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A1KWM9 (SYE_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:NMC2141
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length464 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 – 464464Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001926

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif242 – 2465"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KWM9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: AAAABE5A7EFF1FA4

FASTA46452,461
        10         20         30         40         50         60 
MTVKTRFAPS PTGYLHIGGV RTALFSWAFA RHHKGEFLLR IEDTDLARST AESVNIILDG 

        70         80         90        100        110        120 
MKWVGLNYDN ADNVVYQTRR FDRYKEVIAE LLEKGHAYYC YCSKEELEAM REKAEKEGTA 

       130        140        150        160        170        180 
TYDRRWRPEA GKTLPEIPAG VQPVVRFKTP LDGVTKWADL VKGEISIPNE ALDDLIIARA 

       190        200        210        220        230        240 
DGTPTYNFCV VVDDYDMGVT HVIRGDDHVN NTPKQINILK AIGANLPEYG HLPMILNEQG 

       250        260        270        280        290        300 
KKISKRSGDT VAITDFGAMG ILPEAMLNYL ARLGWAHGDD EFFTMEQFIE WFDLKDVSPS 

       310        320        330        340        350        360 
PSRMDLKKLY WINGEHIKIT TNEKLAEMVK PRLALRDIHE TSKPALEDVL ALVKDRAQDL 

       370        380        390        400        410        420 
NALADECLYF YKKQVPAEAD VAKHWDDEAS ARMLRFAERL EGLEDWNTEA IHDLFKPFCD 

       430        440        450        460 
EEGIKMGKLG MPLRLAVCGT AKTPSVDAVL ALIGKEEVLK RIRA 

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / DSM 15464 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM421808 Genomic DNA. Translation: CAM11289.1.
RefSeqYP_976051.1. NC_008767.1.

3D structure databases

ProteinModelPortalA1KWM9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272831.NMC2141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM11289; CAM11289; NMC2141.
GeneID4676258.
KEGGnmc:NMC2141.
PATRIC20354896. VBINeiMen17609_2667.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycNMEN272831:GJDX-2034-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_NEIMF
AccessionPrimary (citable) accession number: A1KWM9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 57 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