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A6TC43 (SYE_KLEP7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:KPN78578_27030
ORF Names:KPN_02750
OrganismKlebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) [Complete proteome] [HAMAP]
Taxonomic identifier272620 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length472 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001910

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6TC43 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: F978D4906F4AC65B

FASTA47253,603
        10         20         30         40         50         60 
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RNHGGEFVLR IEDTDLERST PEAIEAIMDG 

        70         80         90        100        110        120 
MNWLNLQWDE GPYFQTKRFD RYNNVIDEML EAGTAYKCYC SKERLEALRE EQMAKGEKPR 

       130        140        150        160        170        180 
YDGRCRHSHE HHADDEPCVV RFANPQQGSV IFDDQIRGPI EFSNQELDDL IIRRTDGSPT 

       190        200        210        220        230        240 
YNFCVVVDDW DMAITHVIRG EDHINNTPRQ INILKALNAP VPVYAHVSMI NGDDGKKLSK 

       250        260        270        280        290        300 
RHGAVSVMQY RDDGYLPEAL LNYLVRLGWS HGDQEIFTRE EMIEFFSLGA VSKSASAFNT 

       310        320        330        340        350        360 
DKLLWLNHHY INTLPAEYVA THLQWHIEQE NIDTRNGPQL AELVKLLGER CKTLKEMAQS 

       370        380        390        400        410        420 
CRYFYEEFAE FDADAAKKHL RPVARQPLEM VRDKLAAISD WTAENVHHAI QATADELEVG 

       430        440        450        460        470 
MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK SRSVDRINKA LAFIAEREGQ AS 

« Hide

References

[1]The Klebsiella pneumonia Genome Sequencing Project
McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700721 / MGH 78578.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000647 Genomic DNA. Translation: ABR78164.1.
RefSeqYP_001336394.1. NC_009648.1.

3D structure databases

ProteinModelPortalA6TC43.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272620.KPN_02750.

Proteomic databases

PRIDEA6TC43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR78164; ABR78164; KPN_02750.
GeneID5342113.
KEGGkpn:KPN_02750.
PATRIC20459800. VBIKlePne13394_2771.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycKPNE272620:GKDC-2750-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 nameSYE_KLEP7
AccessionPrimary (citable) accession number: A6TC43
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 48 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