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Q7TUT7 (SYE_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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:PMT_1308
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [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_0000119625

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
Q7TUT7 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 9891E085D9569A1D

FASTA47653,387
        10         20         30         40         50         60 
MKVRVRLAPS PTGTLHIGTA RTAVFNWLFA RHQGGQFLLR IEDTDKERSK PEFTTNILEG 

        70         80         90        100        110        120 
LKWLGLNWDE QPIIQSQHVD DHRAAIQKLL DRDLAYRCYA SETELEAMRE TQKAQGKAPR 

       130        140        150        160        170        180 
YDNRHRDLNP EQEAAFQSEG RTAVVRFRID DDATISWKDL VRGPMHWKGS DLGGDMVISR 

       190        200        210        220        230        240 
RAPAKEIGDP LYNLVVVVDD AAMSISHVIR GEDHIANTAK QLLIYEALGL PIPQFAHTPL 

       250        260        270        280        290        300 
ILNSEGRKLS KRDGVTSISD FQAMGYTAEA MANYMSLLGW SVPEGTDERF TLQQAATVFS 

       310        320        330        340        350        360 
FDRVNKAGAK FDWDKLNWLN SQVLHDLPKD QLLHELKPLW SKAGWALPEE NWCLDLAELL 

       370        380        390        400        410        420 
GPSLTLLKDG VDQARPFFEE PTLQADGLEQ LAVDGAKAGL SNLLDQLDRT SWDGFDVKQA 

       430        440        450        460        470 
QQLLTNAAQA ANVKKGVIMK SLRAALLGRL QGPDLITTWG LLARIGQDLN RLRRCL 

« 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: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE21483.1.
RefSeqNP_895136.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7TUT7.
SMRQ7TUT7. Positions 3-476.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7TUT7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1729270.
GenomeReviewsGene locus PMT_1308 in contig BX548175_GR.
KEGGpmt:PMT1308.
NMPDRfig|74547.1.peg.1303.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADKETAND.
PhylomeDBQ7TUT7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPMAR74547:PMT1308-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_PROMM
AccessionPrimary (citable) accession number: Q7TUT7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 54 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