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A2BPV5 (SYE_PROMS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:A9601_05281
OrganismProchlorococcus marinus (strain AS9601) [Complete proteome] [HAMAP]
Taxonomic identifier146891 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length476 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 – 476476Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_1000001935

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
A2BPV5 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 9D34A58CE8DBBCAD

FASTA47655,285
        10         20         30         40         50         60 
MEKRLRLAPS PTGLFHIGTA RTALFNWLYA QKIGGKFLIR IEDTDFLRSK SEYTKNILQG 

        70         80         90        100        110        120 
LKWLGLKWDE EPIKQSDRIS IHKSHIKKLL ECGAAYRCFT SEDEISELRE EQKKKGLPPK 

       130        140        150        160        170        180 
HDNRHRSLSK EEIETFISQG RTSVIRFKID EKIVIKWIDQ IRGEIKWQGK DLGGDLVLSR 

       190        200        210        220        230        240 
RAKGYEIGDP LYNLAVVVDD NFMNITHVVR GEDHISNTAK QILIYNALNF NLPTFSHTPL 

       250        260        270        280        290        300 
ILNSEGKKLS KRDCVTSIDE FREMGYLPEA LSNYMAFLGW SPKTADREIL SLEEISEIFD 

       310        320        330        340        350        360 
LSEINKAGAK FSWEKLNWIN SQYIKNMESI KLVEIMRTYW DENGWEPPSQ EWANKLAILI 

       370        380        390        400        410        420 
RDSMTLLKDS IDQSKPFFLI PTIQKEGQDF LENRESKLSL KLILNYLIEK NTIKLNKEKA 

       430        440        450        460        470 
KEIINEISKK HNIKKGILMK SLRVAFFGSL IGPDLIQSWE LFAESKTDRT RIERCL 

« 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: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AS9601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000551 Genomic DNA. Translation: ABM69816.1.
RefSeqYP_001008923.1. NC_008816.1.

3D structure databases

ProteinModelPortalA2BPV5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2BPV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4717226.
GenomeReviewsGene locus A9601_05281 in contig CP000551_GR.
KEGGpmb:A9601_05281.
PATRIC22982527. VBIProMar75723_0527.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADKETAND.
PhylomeDBA2BPV5.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPMAR146891:A9601_05281-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_PROMS
AccessionPrimary (citable) accession number: A2BPV5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: January 25, 2012
This is version 37 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