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Protein

3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase

Gene

lsrF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the transfer of an acetyl moiety from 3-hydroxy-5-phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA.UniRule annotation1 Publication

Catalytic activityi

Glycerone phosphate + acetyl-CoA = 3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A.UniRule annotation1 Publication

Kineticsi

kcat is 127 sec(-1).1 Publication

Manual assertion based on experiment ini

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Active sitei203Schiff-base intermediate with substrateUniRule annotation1 Publication1

      GO - Molecular functioni

      Complete GO annotation...

      Keywords - Molecular functioni

      Transferase

      Keywords - Ligandi

      Schiff base

      Enzyme and pathway databases

      BioCyciEcoCyc:G6804-MONOMER.
      ECOL316407:JW1510-MONOMER.
      MetaCyc:G6804-MONOMER.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      3-hydroxy-5-phosphonooxypentane-2,4-dione thiolaseUniRule annotation (EC:2.3.1.245UniRule annotation1 Publication)
      Gene namesi
      Name:lsrFUniRule annotation
      Synonyms:yneB
      Ordered Locus Names:b1517, JW1510
      OrganismiEscherichia coli (strain K12)
      Taxonomic identifieri83333 [NCBI]
      Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
      Proteomesi
      • UP000000318 Componenti: Chromosome
      • UP000000625 Componenti: Chromosome

      Organism-specific databases

      EcoGeneiEG13810. lsrF.

      Subcellular locationi

      • Cytoplasm UniRule annotation

      GO - Cellular componenti

      Complete GO annotation...

      Keywords - Cellular componenti

      Cytoplasm

      Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Mutagenesisi57D → A: No activiy. 1 Publication1
      Mutagenesisi203K → A: No activiy. 1 Publication1
      Mutagenesisi251D → A: No activiy. 1 Publication1

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      ChainiPRO_00001389451 – 2913-hydroxy-5-phosphonooxypentane-2,4-dione thiolaseAdd BLAST291

      Proteomic databases

      PaxDbiP76143.
      PRIDEiP76143.

      Expressioni

      Inductioni

      In the absence of AI-2, repressed by LsrR. Induced by AI-2, via release of the LsrR repressor. In the absence of glucose, induced by cAMP-CRP by direct binding to the upstream region of the lsr promoter.2 Publications

      Interactioni

      Subunit structurei

      Homodecamer.UniRule annotation1 Publication

      Protein-protein interaction databases

      BioGridi4261350. 7 interactors.
      DIPiDIP-12754N.
      IntActiP76143. 5 interactors.
      STRINGi511145.b1517.

      Structurei

      Secondary structure

      1291
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Helixi34 – 43Combined sources10
      Turni46 – 48Combined sources3
      Beta strandi51 – 55Combined sources5
      Helixi59 – 62Combined sources4
      Helixi71 – 74Combined sources4
      Helixi76 – 81Combined sources6
      Beta strandi83 – 87Combined sources5
      Helixi89 – 95Combined sources7
      Helixi98 – 100Combined sources3
      Beta strandi104 – 107Combined sources4
      Beta strandi109 – 111Combined sources3
      Helixi127 – 132Combined sources6
      Beta strandi136 – 142Combined sources7
      Helixi149 – 164Combined sources16
      Turni165 – 167Combined sources3
      Beta strandi170 – 174Combined sources5
      Helixi184 – 196Combined sources13
      Beta strandi200 – 205Combined sources6
      Turni208 – 210Combined sources3
      Helixi211 – 216Combined sources6
      Beta strandi222 – 225Combined sources4
      Helixi232 – 244Combined sources13
      Beta strandi248 – 253Combined sources6
      Helixi254 – 257Combined sources4
      Beta strandi259 – 261Combined sources3
      Helixi262 – 275Combined sources14
      Helixi279 – 287Combined sources9

      3D structure databases

      Select the link destinations:
      PDBei
      RCSB PDBi
      PDBji
      Links Updated
      PDB entryMethodResolution (Å)ChainPositionsPDBsum
      3GKFX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-291[»]
      3GLCX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-291[»]
      3GNDX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-291[»]
      4P2VX-ray2.51A/B/C/D/E/F/G/H/I/K1-291[»]
      ProteinModelPortaliP76143.
      SMRiP76143.
      ModBaseiSearch...
      MobiDBiSearch...

      Miscellaneous databases

      EvolutionaryTraceiP76143.

      Family & Domainsi

      Sequence similaritiesi

      Belongs to the DeoC/FbaB aldolase family.UniRule annotationCurated

      Phylogenomic databases

      eggNOGiENOG41061GT. Bacteria.
      COG1830. LUCA.
      HOGENOMiHOG000224792.
      InParanoidiP76143.
      KOiK08321.
      OMAiIVRHGHR.
      PhylomeDBiP76143.

      Family and domain databases

      Gene3Di3.20.20.70. 1 hit.
      HAMAPiMF_02052. LsrF. 1 hit.
      InterProiIPR013785. Aldolase_TIM.
      IPR002915. DeoC/FbaB/lacD_aldolase.
      IPR033673. LsrF.
      [Graphical view]
      PfamiPF01791. DeoC. 1 hit.
      [Graphical view]
      PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.
      SMARTiSM01133. DeoC. 1 hit.
      [Graphical view]

      Sequencei

      Sequence statusi: Complete.

