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Reviewed, UniProtKB/Swiss-Prot Q3JEF2 (SYE1_NITOC)

Last modified November 3, 2009. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 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.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000237377

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022
Motif236 – 2405"KMSKS" region HAMAP 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
Q3JEF2-1 [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: 16957257] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000127 Genomic DNA. Translation: ABA56794.1.
RefSeqYP_342324.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3JEF2.

Genome annotation databases

GeneID3706338.
GenomeReviewsGene locus Noc_0264 in contig CP000127_GR.
KEGGnoc:Noc_0264.
NMPDRfig|323261.3.peg.870.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3JEF2.
OMAMARYDAN.

Enzyme and pathway databases

BioCycNOCE323261:NOC_0264-MON.

Family and domain databases

HAMAPMF_00022.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
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. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
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: November 3, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents