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A5D5L8 (SYE_PELTS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:PTH_0293
OrganismPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) [Complete proteome] [HAMAP]
Taxonomic identifier370438 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum

Protein attributes

Sequence length480 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 – 480480Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367732

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1051Zinc By similarity
Metal binding1071Zinc By similarity
Metal binding1321Zinc By similarity
Metal binding1341Zinc By similarity
Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5D5L8 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 89F0E27DD52F19CF

FASTA48054,098
        10         20         30         40         50         60 
MVRVRFAPSP TGPLHIGGAR SALFNWLFAR RYGGKFIVRI EDTDLERSSR QSEENILAAL 

        70         80         90        100        110        120 
RWLGLDWDEG VDAGGPCEPY RQTERLHLYR HYAEILLQSG AAYRCYCTEE ELAAEREALM 

       130        140        150        160        170        180 
EKGETPRYLG RCRDLTPQER ARLEAEGRKA AVRFRVPRDR VIQVKDLVRG DVSFECNGMG 

       190        200        210        220        230        240 
DFIIMKSDGI PTYNFAVVVD DHTMAISHVI RAEEHLPNTP RQILLYQALG WDTPEFAHVS 

       250        260        270        280        290        300 
LILGKDRSKM SKRHGATAVE QYREKGYLPE AVVNFLALLG WSPGGENEVL SIEELKQQFS 

       310        320        330        340        350        360 
LEKVSKSPAV FDLDKLNWLN GYYIRQSSLE RVAELAVPFL EKAGYIRAPL SPEEFERVKM 

       370        380        390        400        410        420 
MVASVRKYLN CMEEVIDHVK IYFTDNFNNL DEDAREVMAG QQVPAVLAAL KDKVASGGKL 

       430        440        450        460        470        480 
TGAAARAALK EVGKELGVKG QQIFMPVRVA VSGNTHGPDL DQIMAILGKD EVVKRLSRWV 

« Hide

References

[1]"The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13744 / JCM 10971 / SI.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009389 Genomic DNA. Translation: BAF58474.1.
RefSeqYP_001210843.1. NC_009454.1.

3D structure databases

ProteinModelPortalA5D5L8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370438.PTH_0293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF58474; BAF58474; PTH_0293.
GeneID5139115.
KEGGpth:PTH_0293.
PATRIC22907402. VBIPelThe8413_0328.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPTHE370438:GCGQ-305-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_PELTS
AccessionPrimary (citable) accession number: A5D5L8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 54 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