LUXS_HAEIN
ID LUXS_HAEIN Reviewed; 167 AA.
AC P44007;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=S-ribosylhomocysteine lyase;
DE EC=4.4.1.21;
DE AltName: Full=AI-2 synthesis protein;
DE AltName: Full=Autoinducer-2 production protein LuxS;
GN Name=luxS; OrderedLocusNames=HI_0491;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=9719565; DOI=10.1002/elps.1150191046;
RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P.,
RA Langen H.;
RT "Reference map of the low molecular mass proteins of Haemophilus
RT influenzae.";
RL Electrophoresis 19:1819-1827(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RA Chen C.C.H., Parsons J.F., Lim K., Lehmann C., Tempczyk A., Eisenstein E.,
RA Herzberg O.;
RT "Crystal structure of autoinducer-2 production protein (luxS) from
RT Haemophilus influenzae -- a case of twinned crystal.";
RL Submitted (JUL-2001) to the PDB data bank.
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 -!- 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:0000305}.
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DR EMBL; L42023; AAC22149.1; -; Genomic_DNA.
DR PIR; G64008; G64008.
DR RefSeq; NP_438651.1; NC_000907.1.
DR RefSeq; WP_005693682.1; NC_000907.1.
DR PDB; 1J6W; X-ray; 2.10 A; A/B=2-167.
DR PDB; 1JOE; X-ray; 2.40 A; A/B/C/D=1-167.
DR PDBsum; 1J6W; -.
DR PDBsum; 1JOE; -.
DR AlphaFoldDB; P44007; -.
DR SMR; P44007; -.
DR STRING; 71421.HI_0491; -.
DR EnsemblBacteria; AAC22149; AAC22149; HI_0491.
DR KEGG; hin:HI_0491; -.
DR PATRIC; fig|71421.8.peg.510; -.
DR eggNOG; COG1854; Bacteria.
DR HOGENOM; CLU_107531_2_0_6; -.
DR OMA; GPMGCLT; -.
DR PhylomeDB; P44007; -.
DR BioCyc; HINF71421:G1GJ1-506-MON; -.
DR BRENDA; 4.4.1.21; 2529.
DR EvolutionaryTrace; P44007; -.
DR Proteomes; UP000000579; 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 1: Evidence at protein level;
KW 3D-structure; Autoinducer synthesis; Iron; Lyase; Metal-binding;
KW Quorum sensing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..167
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000172227"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:1J6W"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1J6W"
FT STRAND 16..26
FT /evidence="ECO:0007829|PDB:1J6W"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:1J6W"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1J6W"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:1J6W"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1J6W"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1J6W"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:1J6W"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1J6W"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1J6W"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:1J6W"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:1J6W"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1J6W"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1J6W"
SQ SEQUENCE 167 AA; 18527 MW; A8116FE96BA5F817 CRC64;
MPLLDSFKVD HTKMNAPAVR IAKTMLTPKG DNITVFDLRF CIPNKEILSP KGIHTLEHLF
AGFMRDHLNG DSIEIIDISP MGCRTGFYMS LIGTPNEQKV SEAWLASMQD VLGVQDQASI
PELNIYQCGS YTEHSLEDAH EIAKNVIARG IGVNKNEDLS LDNSLLK