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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
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).

Catalytic activityi

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

Cofactori

Fe cationNote: Binds 1 Fe cation per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551Iron
Metal bindingi59 – 591Iron
Metal bindingi122 – 1221Iron

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. S-ribosylhomocysteine lyase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. quorum sensing Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Autoinducer synthesis, Quorum sensing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciHPYL85963:GJB9-104-MONOMER.

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
Ordered Locus Names:jhp_0097
OrganismiHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
Taxonomic identifieri85963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000804: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152S-ribosylhomocysteine lyasePRO_0000172230Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi85963.jhp0097.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94Combined sources
Beta strandi17 – 2711Combined sources
Beta strandi33 – 408Combined sources
Turni44 – 463Combined sources
Helixi51 – 6818Combined sources
Beta strandi72 – 776Combined sources
Beta strandi81 – 9010Combined sources
Helixi94 – 10815Combined sources
Turni119 – 1213Combined sources
Turni123 – 1264Combined sources
Helixi130 – 14213Combined sources
Helixi144 – 1463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J6XX-ray2.38A/B1-152[»]
ProteinModelPortaliQ9ZMW8.
SMRiQ9ZMW8. Positions 1-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZMW8.

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.Curated

Phylogenomic databases

eggNOGiCOG1854.
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.

Q9ZMW8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKMNVESFNL DHTKVKAPYV RIADRKKGVN GDLIVKYDVR FKQPNRDHMD
60 70 80 90 100
MPSLHSLEHL VAEIIRNHAN YVVDWSPMGC QTGFYLTVLN HDNYTEILEV
110 120 130 140 150
LEKTMQDVLK AKEVPASNEK QCGWAANHTL EGAQNLARAF LDKRAEWSEV

GV
Length:152
Mass (Da):17,424
Last modified:May 1, 1999 - v1
Checksum:iB2E154CF36958315
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001439 Genomic DNA. Translation: AAD05688.1.
PIRiC71973.
RefSeqiNP_222818.1. NC_000921.1.
WP_000783567.1. NC_000921.1.

Genome annotation databases

EnsemblBacteriaiAAD05688; AAD05688; jhp_0097.
GeneIDi889399.
KEGGihpj:jhp0097.
PATRICi20604800. VBIHelPyl98156_0112.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001439 Genomic DNA. Translation: AAD05688.1.
PIRiC71973.
RefSeqiNP_222818.1. NC_000921.1.
WP_000783567.1. NC_000921.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J6XX-ray2.38A/B1-152[»]
ProteinModelPortaliQ9ZMW8.
SMRiQ9ZMW8. Positions 1-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi85963.jhp0097.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD05688; AAD05688; jhp_0097.
GeneIDi889399.
KEGGihpj:jhp0097.
PATRICi20604800. VBIHelPyl98156_0112.

Phylogenomic databases

eggNOGiCOG1854.
KOiK07173.
OMAiKQPNQDH.
OrthoDBiEOG68WRBM.

Enzyme and pathway databases

BioCyciHPYL85963:GJB9-104-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9ZMW8.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: J99 / ATCC 700824.
  2. "A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs."
    Lewis H.A., Furlong E.B., Laubert B., Eroshkina G.A., Batiyenko Y., Adams J.M., Bergseid M.G., Marsh C.D., Peat T.S., Sanderson W.E., Sauder J.M., Buchanan S.G.
    Structure 9:527-537(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).

Entry informationi

Entry nameiLUXS_HELPJ
AccessioniPrimary (citable) accession number: Q9ZMW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 96 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.