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B3ERQ7 (SYE_AMOA5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:Aasi_0504
OrganismAmoebophilus asiaticus (strain 5a2) [Complete proteome] [HAMAP]
Taxonomic identifier452471 [NCBI]
Taxonomic lineageBacteriaBacteroidetesCandidatus Amoebophilus

Protein attributes

Sequence length512 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 – 512512Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000367607

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022_B
Motif263 – 2675"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2661ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3ERQ7 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: B2CFC352FC53C85D

FASTA51258,508
        10         20         30         40         50         60 
MEKPIRVRFA PSPTGALHIG GVRTALYNYL LARKHQGKFI LRIEDTDQNR FVPGAEQYII 

        70         80         90        100        110        120 
DTLQWLGIDP DEGIQQGGPF APYRQSDRKD MYRKYADQLV QAGKAYYAFD TPEELEAMRE 

       130        140        150        160        170        180 
RLQAAKVASP QYNAISREWM KNSLTLPQEE VTARINAGEP YVIRFKMPHK EIVRFYDQVR 

       190        200        210        220        230        240 
GWVKVETSTL DDKVLLKSDG MATYHLANVV DDYLMQISHV IRGEEWLPSA PLHILLYQAF 

       250        260        270        280        290        300 
GWEQTMPQFV HLPILLKPEG HGKLSKRDAD KHGFPIFPIA WQDPATGNHI EGFREKGYLP 

       310        320        330        340        350        360 
EALINFLALL GWSPGGDQEL FTKEALVEAF SLERIGKSGV KFDIQKANWF NQQYLRNKTE 

       370        380        390        400        410        420 
KELSVYLTSE LDKREIAYTT EQAEQICALV KERAIFPQDF WEQGQVFFQA PTTYDAQAIQ 

       430        440        450        460        470        480 
KRWTSQAHET LAGFVDILPT ISPFNAASIK ESLADFLKER SIKINEMMPV IRIALMGTTA 

       490        500        510 
GPDLMQSIEI IGQKETIRRL RTALRIIVPV GS 

« Hide

References

[1]"Complete sequence of Candidatus Amoebophilus asiaticus 5a2."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Horn M., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5a2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001102 Genomic DNA. Translation: ACE05909.1.
RefSeqYP_001957638.1. NC_010830.1.

3D structure databases

ProteinModelPortalB3ERQ7.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3ERQ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6376537.
GenomeReviewsGene locus Aasi_0504 in contig CP001102_GR.
KEGGaas:Aasi_0504.
PATRIC21266465. VBICanAmo76781_0583.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAIEWFNLD.
ProtClustDBPRK01406.

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_AMOA5
AccessionPrimary (citable) accession number: B3ERQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 27 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