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Q30RP4 (SYE2_SULDN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:Suden_1059
OrganismSulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)) [Complete proteome] [HAMAP]
Taxonomic identifier326298 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeSulfurimonas

Protein attributes

Sequence length432 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 – 432432Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367777

Regions

Motif6 – 1611"HIGH" region HAMAP-Rule MF_00022
Motif235 – 2395"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30RP4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: E6E7129BB0460582

FASTA43249,972
        10         20         30         40         50         60 
MLRFAPSPTG DMHIGNLRVA IFNYIVSKQR KEDLVIRIED TDKDRNIEGK DKEILDILNL 

        70         80         90        100        110        120 
FGIDYSVVMY QSENFRFHRA MALQLLQDKR AFNCFCSSDW LDKKREEAKN SKTAYRYDDA 

       130        140        150        160        170        180 
CASLPDELVI DNEHPFTVRI RKPLEPIIIK DHIKGEIKFE PNDIDSFIIM RQDKTPMYNF 

       190        200        210        220        230        240 
ACAVDDMLSD ISLVIRGEDH VSNTPKQILI REALGYSKNI EYAHLPIILN DDGKKMSKRD 

       250        260        270        280        290        300 
DASSVKWLLE EGYLPSAIAN YLILIGNKPP KEIFTIQEAI EWFSLENISK SPARFDINML 

       310        320        330        340        350        360 
KHVNKEHLKI LDAKELSRYV GFADAQIGEV AKIYLEEAST TKELRAKIAL IFAEKNIPDE 

       370        380        390        400        410        420 
FKEYAQTIVK IIQKAPYFEE YEDFKNYIIQ ESGLKGKNFF KPLRILLMGS EHGPDIATVY 

       430 
KHIKNYLGEI VK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000153 Genomic DNA. Translation: ABB44337.1.
RefSeqYP_393572.1. NC_007575.1.

3D structure databases

ProteinModelPortalQ30RP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326298.Suden_1059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB44337; ABB44337; Suden_1059.
GeneID3763816.
KEGGtdn:Suden_1059.
PATRIC23770724. VBISulDen68967_1101.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAYCSKEFL.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSDEN326298:GH9P-1103-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 nameSYE2_SULDN
AccessionPrimary (citable) accession number: Q30RP4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 67 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