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Q65PD0 (SYE_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:BLi00110, BL03267
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length485 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.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119505

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65PD0 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 9B650D12A9B87665

FASTA48556,027
        10         20         30         40         50         60 
MGNEVRVRYA PSPTGHLHIG NARTALFNYL FARSQGGKFI IRIEDTDRKR NIEGGEQSQL 

        70         80         90        100        110        120 
NYLKWLGIDW DESVDVGGEY GPYRQSERND IYKTYYEELL EKGLAYKCYC TEEELEKERE 

       130        140        150        160        170        180 
EQAARGEMPR YSGKCRNLTK EEQEKLEAEG RQPSIRFKVP QGEVIRFDDI VKGEISFETD 

       190        200        210        220        230        240 
GIGDFVIVKK DGTPTYNFAV AVDDYLMKMT HVLRGEDHIS NTPKQIMIYN ALGWDIPAFG 

       250        260        270        280        290        300 
HMTLIVNESR KKLSKRDESI IQFIEQYEEL GYLPEALFNF ITLLGWSPVG EEELFTKEQF 

       310        320        330        340        350        360 
IEIFDVNRLS KSPAVFDTHK LKWVNNQYVK KLDLDQVIEL TVPHLQKAGK VSEELSGSEQ 

       370        380        390        400        410        420 
EWVRKLISLY QEQLSYGAEI VELTELFFKD DIQYNREART VLEEEQVPEV LRVFAEKLEQ 

       430        440        450        460        470        480 
LDSFTADEIK ASIKAVQKET GHKGKKLFMP IRVATTGQTH GPELPQSIEL LGKDTVLKRL 


HNIIQ

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017333 Genomic DNA. Translation: AAU39084.1.
CP000002 Genomic DNA. Translation: AAU21740.1.
RefSeqYP_006711562.1. NC_006322.1.
YP_077378.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65PD0.
ModBaseSearch...

Protein-protein interaction databases

STRING279010.BL03267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU21740; AAU21740; BL03267.
AAU39084; AAU39084; BLi00110.
GeneID3027316.
3097740.
KEGGbld:BLi00110.
bli:BL03267.
PATRIC18945701. VBIBacLic203714_0099.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMADDFDMEI.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-112-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_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]
PANTHERPTHR10119. PTHR10119. 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 nameSYE_BACLD
AccessionPrimary (citable) accession number: Q65PD0
Secondary accession number(s): Q62ZR8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 25, 2004
Last modified: May 1, 2013
This is version 64 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

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