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A9KRX7 (SYE_CLOPH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Cphy_0221
OrganismClostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) [Complete proteome] [HAMAP]
Taxonomic identifier357809 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length490 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.

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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330965

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif257 – 2615"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1091Zinc By similarity
Metal binding1111Zinc By similarity
Metal binding1401Zinc By similarity
Metal binding1421Zinc By similarity
Binding site2601ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KRX7 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: B40D2E85011A7CD6

FASTA49056,076
        10         20         30         40         50         60 
MAKVRTRFAP SPTGRMHVGN LRTALYEYLI AKHEGGDFIL RIEDTDQERL VEGATEIIYR 

        70         80         90        100        110        120 
TIAKTGLIHD EGPDKDKGFG PYVQSERQAT GIYLKYAKEL VENGEAYYCF CTKERLETLK 

       130        140        150        160        170        180 
SAVGEEDGES KEITKYDKHC LHLSKEEVEA NLAAGMPYVI RQNMPTEGTT SFTDAIYGTI 

       190        200        210        220        230        240 
TVENSELDDM ILIKSDGFPT YNFANVIDDH FMEITHVVRG NEYLSSTPKY TRLYKAFGWE 

       250        260        270        280        290        300 
EPVYIHCPLI TNEEHQKLSK RSGHSSFEDL IEQGFVTEAI VNFIALLGWS STTNEEIFSL 

       310        320        330        340        350        360 
EELVREFDYT HINKSPSVFD MNKLRWMNGE YIKRMDSEKY YEYALPQIKK VVTKDYDLKF 

       370        380        390        400        410        420 
IADLVKTRIE TFLDIAEMID FFDELPEYDI AMYTHKKMKT DSENSLKVLQ DVLPRFEELT 

       430        440        450        460        470        480 
CYSVSSIESV LMGYIAENGI KNGQGLWPVR TAVSGKQSTP GGAYEIMSIL GKEESLRRIR 

       490 
IAIDKLSSSL 

« Hide

References

[1]"Complete genome sequence of Clostridium phytofermentans ISDg."
Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C. expand/collapse author list , Han C., Kuske C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700394 / DSM 18823 / ISDg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000885 Genomic DNA. Translation: ABX40608.1.
RefSeqYP_001557347.1. NC_010001.1.

3D structure databases

ProteinModelPortalA9KRX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357809.Cphy_0221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX40608; ABX40608; Cphy_0221.
GeneID5745089.
KEGGcpy:Cphy_0221.
PATRIC19499930. VBICloPhy16213_0228.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAWLPEEMG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCPHY357809:GHCL-242-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_CLOPH
AccessionPrimary (citable) accession number: A9KRX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 50 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