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P75114 (SYE_MYCPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MPN_678
ORF Names:MP164
OrganismMycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic identifier272634 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length484 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
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 – 484484Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119608

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022_B
Motif252 – 2565"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P75114 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: FD7B7F4742B09A50

FASTA48455,621
        10         20         30         40         50         60 
MEKIRTRYAP SPTGYLHVGG ARTAIFNFLL AKHFNGEFII RIEDTDTERN VEGGIESQLE 

        70         80         90        100        110        120 
NLRWLGIIPD ESIYNPGNYG PYIQSQKLAT YKKLAYELVG KGLAYRCFCT KEKLEHERQL 

       130        140        150        160        170        180 
ALEHHQTPKY LGTCRNLHSK HIQTNLDNQV PFTIRLKINQ DAEFAWNDQV RGKITIPGNS 

       190        200        210        220        230        240 
LTDIVLLKAN GIATYNFAVV IDDHDMEITD VLRGAEHISN TAYQLAINQA LGYQRIPRFG 

       250        260        270        280        290        300 
HLSVIVDKSG KKLSKRDTKT IQFIEQFKQE GYLPEAVVNF LALLGWNSDF NREFFTINQL 

       310        320        330        340        350        360 
IESFTVNRVV GAPAFFDIKK LQWINAHYIK ELSDNAYFNF IDNYLTIDFD YLKNKRKEVS 

       370        380        390        400        410        420 
LLFKNQLAFG IEINQLIKET FAPKLGVQHL SVKHRELFKE LQSALQQLSE QLQALPDWTK 

       430        440        450        460        470        480 
DNVKSTLTQI GEQFNLKGKK LFMPLRLIFT NKEHGPDLAG IMVLHGKTQV LALLQEFIHA 


TNLF 

« Hide

References

[1]"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
Nucleic Acids Res. 24:4420-4449(1996) [PubMed: 8948633] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29342 / M129.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00089 Genomic DNA. Translation: AAB95812.1.
PIRS73490.
RefSeqNP_110367.1. NC_000912.1.

3D structure databases

ProteinModelPortalP75114.
ModBaseSearch...

Protein-protein interaction databases

IntActP75114. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID877376.
GenomeReviewsGene locus MPN_678 in contig U00089_GR.
KEGGmpn:MPN678.
PATRIC20022845. VBIMycPne110_0745.

Phylogenomic databases

HOGENOMHBG628189.
OMAESIIQFV.
PhylomeDBP75114.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycMPNE272634:MPN678-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_MYCPN
AccessionPrimary (citable) accession number: P75114
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 79 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

Mycoplasma pneumoniae

Mycoplasma pneumoniae (strain M129): entries and gene names

SIMILARITY comments

Index of protein domains and families