Skip Header

Contribute Send feedback
Read comments (?) or add your own

A9AXJ1 (SYE_HERA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:Haur_0757
OrganismHerpetosiphon aurantiacus (strain ATCC 23779 / DSM 785) [Complete proteome] [HAMAP]
Taxonomic identifier316274 [NCBI]
Taxonomic lineageBacteriaChloroflexiHerpetosiphonalesHerpetosiphonaceaeHerpetosiphon

Protein attributes

Sequence length495 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 By similarity 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 – 495495Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_1000090080

Regions

Motif14 – 2411"HIGH" region HAMAP MF_00022_B
Motif255 – 2595"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9AXJ1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: A7916F5D4F4C7734

FASTA49554,778
        10         20         30         40         50         60 
MSDRPTPART RFAPSPTGYL HIGSLRTVLF SWLWARHTGG QFLLRIEDTD RKRFVEGAEE 

        70         80         90        100        110        120 
QLTSSLQAIG LMWDEGPIVG GPHAPYKQSE RLEIYQAHAQ ALIDKGVAYR SYATADEIAA 

       130        140        150        160        170        180 
INAEREARGE PKLLVFRNLP GIDDAAREAA GADYNVRLSL KTTGQTVVQD LVRGQIVFDN 

       190        200        210        220        230        240 
AALKMPDPVL LKTDGFPTYA LAAMVDDHLM GITHVLRADE WIPTWPIHHQ IYEAFGWEQP 

       250        260        270        280        290        300 
VWVHVPQVLG SDGKKLSKRH GDTSVTEYID LGFVPEAIIN YLALIGWSYD DKTEFMTLEE 

       310        320        330        340        350        360 
LIERFDLNRI RPSGGVFDRD KLLHFNGVYL RNMAPAELAQ RVAPYLSKAG LISAEPTAAE 

       370        380        390        400        410        420 
LAKITEYLPL VQDRLKLLSE APELLDFFFV DPQGYDPALL VPKKGDPAQT VEILGQVKAS 

       430        440        450        460        470        480 
FEAVETWDAP SLDKLLHDFV NQLGLKIPQV FMPIRVAISG RTTSPGLFET LAVLGKAVTL 

       490 
ARISTAAAAL SSASV 

« Hide

References

[1]"Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Bryant D.A., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23779 / DSM 785.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000875 Genomic DNA. Translation: ABX03405.1.
RefSeqYP_001543533.1. NC_009972.1.

3D structure databases

ProteinModelPortalA9AXJ1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9AXJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5732641.
GenomeReviewsGene locus Haur_0757 in contig CP000875_GR.
KEGGhau:Haur_0757.
PATRIC22118459. VBIHerAur93466_0775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAMAHIPLI.

Enzyme and pathway databases

BioCycHAUR316274:HAUR_0757-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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_HERA2
AccessionPrimary (citable) accession number: A9AXJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 30 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