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A7FSY9 (SYE_CLOB1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:CLB_1134
OrganismClostridium botulinum (strain ATCC 19397 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier441770 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

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

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 – 485485Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330961

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1081Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1351Zinc By similarity
Metal binding1371Zinc By similarity
Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7FSY9 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 4D4264727F64BBB2

FASTA48555,743
        10         20         30         40         50         60 
MTNKVRTRFA PSPTGYMHVG NLRTALYAYL IAKHDNGDFI LRIEDTDQER LVEGALDVIY 

        70         80         90        100        110        120 
NTLKITGLSH DEGPDIGGPV GPYVQSERRN IYIEYAEKLI EKGEAYYCFC SKERLDMLRA 

       130        140        150        160        170        180 
NSEALKRPFR YDKHCIDLSK EEIDKKIAEG VPYVIRQKNP TTGSTSFHDE IYGDISVDNS 

       190        200        210        220        230        240 
ELDDMILIKS DGLPTYNFAN VVDDHLMGIT HVVRGSEYLS SSPKYNRLYE AFGWDVPIYV 

       250        260        270        280        290        300 
HCPPIMKDEH HKLSKRNGDA SFEDLMAKGY LKEAILNYIA LLGWNPGGEK EVFSMEELIE 

       310        320        330        340        350        360 
AFNYRNINKA PAVFDTKKLK WMNGEYIRAL SLDKFHEMAL PYYEEALTRD LDTKKISELL 

       370        380        390        400        410        420 
HTRVEVLNEI PEQLDFFNNL LEYSPEMYIH KKMKTTYENS LKSLEEVLPK LEALENWTFE 

       430        440        450        460        470        480 
NIKEVCMNLV KELEVKNGVV LWPIRTAVSG KQFTPGGAFE IADILGKEET LERIKIGIDK 


LKALQ 

« Hide

References

[1]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19397 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000726 Genomic DNA. Translation: ABS34374.1.
RefSeqYP_001383466.1. NC_009697.1.

3D structure databases

ProteinModelPortalA7FSY9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING441770.CLB_1134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS34374; ABS34374; CLB_1134.
GeneID5396897.
KEGGcba:CLB_1134.
PATRIC19356862. VBICloBot110701_1066.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAIFNYICS.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCBOT441770:GH1E-1116-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_CLOB1
AccessionPrimary (citable) accession number: A7FSY9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 52 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