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B0K403 (SYE2_THEPX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:Teth514_2102
OrganismThermoanaerobacter sp. (strain X514) [Complete proteome] [HAMAP]
Taxonomic identifier399726 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteriaceaeThermoanaerobacter

Protein attributes

Sequence length479 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000367784

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022_B
Motif243 – 2475"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0K403 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 237F3A29695EF085

FASTA47955,661
        10         20         30         40         50         60 
MSEVRVRFAP SPTGSLHIGG ARTALFNWLF ARHNGGKFIL RVDDTDLQRS TEESMKGILE 

        70         80         90        100        110        120 
GLKWLGIDWD EGPIYQSQRL EEYRKFANKL LKEGKAYYCF CTKEELEEMR KQAEKEGRPP 

       130        140        150        160        170        180 
MYTGKCRNLT KEQIEEYLRQ GKKPVIRLKV PQQGKTVVHD IIRGDVEFDN STFDDFIIMK 

       190        200        210        220        230        240 
SDNMPTYNFA TVVDDYQMGI THVIRAEEHL SNTPKQILIF EALGLEIPQF AHVSMVLAPD 

       250        260        270        280        290        300 
RSKLSKRHGA TSVQEFRDQG YLPEAIVNYI TLLGWIPKDG EEIFDVSKSI KEFTLERVSK 

       310        320        330        340        350        360 
NPAIYDVQKL TWINGHYIRN YDLDKLTEVV IPFLKAKNFI GEDFDYDYIK KIVSVVRERE 

       370        380        390        400        410        420 
KTLVDVADAM SYYFTEVNEY EEKGVKKYFT KEKVVDILKK AVVTLKEVEP FNKFTTEETY 

       430        440        450        460        470 
RKLVEELQIS SGELFHPTRL AISGRTFGPG LFDIMELLGK ERTIKRIEKA IDFIQKMRK 

« 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: ABY93374.1.
RefSeqYP_001663710.1. NC_010320.1.

3D structure databases

ProteinModelPortalB0K403.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0K403.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5876145.
GenomeReviewsGene locus Teth514_2102 in contig CP000923_GR.
KEGGtex:Teth514_2102.
PATRIC23893932. VBITheSp86957_2180.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAIEWFNLD.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycTSP1755:TETH514_2102-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_THEPX
AccessionPrimary (citable) accession number: B0K403
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 18, 2008
Last modified: January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families