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A2BVD5 (SYE_PROM5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:P9515_05371
OrganismProchlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP]
Taxonomic identifier167542 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length478 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.

Sequence caution

The sequence ABM71746.1 differs from that shown. Reason: Erroneous initiation.

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 – 478478Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330989

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BVD5 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 3A367BE32BF61D78

FASTA47855,322
        10         20         30         40         50         60 
MEKRLRLAPS PTGLLHIGTA RTALFNWLYA KKTNGKFFIR IEDTDIVRSK SEYTTNILDG 

        70         80         90        100        110        120 
LNWLGLSWDE EPIKQSKRIS IYKKNIKKLL EIGAAYRCFT SESEISELRE KQKSSGLPPR 

       130        140        150        160        170        180 
HDNRHRNLTS NEIKAFLSQG RSSVIRFKID DETEIKWEDQ IRGEIKWKGR DLGGDLVLSR 

       190        200        210        220        230        240 
RALGDEIGDP LYNLAVVVDD NFMNITHVVR GEDHISNTAK QILIYKALNF KLPIFSHTPL 

       250        260        270        280        290        300 
ILNSEGKKLS KRDCVTSIDE FREMGYLPEA LANYMAFLGW SIKDSESEIL SLKEISRVFN 

       310        320        330        340        350        360 
LSDINKAGAK FNWEKLNWIN SQYIKQMELT KLRQLIKNYW DDMGWESPSA EWDLKLINLI 

       370        380        390        400        410        420 
RDSMLLLKDA IDQSKPFFTL SQMQKEGEEF LNNKDETRES LKYILCYLKE ENISTIDSNK 

       430        440        450        460        470 
AKEIIHKISV ENSIKKGILM KSLRVAFFGC LSGPDLIQSW ELFSENKSDI TLIERCLI 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9515.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000552 Genomic DNA. Translation: ABM71746.1. Different initiation.
RefSeqYP_001010853.1. NC_008817.1.

3D structure databases

ProteinModelPortalA2BVD5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167542.P9515_05371.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM71746; ABM71746; P9515_05371.
GeneID4719752.
KEGGpmc:P9515_05371.
PATRIC23014650. VBIProMar113831_0556.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPMAR167542:GI3N-556-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_PROM5
AccessionPrimary (citable) accession number: A2BVD5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 50 of the entry and version 2 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