Q8X902 (LUXS_ECO57) 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:	Z3988, ECs3549

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	171 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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-Rule MF_00091
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 171	170	S-ribosylhomocysteine lyase HAMAP-Rule MF_00091		PRO_0000172222
Sites
	Metal binding	54	1	Iron By similarity
	Metal binding	58	1	Iron By similarity
	Metal binding	128	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X902 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1A9457F19962B11A	FASTA	171	19,444
	10 20 30 40 50 60 MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE RGIHTLEHLF 70 80 90 100 110 120 AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADVWKAAMED VLKVQDQNQI 130 140 150 160 170 PELNVYQCGT YQMHSLQEAQ DIARSILERD VRINSNEELA LPKEKLQELH I

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG57796.1. BA000007 Genomic DNA. Translation: BAB36972.1.
PIR	E91072. H85916.
RefSeq	NP_289238.1. NC_002655.2. NP_311576.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X902.
SMR	Q8X902. Positions 3-161.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z3988.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG57796; AAG57796; Z3988. BAB36972; BAB36972; BAB36972.
GeneID	914734. 960942.
KEGG	ece:Z3988. ecs:ECs3549.
PATRIC	18356544. VBIEscCol44059_3460.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1854.
HOGENOM	HOG000040371.
KO	K07173.
OMA	KAPYVRV.
ProtClustDB	PRK02260.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-3513-MONOMER.
BRENDA	4.4.1.21. 2026.
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_ECO57

Accession

Primary (citable) accession number: Q8X902

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program