LUXS_AERS4
ID LUXS_AERS4 Reviewed; 169 AA.
AC A4SIY8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=ASA_0697;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO88860.1; -; Genomic_DNA.
DR RefSeq; WP_005313423.1; NC_009348.1.
DR AlphaFoldDB; A4SIY8; -.
DR SMR; A4SIY8; -.
DR STRING; 382245.ASA_0697; -.
DR EnsemblBacteria; ABO88860; ABO88860; ASA_0697.
DR KEGG; asa:ASA_0697; -.
DR eggNOG; COG1854; Bacteria.
DR HOGENOM; CLU_107531_2_0_6; -.
DR OMA; GPMGCLT; -.
DR OrthoDB; 1779617at2; -.
DR Proteomes; UP000000225; 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.
FT CHAIN 1..169
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000297981"
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 169 AA; 18791 MW; AF4C40294A63EF77 CRC64;
MPLLDSFTVD HTRMEAPAVR VAKTMQTPNK DTITVFDLRF CVPNQEILSE RGIHTLEHLF
AGFMRDHLNG NGVEIIDISP MGCRTGFYMS LIGAPDEARV GAAWQAAMSD VLTVQEQAKI
PELNEYQCGT FSMHSLEEAH EIARNVLARG IGVNHNDELA LPEEKLKSL