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Q73HV5 (SYE1_WOLPM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:WD_0435
OrganismWolbachia pipientis wMel [Complete proteome] [HAMAP]
Taxonomic identifier163164 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length473 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 – 473473Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000119697

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022_B
Motif252 – 2565"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73HV5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: AE03505EC7327E51

FASTA47353,968
        10         20         30         40         50         60 
MPGIVTRFAP SPTGFLHIGG ARTALFNWLY AKHHGGRFLL RIEDTDRKRS TQEAIDAIIE 

        70         80         90        100        110        120 
GLRWLGMSYD GEIVYQSKRI ERHKEVANLL VEKGRAYHCY CPEDEVAEKK AKAREEGKIY 

       130        140        150        160        170        180 
KHKCTTKPPS CHPSSRHWKN MWSRAGMTSG VRSVVRFKVP DSQEIVIDDK IYGQIKVNSD 

       190        200        210        220        230        240 
QLDDIVILRS DNTPTYIFAV VVDDHDAGIT DIIRGSDHLT NTFKHLLIYQ ALDFDIPRFA 

       250        260        270        280        290        300 
HVPLIHGEDG NKLSKRHGAT SVCDYEKMGI LPKAMRNYLL RLGWSHGNDE IISDEQAIEW 

       310        320        330        340        350        360 
FNLESIGRSP ARLDFKKLEH LNNHYISNMS NEDILTLMLR ENTLTDKKKG YLLQGLTELK 

       370        380        390        400        410        420 
KRANYLTELL DLAKFYIQDP PLDLSEEAEQ IVKSNLDIIK LLASFLSKIG DENWNKGFLS 

       430        440        450        460        470 
SQIKECAKLH DMKISDVYHS LRAPITGVMD APGIIDIMVI LGKDECIRRL QAI 

« Hide

References

[1]"Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements."
Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C., McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R., Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F., Nelson W.C. expand/collapse author list , Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R., Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H., O'Neill S.L., Eisen J.A.
PLoS Biol. 2:327-341(2004) [PubMed: 15024419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017196 Genomic DNA. Translation: AAS14158.1.
RefSeqNP_966224.1. NC_002978.6.

3D structure databases

ProteinModelPortalQ73HV5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ73HV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBWOLT00000004018; EBWOLP00000003575; EBWOLG00000004018.
GeneID2738807.
GenomeReviewsGene locus WD_0435 in contig AE017196_GR.
KEGGwol:WD0435.
PATRIC24029446. VBIWolEnd21207_0431.
TIGRWD_0435.

Phylogenomic databases

GeneTreeEBGT00050000030976.
HOGENOMHBG628189.
OMAANFNDES.
PhylomeDBQ73HV5.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycWPIP955:WD_0435-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 nameSYE1_WOLPM
AccessionPrimary (citable) accession number: Q73HV5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families