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

A9BJB2 (SYE1_PETMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:Pmob_0592
OrganismPetrotoga mobilis (strain DSM 10674 / SJ95) [Complete proteome] [HAMAP]
Taxonomic identifier403833 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaePetrotoga

Protein attributes

Sequence length467 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 – 467467Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367734

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif230 – 2345"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2331ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BJB2 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: B499133D7412F892

FASTA46754,997
        10         20         30         40         50         60 
MIRVRFAPSP TGHLHVGGLR TALFNWYFAK KNNGKFILRI EDTDMERSKK EYEDAILEEM 

        70         80         90        100        110        120 
KWVGLDYDEG VDKPGEYGPY RQSERLDIYK HYIDQLLNEE KAYFSVTKND EIIFEGNNLL 

       130        140        150        160        170        180 
DKYKKNNDYS VVVKFKVNND QKISFLDDVR GTIQFDTSNI NDFVILRSNG IPVYNFTVVI 

       190        200        210        220        230        240 
DDYLMKISHV IRGEDHISNT PKQILIYNAL SFELPKFAHL PLILGEDKSP LSKRHGEVSI 

       250        260        270        280        290        300 
TYFREEGYLP KAILNYLSLL GWNANEQIFD YTEKYQEFDL KKVSRNPSIF DYTKLLWTNE 

       310        320        330        340        350        360 
VHLRNDPIEE VHKSFTEWAK YTTVKIDNED SFVKKIIEAS RAKVQTLKQL YEFSKNFFVE 

       370        380        390        400        410        420 
EFEYEEEFIE KYMKKPWFKQ VIEATIRKLS EIDEYNLANV ENTLKEIADL NITSRKNVFQ 

       430        440        450        460 
TIRGSLLGRL VTPGLYESII ILGKNESIKR LKRALEFSNT LDINPRR 

« Hide

References

[1]"Complete sequence of Petroga mobilis SJ95."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Noll K., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 10674 / SJ95.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000879 Genomic DNA. Translation: ABX31326.1.
RefSeqYP_001567649.1. NC_010003.1.

3D structure databases

ProteinModelPortalA9BJB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING403833.Pmob_0592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX31326; ABX31326; Pmob_0592.
GeneID5758525.
KEGGpmo:Pmob_0592.
PATRIC22918772. VBIPetMob40494_0620.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMACLEWAGI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPMOB403833:GH51-614-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. 2 hits.
[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_PETMO
AccessionPrimary (citable) accession number: A9BJB2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 42 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