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Q92F38 (SYE_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:lin0269
OrganismListeria innocua [Complete proteome] [HAMAP]
Taxonomic identifier1642 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length491 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
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: 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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119592

Regions

Motif13 – 2311"HIGH" region HAMAP MF_00022_B
Motif254 – 2585"KMSKS" region HAMAP MF_00022_B

Sites

Metal binding1101Zinc By similarity
Metal binding1121Zinc By similarity
Metal binding1371Zinc By similarity
Metal binding1391Zinc By similarity
Binding site2571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92F38 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: B94060A6A7AC9760

FASTA49156,004
        10         20         30         40         50         60 
MSETKRVRVR YAPSPTGFLH IGNARTALFN YLFARHNDGD FIIRIEDTDA KRNVADGEES 

        70         80         90        100        110        120 
QMKNLKWLGM DWDEGVDVPG KYGPYRQSER QSIYEPLIQQ LLDKGLAYKC YCTEEELEAE 

       130        140        150        160        170        180 
REKQKANGEM PRYSGKCRHL TKEQQAEKEA QGFKPSIRFK VPANETITFN DMVKDDVSFE 

       190        200        210        220        230        240 
SNGIGDFVIA KKDGIPTYNF AVAVDDHLME ISHVLRGDDH ISNTPKQILI YNAFGWEPPI 

       250        260        270        280        290        300 
FGHMTLIVNE SRRKLSKRDG SIIQFIEQYR DLGYLPEALF NFIAMLGWSP EGEEEIFSKE 

       310        320        330        340        350        360 
EFIKMFDPKR LSKSPALFDN VKLTWVNNQY VKKLPLNDVV ELSLPHLQKA GVVSADLDQA 

       370        380        390        400        410        420 
ELDWVHKLVS LYHEQMSYGA EIVPLSEMFF ADAESITFDE EEKAVLAEET VPKVISAFKK 

       430        440        450        460        470        480 
ELEALDVLEA AEVKSAIKRV QKETGVKGKG LFMPIRIVTT GEMHGPELPL AIEVLGLEKV 

       490 
LNRLDTWLQN N

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL596164 Genomic DNA. Translation: CAC95502.1.
PIRAF1466.
RefSeqNP_469614.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ92F38.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1128683.
GenomeReviewsGene locus lin0269 in contig AL592022_GR.
KEGGlin:lin0269.
NMPDRfig|272626.1.peg.267.
PATRIC20297218. VBILisInn102668_0283.

Organism-specific databases

GenoListLIN0269.
CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMADDFDMEI.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLINN272626:LIN0269-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.
KOK09698.
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 nameSYE_LISIN
AccessionPrimary (citable) accession number: Q92F38
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 64 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

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