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Q7V2K3 (SYE_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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:PMM0473
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119626

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022_B
Motif248 – 2525"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V2K3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: E77F0448B7960EC3

FASTA47855,384
        10         20         30         40         50         60 
MEKHLRLAPS PTGLLHIGTA RTALFNWLYA RKINGKFLIR IEDTDIVRSK SEYTTNILNG 

        70         80         90        100        110        120 
LNWLGLNWDE EPINQSKRVS VHKNYIKRLL ESGAAYRCFT SESEILDLRE KQKKSGLPPK 

       130        140        150        160        170        180 
HDNRHRNLTR KEIKEFISQG KSSVIRFKID EETEIKWEDQ IRGEIKWQGK DLGGDLVLSR 

       190        200        210        220        230        240 
RALGDEIGNP LYNLAVVVDD NFMNITHVVR GEDHISNTAK QILIYKALNF KLPIFAHTPL 

       250        260        270        280        290        300 
ILNSEGKKLS KRDSVTSIDE FKEMGYLPEA LANYMAFLGW SIKSPESEIL SLSEISKVFN 

       310        320        330        340        350        360 
LSDVNKAGAK FNWEKLNWIN SQYIKKMELT QLCKFIKKYW EEMGWESPSS EWDLKLTNLI 

       370        380        390        400        410        420 
QDSMILLKDA IDQSKPFFIL SQMKKEGEEF LESKKEVKES LKYILFYLKE ANITKVNKDN 

       430        440        450        460        470 
AREIINKIIV NHSIKKGILM KSLRVAFFGC LSGPDLIQSW ELFSENKIDI PLIERCFN 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE18932.1.
RefSeqNP_892591.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V2K3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V2K3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1726650.
GenomeReviewsGene locus PMM0473 in contig BX548174_GR.
KEGGpmm:PMM0473.
NMPDRfig|59919.1.peg.470.
PATRIC23031710. VBIProMar68066_0527.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADKETAND.
PhylomeDBQ7V2K3.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPMAR167540:PMM0473-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_PROMP
AccessionPrimary (citable) accession number: Q7V2K3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families