LUXS_DEIRA
ID LUXS_DEIRA Reviewed; 158 AA.
AC Q9RRU8;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=S-ribosylhomocysteine lyase {ECO:0000255|HAMAP-Rule:MF_00091};
DE EC=4.4.1.21 {ECO:0000255|HAMAP-Rule:MF_00091};
DE AltName: Full=AI-2 synthesis protein {ECO:0000255|HAMAP-Rule:MF_00091};
DE AltName: Full=Autoinducer-2 production protein LuxS {ECO:0000255|HAMAP-Rule:MF_00091};
GN Name=luxS {ECO:0000255|HAMAP-Rule:MF_00091}; OrderedLocusNames=DR_2387;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=11435117; DOI=10.1016/s0969-2126(01)00613-x;
RA Lewis H.A., Furlong E.B., Laubert B., Eroshkina G.A., Batiyenko Y.,
RA Adams J.M., Bergseid M.G., Marsh C.D., Peat T.S., Sanderson W.E.,
RA Sauder J.M., Buchanan S.G.;
RT "A structural genomics approach to the study of quorum sensing: crystal
RT structures of three LuxS orthologs.";
RL Structure 9:527-537(2001).
CC -!- FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which is
CC secreted by bacteria and is used to communicate both the cell density
CC and the metabolic potential of the environment. The regulation of gene
CC expression in response to changes in cell density is called quorum
CC sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to
CC homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-
CC dihydroxypentane-2,3-dione + L-homocysteine; Xref=Rhea:RHEA:17753,
CC ChEBI:CHEBI:29484, ChEBI:CHEBI:58195, ChEBI:CHEBI:58199; EC=4.4.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00091};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 1 Fe cation per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000255|HAMAP-
CC Rule:MF_00091}.
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DR EMBL; AE000513; AAF11932.1; -; Genomic_DNA.
DR PIR; D75280; D75280.
DR RefSeq; NP_296108.1; NC_001263.1.
DR RefSeq; WP_010889013.1; NZ_CP015081.1.
DR PDB; 1INN; X-ray; 1.80 A; A/B=1-158.
DR PDB; 1J6V; X-ray; 2.10 A; A=1-158.
DR PDB; 1VGX; X-ray; 1.90 A; A/B=1-158.
DR PDB; 1VH2; X-ray; 2.00 A; A=1-158.
DR PDB; 1VJE; X-ray; 1.64 A; A/B=1-158.
DR PDBsum; 1INN; -.
DR PDBsum; 1J6V; -.
DR PDBsum; 1VGX; -.
DR PDBsum; 1VH2; -.
DR PDBsum; 1VJE; -.
DR AlphaFoldDB; Q9RRU8; -.
DR SMR; Q9RRU8; -.
DR STRING; 243230.DR_2387; -.
DR DrugBank; DB02153; 3-sulfino-L-alanine.
DR EnsemblBacteria; AAF11932; AAF11932; DR_2387.
DR KEGG; dra:DR_2387; -.
DR PATRIC; fig|243230.17.peg.2623; -.
DR eggNOG; COG1854; Bacteria.
DR HOGENOM; CLU_107531_2_0_0; -.
DR InParanoid; Q9RRU8; -.
DR OMA; GPMGCLT; -.
DR OrthoDB; 1779617at2; -.
DR BRENDA; 4.4.1.21; 1856.
DR EvolutionaryTrace; Q9RRU8; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1360.80; -; 1.
DR HAMAP; MF_00091; LuxS; 1.
DR InterPro; IPR037005; LuxS_sf.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR003815; S-ribosylhomocysteinase.
DR PANTHER; PTHR35799; PTHR35799; 1.
DR Pfam; PF02664; LuxS; 1.
DR PIRSF; PIRSF006160; AI2; 1.
DR PRINTS; PR01487; LUXSPROTEIN.
DR SUPFAM; SSF63411; SSF63411; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autoinducer synthesis; Iron; Lyase; Metal-binding;
KW Quorum sensing; Reference proteome.
FT CHAIN 1..158
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000172218"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1VJE"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1VJE"
FT STRAND 19..29
FT /evidence="ECO:0007829|PDB:1VJE"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1VJE"
FT HELIX 53..70
FT /evidence="ECO:0007829|PDB:1VJE"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1VJE"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:1VJE"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:1VJE"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1VJE"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:1VJE"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:1VJE"
SQ SEQUENCE 158 AA; 17395 MW; 174CC86C50FB714F CRC64;
MPDMANVESF DLDHTKVKAP YVRLAGVKTT PKGDQISKYD LRFLQPNQGA IDPAAIHTLE
HLLAGYMRDH LEGVVDVSPM GCRTGMYMAV IGEPDEQGVM KAFEAALKDT AGHDQPIPGV
SELECGNYRD HDLAAARQHA RDVLDQGLKV QETILLER
