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A9NEI5 (SYE_ACHLI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:ACL_0139
OrganismAcholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]
Taxonomic identifier441768 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeAcholeplasma

Protein attributes

Sequence length449 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 – 449449Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000074315

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif214 – 2185"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2171ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9NEI5 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 3FBF9203BDA4D10D

FASTA44951,597
        10         20         30         40         50         60 
MKKFRARYAP SPTGHLHIGN ARTALFNYLF ARHHGGDFII RIEDTDVARN VEGGITSQLN 

        70         80         90        100        110        120 
NLKWLGMDWD EGVDVGGSFG PYNQLSRLEL YKKYAFELLE KGYAYKDFKE GSEDFAIRFK 

       130        140        150        160        170        180 
VPENVLYEFD DVIRGTLKFE SKDVEDWIIL KDNGIPTYNF AVVIDDHYME ITHVFRGEEH 

       190        200        210        220        230        240 
ITNTPKQLMV YDALGWEYPT FGHMTIIVNE DRKKLSKRDT NTIQFIEDYK NLGFLPEAML 

       250        260        270        280        290        300 
NFLSLLGWSP KDDEEILSKE ELISLFDEHR LSAAPSYFDK QKLAYINSRY LKALSMDELK 

       310        320        330        340        350        360 
DLTRPFLINH GIEIKNEAWL ESLLSILKDR LSYGAEITKY YDQFFHHDFV LEPAVLEEIK 

       370        380        390        400        410        420 
EFDNEVVIKG FMGAISSVDF TDDVAINQAL KDTGKALNIK GKPLFMPIRI ATTGEAHGPS 

       430        440 
LPVSLSLLGK ELVIKRMNKT LEVLKGETK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000896 Genomic DNA. Translation: ABX80765.1.
RefSeqYP_001620141.1. NC_010163.1.

3D structure databases

ProteinModelPortalA9NEI5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING441768.ACL_0139.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX80765; ABX80765; ACL_0139.
GeneID5804418.
KEGGacl:ACL_0139.
PATRIC20636992. VBIAchLai134690_0123.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMALMLFGRD.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycALAI441768:GI40-139-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. 2 hits.
[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_ACHLI
AccessionPrimary (citable) accession number: A9NEI5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 44 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