDRPVPD YEAAIGKPIK GMKVGIPKEY 

       310        320        330        340        350        360 
RVDGMPEEIE ALWQKGIAWL RDAGAEIVDI SLPHTKYALP AYYIVAPAEA SSNLARYDGV 

       370        380        390        400        410        420 
RYGLRVPGKD IVEMYEKTRA AGFGREVKRR IMIGTYVLSA GYYDAYYLQA QKVRNLIKRD 

       430        440        450        460        470        480 
FENVFAAGVD VILTPATPSA AFGIADEDMA ADPVKMYLND IFTVTVNMAG LPGIAVPAGL 

       490        500        510        520 
DPKGLPLGLQ LIGRPFEEET LFQTAAVIEQ AAGTFQPEKW W 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB48218.1.
RefSeqNP_102432.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98M95.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1225095.
GenomeReviewsGene locus mll0675 in contig BA000012_GR.
KEGGmlo:mll0675.
NMPDRfig|266835.1.peg.537.
PATRIC22475244. VBIMesLot2464_0542.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG481888.
OMAFDEETLF.
ProtClustDBPRK00012.

Family and domain databases

HAMAPMF_00120. GatA.
[Tree]
InterProIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR004412. GatA.
[Graphical view]
Gene3DG3DSA:3.90.1300.10. Amidase_sig_enz. 2 hits.
KOK02433.
PANTHERPTHR11895. Amidase. 1 hit.
PfamPF01425. Amidase. 2 hits.
[Graphical view]
SUPFAMSSF75304. Amidase_sig_enz. 1 hit.
PROSITEPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATA_RHILO
AccessionPrimary (citable) accession number: Q98M95
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2001
Last modified: January 25, 2012
This is version 51 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