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Q02W76 (SYE_LACLS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:LACR_2346
OrganismLactococcus lactis subsp. cremoris (strain SK11) [Complete proteome] [HAMAP]
Taxonomic identifier272622 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length483 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 – 483483Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_1000001914

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022_B
Motif255 – 2595"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02W76 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: C720FE0FACA77DB6

FASTA48355,368
        10         20         30         40         50         60 
MNKKIRVRYA PSPTGLLHIG NARTALFNYL FARHHGGDFI IRIEDTDRER HVEDGERSQL 

        70         80         90        100        110        120 
ENLRWLGMDW DESPETHENY RQSERLPLYQ KYIDQLLAEG KAYYSYKTPE ELEADHAKQE 

       130        140        150        160        170        180 
AAGIPPHYIN EYAGMSDDEK AAYIAERKAQ NIEPVVRISV DEKAIYKWND IVKGEIEFEG 

       190        200        210        220        230        240 
GNIGGDWVIQ KRDGYPTYNF AVVVDDHDMQ ISHVIRGDDH IANTPKQLVV YDALGWEAPQ 

       250        260        270        280        290        300 
FGHMTLIINS ETGKKLSKRD TNTLQFIEDY RKKGYMSDAI FNFIALLGWN PGGEKEIFSR 

       310        320        330        340        350        360 
EELIELFDEN RLSKSPAAFD QKKLDWMDNE YIKNADFAKV FELTKPFLLA ANRFDERAQE 

       370        380        390        400        410        420 
LVKLYQPQMK SADEVVELTD LFYGDFPELT DEAREMLAAE TTPLALSTFR AKLAELPESD 

       430        440        450        460        470        480 
FTVENIFPLF KATQKETGVK GKMLWMPIRI AASGSMHGPE LPETIALLGK EKVLAHLDAA 


LNK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000425 Genomic DNA. Translation: ABJ73796.1.
RefSeqYP_811909.1. NC_008527.1.

3D structure databases

ProteinModelPortalQ02W76.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ02W76.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4433965.
GenomeReviewsGene locus LACR_2346 in contig CP000425_GR.
KEGGllc:LACR_2346.
PATRIC22291563. VBILacLac38071_2512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADKETAND.
PhylomeDBQ02W76.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLLAC272622:LACR_2346-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_LACLS
AccessionPrimary (citable) accession number: Q02W76
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: January 25, 2012
This is version 43 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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