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A5F649 (SYE_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 48. 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:VC0395_A1806, VC395_2330
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

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 ABQ21530.1 differs from that shown. Reason: Erroneous initiation.

The sequence ACP10320.1 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
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 – 474474Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000324781

Regions

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

Sites

Binding site2431ATP By similarity

Experimental info

Sequence conflict3911L → P in AAB86825. Ref.3

Sequences

Sequence LengthMass (Da)Tools
A5F649 [UniParc].

Last modified March 18, 2008. Version 2.
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

References

« Hide 'large scale' references
[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Ogawa 395 / O395.
[2]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Ogawa 395 / O395.
[3]"Cloning and characterization of the gene encoding the OmpA outer membrane protein of Vibrio cholerae."
Liao W.J., Choi M.H., Butterton J.R.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 234-474.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000627 Genomic DNA. Translation: ABQ21530.1. Different initiation.
CP001235 Genomic DNA. Translation: ACP10320.1. Different initiation.
AF030977 Genomic DNA. Translation: AAB86825.1.
RefSeqYP_001217731.1. NC_009457.1.
YP_002820556.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F649.
ModBaseSearch...

Protein-protein interaction databases

STRING345073.VC0395_A1806.

Proteomic databases

PRIDEA5F649.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ21530; ABQ21530; VC0395_A1806.
ACP10320; ACP10320; VC395_2330.
GeneID5136540.
7776117.
KEGGvco:VC0395_A1806.
vcr:VC395_2330.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
ProtClustDBPRK01406.

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_VIBC3
AccessionPrimary (citable) accession number: A5F649
Secondary accession number(s): C3M3H1, O31153, Q9KPZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: May 1, 2013
This is version 48 of the entry and version 2 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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