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Q3JEF2 (SYE1_NITOC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:Noc_0264
OrganismNitrosococcus oceani (strain ATCC 19707 / NCIMB 11848) [Complete proteome] [HAMAP]
Taxonomic identifier323261 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeNitrosococcus

Protein attributes

Sequence length469 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
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: 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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000237377

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3JEF2 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: F103C1F1005D1D0E

FASTA46953,503
        10         20         30         40         50         60 
MTVRTRFAPS PTGYLHVGGV RTALFSWLYA RKHGGRFILR IEDTDRERSS MESVNAILEG 

        70         80         90        100        110        120 
MTWLGLEYDE GPFYQTNRFS RYREIIEQLL ASNHAYLCYC TREELASMRA EQMARKEKPR 

       130        140        150        160        170        180 
YDGRCRERHS PREGVSPVVR FKSPLEGRVV IRDLVRGMVI FQNNELDDLV LARTDGTPTY 

       190        200        210        220        230        240 
NLTVVVDDMD MGMTHVIRGD DHLNNTPRQS NIFYALGKEP PVYAHVPMIL GPDRQRLSKR 

       250        260        270        280        290        300 
HGAVSVMNYR EAGYLPEALL NYLVRLGWSH GDQEIFSVAE MIKLFDIEDV NQSASTFNSE 

       310        320        330        340        350        360 
KLLWLNQQYI KNSAPEHIAH HLSWHLGQLG IDPSKGPDLA AVVKAQQERS KTLLEMAHNS 

       370        380        390        400        410        420 
APFYREFEAY EETAARKHLN ASVLGPLRDL RERFKEAQSW VAPALHEIIL ATVESHHLKL 

       430        440        450        460 
GKLAQPLRVA IMGRPISPPI DVTLELMGQA TTLARIDRAL AWIDHRSNA 

« Hide

References

[1]"Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."
Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., Vergez L.M., Ward B.B.
Appl. Environ. Microbiol. 72:6299-6315(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19707 / NCIMB 11848.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000127 Genomic DNA. Translation: ABA56794.1.
RefSeqYP_342324.1. NC_007484.1.

3D structure databases

ProteinModelPortalQ3JEF2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323261.Noc_0264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA56794; ABA56794; Noc_0264.
GeneID3706338.
KEGGnoc:Noc_0264.
PATRIC22704226. VBINitOce57959_0357.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHYIKELD.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycNOCE323261:GCI3-268-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 nameSYE1_NITOC
AccessionPrimary (citable) accession number: Q3JEF2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 62 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