位置:首页 > 蛋白库 > LUXS_HAEIN
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024