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A8LMK2 (SYE1_DINSH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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 1
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:Dshi_1805
OrganismDinoroseobacter shibae (strain DFL 12) [Complete proteome] [HAMAP]
Taxonomic identifier398580 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Dinoroseobacter

Protein attributes

Sequence length471 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 – 471471Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000330969

Regions

Motif15 – 2511"HIGH" region HAMAP MF_00022_B
Motif243 – 2475"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LMK2 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 4543B982AC18652E

FASTA47150,893
        10         20         30         40         50         60 
MSPTDASPVV TRFAPSPTGY LHIGGARTAL FNWLYARGRG GKFLLRIEDT DKARSTAEAT 

        70         80         90        100        110        120 
EAIFAGLRWL GLDWDGDAVS QAEGAARHAQ VARALQEAGK AYKCFTTQDE IAAFREAARA 

       130        140        150        160        170        180 
EGRSTLFRSP WRDADPASHP DAPYVIRIKA PQEGTTVIAD QVQGDVRIRN DQLDDMILLR 

       190        200        210        220        230        240 
SDGSPVYMLA VVVDDHDMGV THVIRGDDHL NNAARQMMIY DAMGWDMPVF AHIPLIHGPD 

       250        260        270        280        290        300 
GKKLSKRHGA LGVEEYQAMG YPAQAMRNYL ARLGWSHGDD EFFGDAQAQA WFDLDGIGKS 

       310        320        330        340        350        360 
PARLDLKKLD NLSGQHLGVM ADEAIVAGAQ GYLAATGAPP LTEAQETGLS RAMYCLKDRA 

       370        380        390        400        410        420 
KKFPDLLEKA HFILASRPID PDPKAAKSLD TVSRGILAEL TPQLQNASWT RDTLEGVVGG 

       430        440        450        460        470 
LAEAHGLGLG KLAAPLRAAL AGRSATPSVF DMMLVLGRDE TLARLSDATS A

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000830 Genomic DNA. Translation: ABV93547.1.
RefSeqYP_001533148.1. NC_009952.1.

3D structure databases

ProteinModelPortalA8LMK2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8LMK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5712793.
GenomeReviewsGene locus Dshi_1805 in contig CP000830_GR.
KEGGdsh:Dshi_1805.
PATRIC21816261. VBIDinShi9476_1876.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMATEYIRAY.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycDSHI398580:DSHI_1805-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_DINSH
AccessionPrimary (citable) accession number: A8LMK2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 31 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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