O50164 (LUXS_BORBU) 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:	BB_0377

Organism

Borrelia burgdorferi (Lyme disease spirochete)

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	157 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) By similarity. HAMAP MF_00091
Catalytic activity	S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. HAMAP MF_00091
Cofactor	Binds 1 iron ion per subunit By similarity. HAMAP MF_00091
Subunit structure	Homodimer By similarity. HAMAP MF_00091
Sequence similarities	Belongs to the LuxS family.
Sequence caution	The sequence AAC66762.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Autoinducer synthesis Quorum sensing
Ligand	Iron Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	quorum sensing Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	S-ribosylhomocysteine lyase activity Inferred from electronic annotation. Source: EC 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 – 157	157	S-ribosylhomocysteine lyase HAMAP MF_00091		PRO_0000172212
Sites
	Metal binding	53	1	Iron By similarity
	Metal binding	57	1	Iron By similarity
	Metal binding	124	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	O50164 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 89C3844C37BB7504	FASTA	157	18,098
	10 20 30 40 50 60 MKKITSFTID HTKLNPGIYV SRKDTFENVI FTTIDIRIKA PNIEPIIENA AIHTIEHIGA 70 80 90 100 110 120 TLLRNNEVWT EKIVYFGPMG CRTGFYLIIF GDYESKDLVD LVSWLFSEIV NFSEPIPGAS 130 140 150 DKECGNYKEH NLDMAKYESS KYLQILNNIK EENLKYP

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC66762.1. Different initiation.
PIR	H70146.
RefSeq	NP_212511.2. NC_001318.1.
3D structure databases
ProteinModelPortal	O50164.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000009026; EBBORP00000008356; EBBORG00000009025.
GeneID	1195214.
GenomeReviews	Gene locus BB_0377 in contig AE000783_GR.
KEGG	bbu:BB0377.
NMPDR	fig|224326.1.peg.761.
PATRIC	20557364. VBIBorBur75917_0772.
TIGR	BB_0377.
Phylogenomic databases
GeneTree	EBGT00050000007432.
HOGENOM	HBG347473.
OMA	TTFDIRM.
PhylomeDB	O50164.
ProtClustDB	PRK02260.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0377-MONOMER.
Family and domain databases
HAMAP	MF_00091. LuxS. [Tree]
InterPro	IPR011249. Metalloenz_metal-bd. IPR003815. S-ribosylhomocysteinase. [Graphical view]
Gene3D	G3DSA:3.30.1360.80. S-ribosylhomocysteinase. 1 hit.
KO	K07173.
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_BORBU

Accession

Primary (citable) accession number: O50164

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program