Q83JZ4 (LUXS_SHIFL) 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:	SF2714, S2901

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	171 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-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
	Chain	1 – 171	171	S-ribosylhomocysteine lyase HAMAP-Rule MF_00091		PRO_0000172252
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)
	Q83JZ4 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 131F57F1866C7A75	FASTA	171	19,430
	10 20 30 40 50 60 MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE RGIHTLEHLF 70 80 90 100 110 120 AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMED VLKVQDQNQI 130 140 150 160 170 PELNVYQCGT YQMHSLQEAQ DIARSILERE VRINSNEELA LPKEKLQELH I

References

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005674 Genomic DNA. Translation: AAN44206.1. AE014073 Genomic DNA. Translation: AAP18033.1.
RefSeq	NP_708499.1. NC_004337.2. NP_838223.1. NC_004741.1.
3D structure databases
ProteinModelPortal	Q83JZ4.
SMR	Q83JZ4. Positions 3-161.
ModBase	Search...
Protein-protein interaction databases
STRING	198214.SF2714.
Proteomic databases
PaxDb	Q83JZ4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN44206; AAN44206; SF2714. AAP18033; AAP18033; S2901.
GeneID	1025700. 1079166.
KEGG	sfl:SF2714. sfx:S2901.
PATRIC	18707461. VBIShiFle31049_3191.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1854.
HOGENOM	HOG000040371.
KO	K07173.
OMA	KAPYVRV.
ProtClustDB	PRK02260.
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_SHIFL

Accession

Primary (citable) accession number: Q83JZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program