Q9XDU6 (LUXS_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-ribosylhomocysteine lyase
EC=4.4.1.21

Alternative name(s):
AI-2 synthesis protein
Autoinducer-2 production protein LuxS

Gene names

Name:	luxS
Ordered Locus Names:	CPE0178

Organism

Clostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

195102 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium perfringens

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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). Ref.3
Catalytic activity	S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. HAMAP-Rule MF_00091
Cofactor	Binds 1 iron ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the LuxS family.

Ontologies

Keywords
Biological process	Autoinducer synthesis Quorum sensing
Ligand	Iron Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC quorum sensing Inferred from electronic annotation. Source: HAMAP
Molecular_function	S-ribosylhomocysteine lyase activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 151	151	S-ribosylhomocysteine lyase HAMAP-Rule MF_00091		PRO_0000172217
Sites
	Metal binding	54	1	Iron By similarity
	Metal binding	58	1	Iron By similarity
	Metal binding	121	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9XDU6 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: F9564886EBF75561	FASTA	151	16,932
	10 20 30 40 50 60 MVKVESFELD HTKVKAPYVR KAGIKIGPKG DIVSKFDLRF VQPNKELLSD KGMHTLEHFL 70 80 90 100 110 120 AGFMREKLDD VIDISPMGCK TGFYLTSFGD IDVKDIIEAL EYSLSKVLEQ EEIPAANELQ 130 140 150 CGSAKLHSLE LAKSHAKQVL ENGISDKFYV E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of novel VirR/VirS-regulated genes in Clostridium perfringens." Banu S., Ohtani K., Yaguchi H., Swe T., Cole S.T., Hayashi H., Shimizu T. Mol. Microbiol. 35:854-864(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 13 / Type A.
[2]	"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater." Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H. Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 13 / Type A.
[3]	"The luxS gene is involved in cell-cell signalling for toxin production in Clostridium perfringens." Ohtani K., Hayashi H., Shimizu T. Mol. Microbiol. 44:171-179(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB028629 Genomic DNA. Translation: BAA81641.1. BA000016 Genomic DNA. Translation: BAB79884.1.
PIR	T43793.
RefSeq	NP_561094.1. NC_003366.1.
3D structure databases
ProteinModelPortal	Q9XDU6.
ModBase	Search...
Protein-protein interaction databases
STRING	195102.CPE0178.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB79884; BAB79884; BAB79884.
GeneID	988419.
KEGG	cpe:CPE0178.
PATRIC	19494236. VBICloPer59675_0235.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1854.
HOGENOM	HOG000040372.
KO	K07173.
OMA	KAPYVRV.
ProtClustDB	PRK02260.
Enzyme and pathway databases
BioCyc	CPER195102:GJFM-203-MONOMER.
Family and domain databases
Gene3D	3.30.1360.80. 1 hit.
HAMAP	MF_00091. LuxS.
InterPro	IPR011249. Metalloenz_LuxS/M16. IPR003815. S-ribosylhomocysteinase. [Graphical view]
Pfam	PF02664. LuxS. 1 hit. [Graphical view]
PIRSF	PIRSF006160. AI2. 1 hit.
PRINTS	PR01487. LUXSPROTEIN.
ProDom	PD013172. S-ribosylhomocysteinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF63411. Metalloenz_metal-bd. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LUXS_CLOPE

Accession

Primary (citable) accession number: Q9XDU6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program