      P76143-1 [UniParc]FASTAAdd to basket

      « Hide

              10         20         30         40         50
      MADLDDIKDG KDFRTDQPQK NIPFTLKGCG ALDWGMQSRL SRIFNPKTGK
      60 70 80 90 100
      TVMLAFDHGY FQGPTTGLER IDINIAPLFE HADVLMCTRG ILRSVVPPAT
      110 120 130 140 150
      NRPVVLRASG ANSILAELSN EAVALSMDDA VRLNSCAVAA QVYIGSEYEH
      160 170 180 190 200
      QSIKNIIQLV DAGMKVGMPT MAVTGVGKDM VRDQRYFSLA TRIAAEMGAQ
      210 220 230 240 250
      IIKTYYVEKG FERIVAGCPV PIVIAGGKKL PEREALEMCW QAIDQGASGV
      260 270 280 290
      DMGRNIFQSD HPVAMMKAVQ AVVHHNETAD RAYELYLSEK Q
      Length:291
      Mass (Da):31,893
      Last modified:February 1, 1997 - v1
      Checksum:iD5CC245A5C709F1C
      GO

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      U00096 Genomic DNA. Translation: AAC74590.1.
      AP009048 Genomic DNA. Translation: BAE76457.1.
      PIRiH64905.
      RefSeqiNP_416034.1. NC_000913.3.
      WP_000774165.1. NZ_LN832404.1.

      Genome annotation databases

      EnsemblBacteriaiAAC74590; AAC74590; b1517.
      BAE76457; BAE76457; BAE76457.
      GeneIDi946071.
      KEGGiecj:JW1510.
      eco:b1517.
      PATRICi32118330. VBIEscCol129921_1585.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      U00096 Genomic DNA. Translation: AAC74590.1.
      AP009048 Genomic DNA. Translation: BAE76457.1.
      PIRiH64905.
      RefSeqiNP_416034.1. NC_000913.3.
      WP_000774165.1. NZ_LN832404.1.

      3D structure databases

      Select the link destinations:
      PDBei
      RCSB PDBi
      PDBji
      Links Updated
      PDB entryMethodResolution (Å)ChainPositionsPDBsum
      3GKFX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-291[»]
      3GLCX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-291[»]
      3GNDX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-291[»]
      4P2VX-ray2.51A/B/C/D/E/F/G/H/I/K1-291[»]
      ProteinModelPortaliP76143.
      SMRiP76143.
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi4261350. 7 interactors.
      DIPiDIP-12754N.
      IntActiP76143. 5 interactors.
      STRINGi511145.b1517.

      Proteomic databases

      PaxDbiP76143.
      PRIDEiP76143.

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsemblBacteriaiAAC74590; AAC74590; b1517.
      BAE76457; BAE76457; BAE76457.
      GeneIDi946071.
      KEGGiecj:JW1510.
      eco:b1517.
      PATRICi32118330. VBIEscCol129921_1585.

      Organism-specific databases

      EchoBASEiEB3571.
      EcoGeneiEG13810. lsrF.

      Phylogenomic databases

      eggNOGiENOG41061GT. Bacteria.
      COG1830. LUCA.
      HOGENOMiHOG000224792.
      InParanoidiP76143.
      KOiK08321.
      OMAiIVRHGHR.
      PhylomeDBiP76143.

      Enzyme and pathway databases

      BioCyciEcoCyc:G6804-MONOMER.
      ECOL316407:JW1510-MONOMER.
      MetaCyc:G6804-MONOMER.

      Miscellaneous databases

      EvolutionaryTraceiP76143.
      PROiP76143.

      Family and domain databases

      Gene3Di3.20.20.70. 1 hit.
      HAMAPiMF_02052. LsrF. 1 hit.
      InterProiIPR013785. Aldolase_TIM.
      IPR002915. DeoC/FbaB/lacD_aldolase.
      IPR033673. LsrF.
      [Graphical view]
      PfamiPF01791. DeoC. 1 hit.
      [Graphical view]
      PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.
      SMARTiSM01133. DeoC. 1 hit.
      [Graphical view]
      ProtoNetiSearch...

      Entry informationi

      Entry nameiLSRF_ECOLI
      AccessioniPrimary (citable) accession number: P76143
      Secondary accession number(s): Q2MB99
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: November 1, 1997
      Last sequence update: February 1, 1997
      Last modified: November 2, 2016
      This is version 109 of the entry and version 1 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programProkaryotic Protein Annotation Program

      Miscellaneousi

      Keywords - Technical termi

      3D-structure, Complete proteome, Reference proteome

      Documents

      1. Escherichia coli
        Escherichia coli (strain K12): entries and cross-references to EcoGene
      2. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      3. SIMILARITY comments
        Index of protein domains and families

      Similar proteinsi

      Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
      100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
      90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
      50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.