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

Q896M5 (SYE_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:CTC_00977
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length488 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.

Sequence caution

The sequence AAO35565.1 differs from that shown. Reason: Erroneous initiation.

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 – 488488Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119546

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1091Zinc By similarity
Metal binding1111Zinc By similarity
Metal binding1361Zinc By similarity
Metal binding1381Zinc By similarity
Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q896M5 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: FBB37A170846127B

FASTA48856,137
        10         20         30         40         50         60 
MNGNKIRTRF APSPTGYMHV GNLRTALYAY LIAKHENGDF LLRIEDTDQE RQVEGALDII 

        70         80         90        100        110        120 
YNTLKMTGIH HDEGPDIGGP VGPYVQSERK HIYTEYAQKL IDKGEAYYCF CTKERLDMLR 

       130        140        150        160        170        180 
ENSESLGRPH KYDKHCSHLS KEEIEENLKA GIPFVIRQNN PNKGTTYFED EIFGKITVDN 

       190        200        210        220        230        240 
SELDDMVLIK SDGFPTYNFA NVVDDHLMGI THVVRGSEYL SSSPKYNRLY DAFGWDVPKY 

       250        260        270        280        290        300 
IHCPPIMKDS HSKLSKRNGD ASFQDLLEKG YLKDAILNYI ALLGWNPGTT EEIFSLEDLI 

       310        320        330        340        350        360 
GKFDYKSINK APAIFDNKKL KWMNGEYIRM FSLEEFHKLA LPYYKGVITK DFDLLKISEL 

       370        380        390        400        410        420 
LHTRTELLSE IPEQVDFFDE LPEYSCDLYV HKKMKTNFEN SLESLEKALP VLESIDNWNT 

       430        440        450        460        470        480 
ETIHDSIMEL IKELEVKNGI VLWPIRTAVS GKKFTPGGAF EIAEILGKEE TLKRVKIGIE 


KLKNEINQ 

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015927 Genomic DNA. Translation: AAO35565.1. Different initiation.
RefSeqNP_781628.1. NC_004557.1.

3D structure databases

ProteinModelPortalQ896M5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING212717.CTC00977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO35565; AAO35565; CTC_00977.
GeneID1058871.
KEGGctc:CTC00977.
PATRIC19509821. VBICloTet101274_0959.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAKLEWYNG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCTET212717:GJAM-893-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_CLOTE
AccessionPrimary (citable) accession number: Q896M5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: May 14, 2014
This is version 74 of the entry and version 2 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