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Q8YAC7 (TILS_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Bifunctional protein TilS/HprT

Including the following 2 domains:

  1. tRNA(Ile)-lysidine synthase
    EC=6.3.4.19
    Alternative name(s):
    tRNA(Ile)-2-lysyl-cytidine synthase
    tRNA(Ile)-lysidine synthetase
  2. Hypoxanthine-guanine phosphoribosyltransferase
    Short name=HGPRT
    Short name=HGPRTase
    EC=2.4.2.8
Gene names
Name:tilS/hprT
Ordered Locus Names:lmo0219
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length648 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine By similarity. HAMAP-Rule MF_01161

Catalytic activity

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01161

GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01161

(tRNA(Ile2))-cytidine34 + L-lysine + ATP = (tRNA(Ile2))-lysidine34 + AMP + diphosphate + H2O. HAMAP-Rule MF_01161

Cofactor

Binds 2 magnesium ions per subunit. One of the ions does not make direct protein contacts By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01161.

Domain

The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding. HAMAP-Rule MF_01161

Sequence similarities

In the N-terminal section; belongs to the tRNA(Ile)-lysidine synthase family.

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 648648Bifunctional protein TilS/HprT HAMAP-Rule MF_01161
PRO_0000181718

Regions

Nucleotide binding29 – 346ATP Potential

Sites

Metal binding6271Magnesium 1 By similarity

Experimental info

Sequence conflict51E → D in AAM74001. Ref.2
Sequence conflict571L → I in AAM74001. Ref.2
Sequence conflict601Q → H in AAM74001. Ref.2
Sequence conflict671K → N in AAM74001. Ref.2
Sequence conflict701R → N in AAM74001. Ref.2
Sequence conflict741T → A in AAM74001. Ref.2
Sequence conflict781R → S in AAM74001. Ref.2
Sequence conflict901I → V in AAM74001. Ref.2
Sequence conflict951Q → E in AAM74001. Ref.2
Sequence conflict1011L → I in AAM74001. Ref.2
Sequence conflict1211N → K in AAM74001. Ref.2
Sequence conflict1261V → A in AAM74001. Ref.2
Sequence conflict2551Q → R in AAM74001. Ref.2
Sequence conflict261 – 2622SS → TN in AAM74001. Ref.2
Sequence conflict3181I → V in AAM74001. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8YAC7 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: DACEA788D7AD5F77

FASTA64874,368
        10         20         30         40         50         60 
MDDTEKRVHK YIEKHDLIRS DDKLLVAVSG GPDSLALLHF LWNSNLVPKE AISVAHLNHQ 

        70         80         90        100        110        120 
LRENAAKEQR VVETFCERQG IPFYIEEVDI KSRAQSLQKG LEETARIVRY DFFEKVMAEK 

       130        140        150        160        170        180 
NINKLVLAHH ADDQIETILM RLVRGSASIG WSGIQPKREL KGGQAIRPFL PITKAEIIDY 

       190        200        210        220        230        240 
AQKHELAYEI DESNTSQEYT RNRYRAQLLP FLKQENPAVY SHFERFSEET SEDFQFLEAL 

       250        260        270        280        290        300 
ASDLLKKNLI KNGKQTTLLL SSFKNEANPL QRRAIHLLLR YLYNEDASFI TVNHIYQIIQ 

       310        320        330        340        350        360 
MIQSDNPSSS IDLPNKLIAN RAYDKLHFQF GEREAPSEFY HQLELNDRIE LDNKASIRLK 

       370        380        390        400        410        420 
LKSSVVQTNG LNGMLLDAEE ITLPLIVRNR VNGDRMTMKG QAGSKKLKDI FIDAKIPRQE 

       430        440        450        460        470        480 
RDKLPVITDY TGKILWVPGV KKSAYDREFS RSKKQYIIRY TRNIGGNESM HNDIQKVLIS 

       490        500        510        520        530        540 
EDELQEKIRE LGRELTTEYE GRNPLVVGVL KGATPFMTDL LKRVDTYLEM DFMDVSSYGN 

       550        560        570        580        590        600 
GTVSSGEVKI IKDLNASVEG RDVLVIEDII DSGRTLSYLV DLIKYRKAKS VKLVTLLDKP 

       610        620        630        640 
AGRNVEIEAD YVGFVVPNEF VVGYGLDYAE RYRNLPYIGI LKPEIYSE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591974 Genomic DNA. Translation: CAD00746.1.
AF467001 Genomic DNA. Translation: AAM74001.1.
PIRAD1102.
RefSeqNP_463750.1. NC_003210.1.

3D structure databases

ProteinModelPortalQ8YAC7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo0219.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD00746; CAD00746; CAD00746.
GeneID987055.
KEGGlmo:lmo0219.
PATRIC20309445. VBILisMon69206_0224.

Organism-specific databases

GenoListLMO0219.

Phylogenomic databases

eggNOGCOG0634.
HOGENOMHOG000217053.
KOK15780.
OMANDISYPL.
OrthoDBEOG693GNP.
PhylomeDBQ8YAC7.

Enzyme and pathway databases

BioCycLMON169963:LMO0219-MONOMER.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_01161. tRNA_Ile_lys_synt.
InterProIPR005904. Hxn_phspho_trans.
IPR012094. Lysidine-tRNA-synth.
IPR012796. Lysidine-tRNA-synth_C.
IPR012795. Lysidine-tRNA-synth_N.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. tRNA-lysidine/thiocyt_synth.
[Graphical view]
PANTHERPTHR11807:SF2. PTHR11807:SF2. 1 hit.
PfamPF01171. ATP_bind_3. 1 hit.
PF00156. Pribosyltran. 1 hit.
PF11734. TilS_C. 1 hit.
[Graphical view]
SMARTSM00977. TilS_C. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
SSF56037. SSF56037. 1 hit.
TIGRFAMsTIGR01203. HGPRTase. 1 hit.
TIGR02433. lysidine_TilS_C. 1 hit.
TIGR02432. lysidine_TilS_N. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTILS_LISMO
AccessionPrimary (citable) accession number: Q8YAC7
Secondary accession number(s): Q8KU03
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families