Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

S-ribosylhomocysteine lyase

Gene

luxS

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

Functioni

Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).2 Publications

Catalytic activityi

S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.

Cofactori

Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541IronBy similarity
Metal bindingi58 – 581IronBy similarity
Metal bindingi128 – 1281IronBy similarity

GO - Molecular functioni

  • iron ion binding Source: InterPro
  • S-ribosylhomocysteine lyase activity Source: EcoCyc

GO - Biological processi

  • cell-cell signaling involved in quorum sensing Source: EcoCyc
  • L-methionine biosynthetic process from S-adenosylmethionine Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Autoinducer synthesis, Quorum sensing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12712-MONOMER.
ECOL316407:JW2662-MONOMER.
MetaCyc:EG12712-MONOMER.
BRENDAi4.4.1.21. 2026.
SABIO-RKP45578.

Names & Taxonomyi

Protein namesi
Recommended name:
S-ribosylhomocysteine lyase (EC:4.4.1.21)
Alternative name(s):
AI-2 synthesis protein
Autoinducer-2 production protein LuxS
Gene namesi
Name:luxS
Synonyms:ygaG
Ordered Locus Names:b2687, JW2662
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12712. luxS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3496.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 171170S-ribosylhomocysteine lyasePRO_0000172220Add
BLAST

Proteomic databases

EPDiP45578.
PaxDbiP45578.
PRIDEiP45578.

2D gel databases

SWISS-2DPAGEP45578.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4263180. 15 interactions.
DIPiDIP-10131N.
IntActiP45578. 5 interactions.
STRINGi511145.b2687.

Chemistry

BindingDBiP45578.

Structurei

3D structure databases

ProteinModelPortaliP45578.
SMRiP45578. Positions 3-161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.Curated

Phylogenomic databases

eggNOGiENOG4106762. Bacteria.
COG1854. LUCA.
HOGENOMiHOG000040371.
InParanoidiP45578.
KOiK07173.
OMAiAGFMREH.
PhylomeDBiP45578.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS. 1 hit.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamiPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFiPIRSF006160. AI2. 1 hit.
PRINTSiPR01487. LUXSPROTEIN.
ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63411. SSF63411. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P45578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE
60 70 80 90 100
RGIHTLEHLF AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV
110 120 130 140 150
ADAWKAAMED VLKVQDQNQI PELNVYQCGT YQMHSLQEAQ DIARSILERD
160 170
VRINSNEELA LPKEKLQELH I
Length:171
Mass (Da):19,416
Last modified:January 23, 2007 - v3
Checksum:i131F57F1866DA105
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311D → E in AAB40286 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75734.1.
AP009048 Genomic DNA. Translation: BAA16549.1.
U83186 Genomic DNA. Translation: AAB40286.1.
M86657 Genomic DNA. No translation available.
PIRiH65048.
RefSeqiNP_417172.1. NC_000913.3.
WP_001130211.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75734; AAC75734; b2687.
BAA16549; BAA16549; BAA16549.
GeneIDi947168.
KEGGiecj:JW2662.
eco:b2687.
PATRICi32120768. VBIEscCol129921_2781.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75734.1.
AP009048 Genomic DNA. Translation: BAA16549.1.
U83186 Genomic DNA. Translation: AAB40286.1.
M86657 Genomic DNA. No translation available.
PIRiH65048.
RefSeqiNP_417172.1. NC_000913.3.
WP_001130211.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP45578.
SMRiP45578. Positions 3-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263180. 15 interactions.
DIPiDIP-10131N.
IntActiP45578. 5 interactions.
STRINGi511145.b2687.

Chemistry

BindingDBiP45578.
ChEMBLiCHEMBL3496.

2D gel databases

SWISS-2DPAGEP45578.

Proteomic databases

EPDiP45578.
PaxDbiP45578.
PRIDEiP45578.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75734; AAC75734; b2687.
BAA16549; BAA16549; BAA16549.
GeneIDi947168.
KEGGiecj:JW2662.
eco:b2687.
PATRICi32120768. VBIEscCol129921_2781.

Organism-specific databases

EchoBASEiEB2573.
EcoGeneiEG12712. luxS.

Phylogenomic databases

eggNOGiENOG4106762. Bacteria.
COG1854. LUCA.
HOGENOMiHOG000040371.
InParanoidiP45578.
KOiK07173.
OMAiAGFMREH.
PhylomeDBiP45578.

Enzyme and pathway databases

BioCyciEcoCyc:EG12712-MONOMER.
ECOL316407:JW2662-MONOMER.
MetaCyc:EG12712-MONOMER.
BRENDAi4.4.1.21. 2026.
SABIO-RKP45578.

Miscellaneous databases

PROiP45578.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS. 1 hit.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamiPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFiPIRSF006160. AI2. 1 hit.
PRINTSiPR01487. LUXSPROTEIN.
ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63411. SSF63411. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLUXS_ECOLI
AccessioniPrimary (citable) accession number: P45578
Secondary accession number(s): P77134, P77805
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

E.coli strain DH5-alpha does not make AI-2; it has a frameshift mutation in the luxS gene that disrupts the protein coding region.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.