Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C6Q1 (SYE_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:VC_2214
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length474 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.

Sequence caution

The sequence AAF95358.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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 – 474474Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119691

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C6Q1 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: D7F6FC1B9CDF5146

FASTA47453,379
        10         20         30         40         50         60 
MTVKTRFAPS PTGYLHVGGA RTALYSWLYA KSQGGEFVLR IEDTDLERST QAAVDAIIEG 

        70         80         90        100        110        120 
MTWLGLEWDE GPYYQTKRFD RYNQVIDQLL AEGKAYKCYA PKELLDEIRA EQEANKEMPR 

       130        140        150        160        170        180 
YDANHPKIKA VNDAAKEGEP CCIRFRNPKE GSVVFDDQIR GRIEIRNDQL DDLIIRRTDG 

       190        200        210        220        230        240 
TPTYNFCVVV DDVDMGISHV IRGEDHINNT PRQINIYKAM GATIPTFAHC AMILGDDGAK 

       250        260        270        280        290        300 
LSKRHGAVSV MQYRDDGYLP EALLNYLVRL GWGHGDQEIF SRDEMINLFS LNAISKSASA 

       310        320        330        340        350        360 
FNTDKLLWLN NHYIKTSEPE YVAKHLEWHF ENQGINKATG PALAEVVKLV GERCNTLVEL 

       370        380        390        400        410        420 
AQQSRYFYED FAEFDADAAK KHLRGVAKEP LMLALSKIEA LTEWNTEALH HVIAQVCEEL 

       430        440        450        460        470 
EIGMGKIGMP LRVAVTGGGQ SPSVDAVMNL IGQERVIARI KMALEYIETR EANA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF95358.1. Different initiation.
PIRG82104.
RefSeqNP_231845.1. NC_002505.1.

3D structure databases

ProteinModelPortalP0C6Q1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC2214.

Proteomic databases

PRIDEP0C6Q1.

Protocols and materials databases

DNASU2613253.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF95358; AAF95358; VC_2214.
GeneID2613253.
KEGGvch:VC2214.
PATRIC20083473. VBIVibCho83274_2112.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

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_VIBCH
AccessionPrimary (citable) accession number: P0C6Q1
Secondary accession number(s): O31153, Q9KPZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: May 14, 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