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Q65VB3 (SYE_MANSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:MS0490
OrganismMannheimia succiniciproducens (strain MBEL55E) [Complete proteome] [HAMAP]
Taxonomic identifier221988 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeBasfia

Protein attributes

Sequence length480 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.

Sequence caution

The sequence AAU37097.1 differs from that shown. Reason: Erroneous initiation.

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

tRNA binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119595

Regions

Motif21 – 3111"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1101Zinc By similarity
Metal binding1121Zinc By similarity
Metal binding1371Zinc By similarity
Metal binding1391Zinc By similarity
Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65VB3 [UniParc].

Last modified March 24, 2009. Version 3.
Checksum: 36E148D4CA10F528

FASTA48054,588
        10         20         30         40         50         60 
MELKALFNLD PNVKVRTRFA PSPTGYLHVG GARTALYSWL YAKHNDGEFV LRIEDTDLER 

        70         80         90        100        110        120 
STPEATAAIL DAMEWLNLTW EHGPYFQTER FDRYNEVIDQ MIEQGLAYRC YCSKERLEEL 

       130        140        150        160        170        180 
RHQQEANKEK PRYDRHCLHD HEHSPYEPHV VRFKNPQEGS VVFEDAVRGR IEISNHELDD 

       190        200        210        220        230        240 
LIIRRSDGSP TYNFCVVVDD WDMGITHVVR GEDHINNTPR QINILKALGA PIPVYAHVSM 

       250        260        270        280        290        300 
INGDDGQKLS KRHGAVSVMQ YRDEGYLPEA LLNYLVRLGW GHGDQEIFTL EEMIKLFELE 

       310        320        330        340        350        360 
HVSKSASAFN TEKLLWLNQH YIRELPAEYV AQHLAWQYQE QGIDTSKGPA LTEIVSMLGE 

       370        380        390        400        410        420 
RCKTLKEMAA SSRYFFEEFD GFDEAAAKKH LKAAAVEPLE KVKEKLTALS GWDAHSAHEA 

       430        440        450        460        470        480 
IEQTAAELEV GMGKVGMPLR VAVTGAGQSP SMDVTLAGIG RERVLARIQK AIDFIKAKNA 

« Hide

References

[1]"The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens."
Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., Jeong H., Hur C.G., Kim J.J.
Nat. Biotechnol. 22:1275-1281(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBEL55E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016827 Genomic DNA. Translation: AAU37097.1. Different initiation.
RefSeqYP_087682.1. NC_006300.1.

3D structure databases

ProteinModelPortalQ65VB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING221988.MS0490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU37097; AAU37097; MS0490.
GeneID3075217.
KEGGmsu:MS0490.
PATRIC22444404. VBIManSuc86752_0452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBMAN221988:GHGM-511-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_MANSM
AccessionPrimary (citable) accession number: Q65VB3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 67 of the entry and version 3 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