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Q8RB93 (SYE1_THETN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:TTE0929
OrganismThermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Caldanaerobacter subterraneus subsp. tengcongensis) [Complete proteome] [HAMAP]
Taxonomic identifier273068 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteriaceaeCaldanaerobacter

Protein attributes

Sequence length481 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 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 – 481481Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000119684

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022_B
Motif244 – 2485"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2471ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RB93 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 37CC69781868C394

FASTA48155,544
        10         20         30         40         50         60 
MMSEVRVRFA PSPTGSLHIG GARTALFNWL FARHHGGKFI LRVDDTDLER STEESMRGIL 

        70         80         90        100        110        120 
EGLQWLGIDW DEGPIYQSQR LDEYRKFANK LLEEGKAYYC FCTKEELEEM RKQAEREGRP 

       130        140        150        160        170        180 
FMYTGKCRNL TKEQIENYLK EGKKPVIRLK TPREGKTVVH DIIRGDVEFD NSTIDDFIIM 

       190        200        210        220        230        240 
KSDGMPTYNF ATVVDDYQMG ITHIIRAEEH LSNTPKQILI YEALGVPLPQ FAHVSMVLAP 

       250        260        270        280        290        300 
DRTKLSKRHG ATSVQEFRDQ GYLPEAIVNY ITLLGWAPLD GEEIFDVRKS IREFSLERVS 

       310        320        330        340        350        360 
KNPAVYDVQK LTWINGHYIR SYDLDKLTQA IIPFLQKKGL IGENYDYEYI KKIVSVVRER 

       370        380        390        400        410        420 
EKTLVDIADA MTYYFKEVES YEEKGVQKYF TKEGVVDILK KAAETLKNLE PFNKFTAEEA 

       430        440        450        460        470        480 
YRKLVEELGI SSSALFHPTR LAISGRTFGP GLFDIMEFLG KEKTVARIER AIKFIEENIK 


G 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008691 Genomic DNA. Translation: AAM24185.1.
RefSeqNP_622581.1. NC_003869.1.

3D structure databases

ProteinModelPortalQ8RB93.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID995885.
GenomeReviewsGene locus TTE0929 in contig AE008691_GR.
KEGGtte:TTE0929.
NMPDRfig|273068.3.peg.227.
PATRIC23896538. VBITheTen82880_0929.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMANATIIEM.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycTTEN273068:TTE0929-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 nameSYE1_THETN
AccessionPrimary (citable) accession number: Q8RB93
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2002
Last modified: January 25, 2012
This is version 61 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