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Q0BZ24 (SYE2_HYPNA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:HNE_2579
OrganismHyphomonas neptunium (strain ATCC 15444) [Complete proteome] [HAMAP]
Taxonomic identifier228405 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeHyphomonas

Protein attributes

Sequence length445 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 – 445445Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367692

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif241 – 2455"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BZ24 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 0B425672130E5C68

FASTA44549,179
        10         20         30         40         50         60 
MTHPVVRFAP SPTGRLHVGN VRTALINWMF SRGQQGKFIL RIDDTDLERS TAEHEEALKV 

        70         80         90        100        110        120 
DLTWLGLTWD DSFSQSHRFA NYDAAADKLR ALHLLYPCYE TAEELDVKRK IAQTRGRPPV 

       130        140        150        160        170        180 
YDRAALSLTA QDRADLEAKG RKPHWRFKLS GERVEWNDLV RGPQSIDTAS VSDPILIRED 

       190        200        210        220        230        240 
GSYLYTLPSV VDDIEAGITH VVRGEDHVTN SGAQIEIFMA LGGKAPEMAH TPLLIGADGA 

       250        260        270        280        290        300 
ALSKRIGSLS MGELRARGYE PMAICSHLAK LGTSDNIEAR ATLEQLCEEF SFSKIGRAPA 

       310        320        330        340        350        360 
RFDDNDLNAL NAALVHAMPF EAVRERLITL DARAASEPFW LAVRENCTFV ADAISWVDMV 

       370        380        390        400        410        420 
YGSPAPLVAE EDREFISGAA MYLPEGELTT ESWSAWTNAL KAATGRKGRG LFMPLRKALT 

       430        440 
GAEHGPEMSA VLPLIGREKV LQRLS 

« Hide

References

[1]"Comparative genomic evidence for a close relationship between the dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter crescentus."
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., Brinkac L.M. expand/collapse author list , Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., Ward N.L.
J. Bacteriol. 188:6841-6850(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15444.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000158 Genomic DNA. Translation: ABI77356.1.
RefSeqYP_761269.1. NC_008358.1.

3D structure databases

ProteinModelPortalQ0BZ24.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228405.HNE_2579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI77356; ABI77356; HNE_2579.
GeneID4288956.
KEGGhne:HNE_2579.
PATRIC32218015. VBIHypNep17450_2587.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAKEDIAKP.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycHNEP228405:GI69-2580-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_HYPNA
AccessionPrimary (citable) accession number: Q0BZ24
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 61 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