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A1U1V3 (SYE_MARAV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:Maqu_1891
OrganismMarinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845)) [Complete proteome] [HAMAP]
Taxonomic identifier351348 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeMarinobacter

Protein attributes

Sequence length493 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

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
Nucleotide-binding
   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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001921

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1U1V3 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 837B332158625415

FASTA49356,592
        10         20         30         40         50         60 
MTVRTRIAPS PTGDPHVGTA YVALFNLCFA RQHGGQFILR IEDTDQARST AESEQDILTA 

        70         80         90        100        110        120 
LRWLGLNWDE GPDVGGPHGP YRQSERKHMY GQYAEDLVTA GHAFYCFRTP EELDAIREER 

       130        140        150        160        170        180 
KAQGLNPGIK GDLELPEEEV KRRLDAGDPY VIRMKVPDEG VCEIQDMLRG TIEIDWAQVD 

       190        200        210        220        230        240 
CQILLKSDGM PTYHLANVVD DHLMGITHVL RGEEWINSAP KHKLLYQYFG WDMPELCHLP 

       250        260        270        280        290        300 
LLRNPDKSKL SKRKNPTSIN FYERMGFLPE AVTNYLGRMG WSMPDEREKF TLDEMIENFD 

       310        320        330        340        350        360 
IQRVSLGGPV FDVEKLRWLN GQWIREELSD EQFMARMQQW WFNQDDLKAL VPHIKGRAEV 

       370        380        390        400        410        420 
FSDVAPMAQF MFSGMLNLKP EDFAHNKLDE SQVKRVLQFA LWKLEAQRHW SKNTIFADIK 

       430        440        450        460        470        480 
ALAKAMDLKM GDFMFSIFVA IAGTPNSWSV MDSMALLGPD MTRSRLRHAL EVMGGFSKKE 

       490 
TKKVEKEYAA LGV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Edwards K., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700491 / DSM 11845 / VT8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000514 Genomic DNA. Translation: ABM18972.1.
RefSeqYP_959159.1. NC_008740.1.

3D structure databases

ProteinModelPortalA1U1V3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351348.Maqu_1891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM18972; ABM18972; Maqu_1891.
GeneID4654328.
KEGGmaq:Maqu_1891.
PATRIC22459086. VBIMarAqu65105_2301.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAHYIKELD.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMHYD351348:GHYZ-1933-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_MARAV
AccessionPrimary (citable) accession number: A1U1V3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 55 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