LUXS_NEIG1
ID LUXS_NEIG1 Reviewed; 168 AA.
AC Q5F534;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=NGO2102;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000255|HAMAP-Rule:MF_00091}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00091};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-Rule:MF_00091};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00091}.
CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000255|HAMAP-
CC Rule:MF_00091}.
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DR EMBL; AE004969; AAW90703.1; -; Genomic_DNA.
DR RefSeq; WP_003687075.1; NC_002946.2.
DR RefSeq; YP_209115.1; NC_002946.2.
DR AlphaFoldDB; Q5F534; -.
DR SMR; Q5F534; -.
DR STRING; 242231.NGO_2102; -.
DR EnsemblBacteria; AAW90703; AAW90703; NGO_2102.
DR GeneID; 66754430; -.
DR KEGG; ngo:NGO_2102; -.
DR PATRIC; fig|242231.10.peg.2543; -.
DR HOGENOM; CLU_107531_2_0_4; -.
DR OMA; GPMGCLT; -.
DR Proteomes; UP000000535; Chromosome.
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 3: Inferred from homology;
KW Autoinducer synthesis; Iron; Lyase; Metal-binding; Quorum sensing;
KW Reference proteome.
FT CHAIN 1..168
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000298015"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091"
SQ SEQUENCE 168 AA; 18623 MW; 374BD83A58B92FBD CRC64;
MPLLDSFKVD HTRMHAPAVR VAKTMTTPKG DTITVFDLRF CIPNKEILPE KGIHTLEHLF
AGFMRDHLNG AGVEIIDISP MGCRTGFYMS LIGTPSEQQV ADAWLASMQD VLNVKDQSKI
PELNEYQCGT YLMHSLAEAQ QIAQNVLARK VAVNRNGDLA LDESLLNA