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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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).UniRule annotation

Catalytic activityi

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

Cofactori

Fe cationUniRule annotationNote: Binds 1 Fe cation per subunit.UniRule annotation

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Autoinducer synthesis, Quorum sensing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi4.4.1.21. 5712.

Names & Taxonomyi

Protein namesi
Recommended name:
S-ribosylhomocysteine lyaseUniRule annotation (EC:4.4.1.21UniRule annotation)
Alternative name(s):
AI-2 synthesis proteinUniRule annotation
Autoinducer-2 production protein LuxSUniRule annotation
Gene namesi
Name:luxSUniRule annotation
Ordered Locus Names:SF2714, S2901
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 171171S-ribosylhomocysteine lyasePRO_0000172252Add
BLAST

Proteomic databases

PaxDbiQ83JZ4.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF2714.

Structurei

3D structure databases

ProteinModelPortaliQ83JZ4.
SMRiQ83JZ4. Positions 3-161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040371.
KOiK07173.
OMAiKQPNQDH.
OrthoDBiEOG68WRBM.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS.
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.

Q83JZ4-1 [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 DIARSILERE
160 170
VRINSNEELA LPKEKLQELH I
Length:171
Mass (Da):19,430
Last modified:June 1, 2003 - v1
Checksum:i131F57F1866C7A75
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN44206.1.
AE014073 Genomic DNA. Translation: AAP18033.1.
RefSeqiNP_708499.1. NC_004337.2.
WP_001130212.1. NZ_JMRK01000114.1.

Genome annotation databases

EnsemblBacteriaiAAN44206; AAN44206; SF2714.
AAP18033; AAP18033; S2901.
GeneIDi1025700.
KEGGisfl:SF2714.
sfx:S2901.
PATRICi18707461. VBIShiFle31049_3191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN44206.1.
AE014073 Genomic DNA. Translation: AAP18033.1.
RefSeqiNP_708499.1. NC_004337.2.
WP_001130212.1. NZ_JMRK01000114.1.

3D structure databases

ProteinModelPortaliQ83JZ4.
SMRiQ83JZ4. Positions 3-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF2714.

Proteomic databases

PaxDbiQ83JZ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN44206; AAN44206; SF2714.
AAP18033; AAP18033; S2901.
GeneIDi1025700.
KEGGisfl:SF2714.
sfx:S2901.
PATRICi18707461. VBIShiFle31049_3191.

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040371.
KOiK07173.
OMAiKQPNQDH.
OrthoDBiEOG68WRBM.

Enzyme and pathway databases

BRENDAi4.4.1.21. 5712.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS.
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...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiLUXS_SHIFL
AccessioniPrimary (citable) accession number: Q83JZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.