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A4SGA5 (SYE_PROVI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:Cvib_1503
OrganismProsthecochloris vibrioformis (strain DSM 265) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 265)) (Chlorobium phaeovibrioides (strain DSM 265)) [Complete proteome] [HAMAP]
Taxonomic identifier290318 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length521 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 – 521521Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367739

Regions

Motif30 – 4011"HIGH" region HAMAP-Rule MF_00022
Motif277 – 2815"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2801ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SGA5 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: AE751037843FB84D

FASTA52159,828
        10         20         30         40         50         60 
MFLTDGSSLN SLTMTRRMMV GKRVRTRFAP SPTGYLHVGG LRTALYNYLF AKRMDGDFVV 

        70         80         90        100        110        120 
RIEDTDQSRK VADAQENLIK TLEWAGLMPD ESPLHGGDFG PYLQSERLDI YKKYCEQLLE 

       130        140        150        160        170        180 
AGHAYHCFAT SEELEENRQL QLKQGLQPKY NRKWLPEDMG GSMPRSEIQK KLDEGVPSVV 

       190        200        210        220        230        240 
RMKVPDYVSV WFEDIIRGPI EFDSATIDDQ VLMKSDGFPT YHFASVIDDH LMEFTHIIRG 

       250        260        270        280        290        300 
EEWLPSMPKH LLLYEFLGWE PPKYAHLPLL LNPDRSKLSK RQGDVSVEDY IRKGYSGEAI 

       310        320        330        340        350        360 
VNFVALLGWN QGEGCEQEVY SLQELTERFS LERVGKAGSI FTIDKLNWLE KQYIKNRPAE 

       370        380        390        400        410        420 
DIIRVIKPLL LSELEKKETL LDPATITGER YLEDVIELMR ERVGFEREFV TFSSYFFFEP 

       430        440        450        460        470        480 
ETYEEDAVKK RWTPDTNSLL DEFLPVLESM PDFTAEAIEA ALKEFVAPKG LKAAALIHPL 

       490        500        510        520 
RIVSSGVSFG PSLYHMLEVL GREAVVRRIR KGMAVITLPQ Q 

« Hide

References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP37514.1.
RefSeqYP_001131016.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SGA5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290318.Cvib_1503.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP37514; ABP37514; Cvib_1503.
GeneID4970581.
KEGGpvi:Cvib_1503.
PATRIC21397514. VBIChlPha132153_1582.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCPHA290318:GHNQ-1542-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 nameSYE_PROVI
AccessionPrimary (citable) accession number: A4SGA5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 49 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