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Q21KM1 (SYE_SACD2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:Sde_1496
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

Protein attributes

Sequence length503 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 – 503503Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001954

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif251 – 2555"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2541ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21KM1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 949A48353F24A945

FASTA50356,833
        10         20         30         40         50         60 
MTVRTRVAPS PTGDPHVGTA YIALFNLCFA RKHGGQFILR IEDTDQSRST PESEQAILDS 

        70         80         90        100        110        120 
LRWLGLEWDE GPDVGGAAGP YRQSERKEIY AQYVQQLLDA GHAFKCYRTT EELDMLRAAR 

       130        140        150        160        170        180 
KEAGIHSALK QSDLMLTEQE QAEREAAGIP YVVRMKVPEE EGACQVTDLL RGNIDLDWSM 

       190        200        210        220        230        240 
VDAQILMKSD GMPTYHLANV VDDHLMKITH VIRGEEWINS APKHILLYQY FGWDVPVFCH 

       250        260        270        280        290        300 
LPLLRNPDKT KLSKRKNPTS ILYYKQAGYL PEALTNYLGR MGWSMPDESE KFSIQEMLNH 

       310        320        330        340        350        360 
FDIARVSLGG PVFDIEKLNW LNGLWIREDL DDAALAQRLV DWKFNQDNLL AVIPHVKQRM 

       370        380        390        400        410        420 
ETLGDFLPMV SFLAANTLGI TEESFKGNKL DLEDQKKVLQ FALWQLDTMR TWERDDIFAT 

       430        440        450        460        470        480 
LKGLADGMGI KLKDFLAPLF VAISGSTASF SVMDAMVLLG SDLSRARLRV AVEVLGGAGK 

       490        500 
KVLKRYEKEF AALSQLNEES DAE 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2-40 / ATCC 43961 / DSM 17024.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD80758.1.
RefSeqYP_526970.1. NC_007912.1.

3D structure databases

ProteinModelPortalQ21KM1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203122.Sde_1496.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD80758; ABD80758; Sde_1496.
GeneID3965233.
KEGGsde:Sde_1496.
PATRIC23401889. VBISacDeg56404_1633.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMALMERADI.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSDEG203122:GI2M-1518-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_SACD2
AccessionPrimary (citable) accession number: Q21KM1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 62 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