Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A1B8E0 (SYE2_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:Pden_3717
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length468 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-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

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: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000330987

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif241 – 2455"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1B8E0 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 149B94D134DCD814

FASTA46851,210
        10         20         30         40         50         60 
MTDSRPVVTR FAPSPTGYLH IGGARTALFN WLFARGRNGK FLLRIEDTDR TRSTPEATEA 

        70         80         90        100        110        120 
ILQGLRWLGL DWDGEPVSQF AGRERHAEVA HAMLENGTAY KCFSTTEEIE AFREQAKAEG 

       130        140        150        160        170        180 
RSTLFLSPWR DADPAGLPDA PYAIRLKAPR DGETVVRDAV QGDVTFGNAQ LDDMVLLRSD 

       190        200        210        220        230        240 
GTPTYMLAVV VDDHDMGVTH VIRGDDHLTN AARQIQIYQA MGWDIPVFAH IPLIHGTDGK 

       250        260        270        280        290        300 
KLSKRHGAVG LHEYAAMGYP AAAMRNYLAR LGWSHGDDEL FDDAQAKAWF DLDGIGKAPA 

       310        320        330        340        350        360 
RLDFKKLEHV SGWHIARMDD VELLDEIADF RAATGAEPLS ERQVARLRPA LGALKTKAKT 

       370        380        390        400        410        420 
LPALLEQAHF ALIDRPVQIE EKAAAALDIV SRSILKELTA AVQNASWGRD ELEAAAKQIG 

       430        440        450        460 
ESHGLGLGKV AAPLRAALAG RSSTPSVFDM MLALGRDETL ARMQDQAG 

« Hide

References

[1]"Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000490 Genomic DNA. Translation: ABL71784.1.
RefSeqYP_917480.1. NC_008687.1.

3D structure databases

ProteinModelPortalA1B8E0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_3717.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL71784; ABL71784; Pden_3717.
GeneID4582269.
KEGGpde:Pden_3717.
PATRIC22858594. VBIParDen97112_3655.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-3760-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_PARDP
AccessionPrimary (citable) accession number: A1B8E0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 57 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries