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

B0K5F4 (SYE1_THEPX) 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:Teth514_0844
OrganismThermoanaerobacter sp. (strain X514) [Complete proteome] [HAMAP]
Taxonomic identifier399726 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter

Protein attributes

Sequence length485 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 – 485485Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367783

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0K5F4 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 9F1B4B1D2ABC4617

FASTA48556,471
        10         20         30         40         50         60 
MNNLRVRFAP SPTGAIHIGN IRTALFNYLF SRSEGATFVL RIEDTDLERS SKEFEELIFK 

        70         80         90        100        110        120 
ELEWLGIEWD EGPDKPGPYG PYRQSERLEI YHKFAQKLIE EKKAYRCYCT PEELEEDRRK 

       130        140        150        160        170        180 
AVERGDIPRY SGRCRYLTKE QEEAFIREGR KPVIRFIIPD DEVIEFEDMI KGKITIKSDT 

       190        200        210        220        230        240 
LGGDMVIVKS DGMPTYNFAV VIDDALMKIT HVIRGEDHIY NTPKQILIYK ALGFEIPKFA 

       250        260        270        280        290        300 
HAPLILGPDR TKLSKRHGNT YIGQYRELGY LPEAMFNFLS LLSWSPEDNV EIMSKEEIIK 

       310        320        330        340        350        360 
KFNFRRIHSA NPVFDIEKLN WMNQQYIQKS SIERIVDLAI PHLRRAGYID GIDDMVYNWL 

       370        380        390        400        410        420 
KDVISLYKDG LQYVAQITEK AKMFFVEEVE YSDETVKILN SPNSKIVLEV VKKVIEEADE 

       430        440        450        460        470        480 
ITEEYVKDLL KKLQKETKVK GKEFFMPIRV AITGEDHGPE LVKIIPLLGK DKVINRLKKA 


INLIK 

« Hide

References

[1]"Complete sequence of Thermoanaerobacter sp. X514."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X514.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000923 Genomic DNA. Translation: ABY92147.1.
RefSeqYP_001662483.1. NC_010320.1.

3D structure databases

ProteinModelPortalB0K5F4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399726.Teth514_0844.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY92147; ABY92147; Teth514_0844.
GeneID5876365.
KEGGtex:Teth514_0844.
PATRIC23891279. VBITheSp86957_0889.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAFFVEEVD.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycTSP399726:GHCK-867-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 nameSYE1_THEPX
AccessionPrimary (citable) accession number: B0K5F4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
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