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Q6G3V1 (SYE2_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:BH06460
OrganismBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier283166 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length459 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 – 459459Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119511

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G3V1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: CC9AB73BC04B3047

FASTA45952,847
        10         20         30         40         50         60 
MIKVRFAPSP TGYIHIGNIR IALFNWLYAQ AHNGTFILRY DNTDVERSKQ EYIDAIAVDL 

        70         80         90        100        110        120 
EWLGIQPDEI YYQSKRFNRY DEVAEILKQR GLLYPCYETA EELDRRRKIQ LSRKLPPVYD 

       130        140        150        160        170        180 
RAALKLTPEK KREFETQGRK PHWRFLLPNF ENDPLQKKRT EVCWNDAVKG KQTIDLASLS 

       190        200        210        220        230        240 
DPVLIREDGS YLYTLPSVVD DIDMAITHII RGDDHITNTG AQIALFEALN AKLPTFGHIN 

       250        260        270        280        290        300 
LLTTLLGKGL SKRNNDLSIH SLRADGFESI AVQCLAVLIG TSQNVHPYPN QAVLLEHFNL 

       310        320        330        340        350        360 
QDTSRSVAKF DIADLLTLNS HFVHELTYEE VKKRLENLSI NGEKVECFWN AIRSNINKVN 

       370        380        390        400        410        420 
DAVLWWKMLH DEQNFDTVAL EDRAFVRQSL NLLPEGTLNE ESWKVWTVAL KEKTGRRGKA 

       430        440        450 
LFMPLRQALT GMDHGPEMGK ILQLLGREKV IERLIIQGE 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897699 Genomic DNA. Translation: CAF27450.1.
RefSeqYP_033475.1. NC_005956.1.

3D structure databases

ProteinModelPortalQ6G3V1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283166.BH06460.

Proteomic databases

PRIDEQ6G3V1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF27450; CAF27450; BH06460.
GeneID2864754.
KEGGbhe:BH06460.
PATRIC20545109. VBIBarHen29080_0703.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMARIALFNW.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBHEN283166:GIVZ-645-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_BARHE
AccessionPrimary (citable) accession number: Q6G3V1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 68 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