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A9HLD9 (SYE2_GLUDA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Glutamate--tRNA ligase 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:GDI2211, Gdia_0429
OrganismGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP]
Taxonomic identifier272568 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000367676

Regions

Motif7 – 1711"HIGH" region HAMAP MF_00022_B
Motif240 – 2445"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2431ATP By similarity

Experimental info

Sequence conflict149 – 1535QDRGV → RTVAW in ACI50225. Ref.2
Sequence conflict4181E → K in ACI50225. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A9HLD9 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: FF25EFA70635693F

FASTA44349,680
        10         20         30         40         50         60 
MKLRFAPSPT GLIHVGNARQ AIANALYARR HGGTFQLRID DTDRERSRDE YVDALHTDLA 

        70         80         90        100        110        120 
WLGITWDETF RQSDRLDRYA AAIETLKASG RLYPCFESEQ ELASKREARI RMRKPPIYDR 

       130        140        150        160        170        180 
AMLRMTAEQR AQAEANGKVP YWRFRLSDQD RGVDDMVMGR SQVKLQSISD PVLVRADGTV 

       190        200        210        220        230        240 
LYTLASVVDD METGVTHVLR GEDHLTNTGV QIDIAEALGG KVGQFAFAHL PLLLDEAGGK 

       250        260        270        280        290        300 
LSKRFDGLSI RALRQDGIDP VAIVSYLARL GSADDPAPLS FDDLAASYDV RRVSRSAARF 

       310        320        330        340        350        360 
DMRQLLALNR RVMHQMPFGA IRDRLPEGAT EAFWMAVRGN VDMVSELRHW WDVVGGVIVP 

       370        380        390        400        410        420 
PVQDDEGAYL LQALALLPPE PWDAQTWKDW TTAVRDATGR SGKSVFHPLR VALTGEEEGP 

       430        440 
EMRDLLPLMG HDRVAERLRI AAR 

« Hide

References

[1]"Gluconacetobacter diazotrophicus Pal5 complete genome."
Bertalan M., Baldani I.J., Ferreira P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49037 / DSM 5601 / PAl5.
[2]"Complete sequence of chromosome of Gluconacetobacter diazotrophicus PAl 5."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Triplett E.W.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49037 / DSM 5601 / PAl5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM889285 Genomic DNA. Translation: CAP56154.1.
CP001189 Genomic DNA. Translation: ACI50225.1.
RefSeqYP_001602456.1. NC_010125.1.
YP_002274840.1. NC_011365.1.

3D structure databases

ProteinModelPortalA9HLD9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9HLD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5792212.
6973823.
GenomeReviewsGene locus GDI2211 in contig AM889285_GR.
Gene locus Gdia_0429 in contig CP001189_GR.
KEGGgdi:GDI_2211.
gdj:Gdia_0429.
PATRIC22049240. VBIGluDia203729_0436.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMADQERIEW.
ProtClustDBPRK12558.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_GLUDA
AccessionPrimary (citable) accession number: A9HLD9
Secondary accession number(s): B5ZCG1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families