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Q65PD0 (SYE_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
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 › 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 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 – 485485Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119505

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022_B
Motif252 – 2565"KMSKS" region HAMAP MF_00022_B

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: 15383718] [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: 15461803] [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_077378.1. NC_006270.3.
YP_089777.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65PD0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65PD0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000055900; EBBACP00000054431; EBBACG00000055891.
EBBACT00000059426; EBBACP00000057859; EBBACG00000059417.
GeneID3027316.
3097740.
GenomeReviewsGene locus BLi00110 in contig AE017333_GR.
Gene locus BL03267 in contig CP000002_GR.
KEGGbld:BLi00110.
bli:BL03267.
NMPDRfig|279010.5.peg.1487.
PATRIC18945701. VBIBacLic203714_0099.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
GeneTreeEBGT00050000002239.
HOGENOMHBG628189.
OMADDFDMEI.
PhylomeDBQ65PD0.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI00110-MONOMER.
BLIC279010:BL03267-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.
KOK09698.
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 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: January 25, 2012
This is version 55 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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