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Reviewed, UniProtKB/Swiss-Prot Q2G6Q3 (SYE2_NOVAD)

Last modified June 16, 2009. Version 22. 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 2
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 2
      Short name=GluRS 2
Gene names
Name: gltX2
Ordered Locus Names: Saro_2031
OrganismNovosphingobium aromaticivorans (strain DSM 12444) [Complete proteome] [HAMAP]
Taxonomic identifier279238 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium

Protein attributes

Sequence length487 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

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
Nucleotide-binding
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Glutamyl-tRNA synthetase 2 HAMAP MF_00022
PRO_0000237381

Regions

Motif24 – 3411"HIGH" region HAMAP MF_00022
Motif258 – 2625"KMSKS" region HAMAP MF_00022

Sites

Binding site2611ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2G6Q3-1 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 8DCC1B1CDBC397A2

FASTA48753,204
        10         20         30         40         50         60 
MASATDTVSA GSTPRDKVVT RFAPSPTGFL HIGGARTALF NWLYARHHGG TYLLRIEDTD 

        70         80         90        100        110        120 
RARSTDAAID AIFDGLEWLG LGGDEPAVFQ FARSDRHAEV AHKLLEAGHA YRCYLTQEEL 

       130        140        150        160        170        180 
AARRELAQAE RRPFRIDSEW RDATPDQWPA DQSYVVRMKA PREGETTIVD KVQGSITVQN 

       190        200        210        220        230        240 
SELDDFIILR SDGTPTYMLA VVVDDHDMGV THVIRGDDHI NNAFRQLVII RGMHAIEGGW 

       250        260        270        280        290        300 
PDPVYAHIPL IHGADGAKLS KRHGALGVDA YRDEMGLLPE AVFNYLLRLG WGHGDEEIIS 

       310        320        330        340        350        360 
REQAVAWFDI GDVNKGASRF DLKKLLNLNG HYIREADDAR LAALVAPRLA TLAPGFAPDK 

       370        380        390        400        410        420 
GLDLLTRAMP VLKVRAADIN ELAAGSVFLF AQRPLAMAEK AASLLTDDAR AILTKVAGVL 

       430        440        450        460        470        480 
EAENVWTTGV LEATVKQMAE ELGIGLGKIA QPLRASLTGQ TTSPGIFDVL ALLGKDESLS 


RIRDQAA 

« Hide

References

[1]"Complete sequence of Novosphingobium aromaticivorans DSM 12444."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N. expand/collapse author list , Fredrickson J., Balkwill D., Romine M.F., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000248 Genomic DNA. Translation: ABD26470.1.
RefSeqYP_497304.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3917678.
GenomeReviewsGene locus Saro_2031 in contig CP000248_GR.
KEGGnar:Saro_2031.
NMPDRfig|48935.1.peg.2297.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2G6Q3.
OMAQ2G6Q3. MARYDAN.

Enzyme and pathway databases

BioCycNARO279238:SARO_2031-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.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA: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.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_NOVAD
AccessionPrimary (citable) accession number: Q2G6Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 21, 2006
Last modified: June 16, 2009
This is version 22 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