Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q30UA5 (SYE1_SULDN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Suden_0145
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 length462 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 – 462462Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000237418

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30UA5 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 00E093B1CC2AA922

FASTA46251,928
        10         20         30         40         50         60 
MIVTRFAPSP TGYLHIGGLR TALFSYLWAR KNGGKFLLRI EDTDKARNSQ EAAEAIVKAF 

        70         80         90        100        110        120 
NWLGLEHDGE ITYQSQRDDI YAIYVKQLLD EGKAYRCYMS REELDALRET QMANKERTKY 

       130        140        150        160        170        180 
DGKYRDFDGT PPDGVDSVIR IKAPLSGEII VRDGVKGDVV FKAEDILDDF VIARADGSPT 

       190        200        210        220        230        240 
YNFVVAIDDH LMGVTEVIRG DDHLSNTPKQ IVIYEALGFD VPKFYHVPMI HNSEGKKLSK 

       250        260        270        280        290        300 
RDGATDVMAY KEMGYTPAAL LNFLVRLGWS NGDQEIFSMD EMRELFDPKN INRSASIYNT 

       310        320        330        340        350        360 
EKLDWLNSHY IKNTPNQELA KMLEEYNLTI ASHDKKEILL DALKERAKTL KELALLVTEV 

       370        380        390        400        410        420 
INPPASYDEK ALEKSLKGEA VEVLNNFIAK LSACKELHLP SEYHHVMQEV VDEMGIGFGK 

       430        440        450        460 
IGQPLRVALL GKMSGPGLDS VMAVIGIDET ILRVKSALAL VK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000153 Genomic DNA. Translation: ABB43426.1.
RefSeqYP_392661.1. NC_007575.1.

3D structure databases

ProteinModelPortalQ30UA5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326298.Suden_0145.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB43426; ABB43426; Suden_0145.
GeneID3763762.
KEGGtdn:Suden_0145.
PATRIC23768756. VBISulDen68967_0151.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSDEN326298:GH9P-150-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_SULDN
AccessionPrimary (citable) accession number: Q30UA5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 6, 2005
Last modified: February 19, 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