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Q6G3V1 (SYE2_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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 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 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 – 459459Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000119511

Regions

Motif8 – 1811"HIGH" region HAMAP MF_00022_B
Motif249 – 2535"KMSKS" region HAMAP MF_00022_B

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: 15210978] [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...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2864754.
GenomeReviewsGene locus BH06460 in contig BX897699_GR.
KEGGbhe:BH06460.
NMPDRfig|283166.1.peg.603.
PATRIC20545109. VBIBarHen29080_0703.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMALLYPCYE.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycBHEN283166:BH06460-MONOMER.

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_BARHE
AccessionPrimary (citable) accession number: Q6G3V1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families