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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi54IronUniRule annotation1
Metal bindingi58IronUniRule annotation1
Metal bindingi126IronUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processAutoinducer synthesis, Quorum sensing
LigandIron, Metal-binding

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:RBAM_027680
OrganismiBacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum)
Taxonomic identifieri326423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus amyloliquefaciens group
Proteomesi
  • UP000001120 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000048361 – 157S-ribosylhomocysteine lyaseAdd BLAST157

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA7Z800
SMRiA7Z800
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4106762 Bacteria
COG1854 LUCA
HOGENOMiHOG000040372
KOiK07173
OMAiAIHTLEH

Family and domain databases

Gene3Di3.30.1360.80, 1 hit
HAMAPiMF_00091 LuxS, 1 hit
InterProiView protein in InterPro
IPR037005 LuxS_sf
IPR011249 Metalloenz_LuxS/M16
IPR003815 S-ribosylhomocysteinase
PANTHERiPTHR35799 PTHR35799, 1 hit
PfamiView protein in Pfam
PF02664 LuxS, 1 hit
PIRSFiPIRSF006160 AI2, 1 hit
PRINTSiPR01487 LUXSPROTEIN
ProDomiView protein in ProDom or Entries sharing at least one domain
PD013172 S-ribosylhomocysteinase, 1 hit
SUPFAMiSSF63411 SSF63411, 1 hit

Sequencei

Sequence statusi: Complete.

A7Z800-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSVESFELD HNAVVAPYVR HCGVHKVGTD GVVNKFDIRF CQPNKQAMKP
60 70 80 90 100
DTIHTLEHLL AFTIRTHSEK YDHFDIIDIS PMGCQTGYYL VVSGEPTAEE
110 120 130 140 150
IVDLLDATLK EAIDITEIPA ANEKQCGQAK LHDLEGAKRL MRFWLSQDKE

DLLKVFG
Length:157
Mass (Da):17,696
Last modified:October 23, 2007 - v1
Checksum:iD881E19984E730FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000560 Genomic DNA Translation: ABS75126.1
RefSeqiWP_003152237.1, NC_009725.1

Genome annotation databases

EnsemblBacteriaiABS75126; ABS75126; RBAM_027680
KEGGibay:RBAM_027680

Similar proteinsi

Entry informationi

Entry nameiLUXS_BACVZ
AccessioniPrimary (citable) accession number: A7Z800
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: April 25, 2018
This is version 69 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
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Main funding by: National Institutes of Health