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Q9X172 (SYE1_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 1
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:TM_1351
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference 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 – 469469Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000119680

Regions

Motif8 – 1811"HIGH" region HAMAP MF_00022_B
Motif250 – 2545"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2531ATP By similarity

Secondary structure

1 .................................................................................. 469
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X172 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: F27D3AB4FE070BD8

FASTA46954,607
        10         20         30         40         50         60 
MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER EYEEKLMESL 

        70         80         90        100        110        120 
RWLGLLWDEG PDVGGDHGPY RQSERVEIYR EHAERLVKEG KAYYVYAYPE EIEEMREKLL 

       130        140        150        160        170        180 
SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI 

       190        200        210        220        230        240 
GDFVIMRSNG LPTYNFACVV DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV 

       250        260        270        280        290        300 
STILGPDGKK LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF 

       310        320        330        340        350        360 
SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID EEYFKKVLEI 

       370        380        390        400        410        420 
TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE ELQNVRWTME EITPVFKKVL 

       430        440        450        460 
KQHGVKPKEF YMTLRRVLTG REEGPELVNI IPLLGKEIFL RRIERSLGG

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Crystal structure of glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (glutamate-tRNA ligase 1) (glurS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution."
Joint center for structural genomics (JCSG)
Submitted (DEC-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD36422.1.
PIRG72264.
RefSeqNP_229152.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O5RX-ray2.34A1-469[»]
ProteinModelPortalQ9X172.
SMRQ9X172. Positions 1-468.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID898129.
GenomeReviewsGene locus TM_1351 in contig AE000512_GR.
KEGGtma:TM1351.
NMPDRfig|243274.1.peg.1336.
PATRIC23937640. VBITheMar51294_1363.
TIGRTM_1351.

Phylogenomic databases

HOGENOMHBG628189.
OMAVRFRMPD.
PhylomeDBQ9X172.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycTMAR243274:TM_1351-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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:1.10.8.70. aa-tRNA-synth_I_codon-bd_sub1. 1 hit.
G3DSA: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.
KOK09698.
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 nameSYE1_THEMA
AccessionPrimary (citable) accession number: Q9X172
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 83 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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