ID   CLOR_STRRC              Reviewed;         277 AA.
AC   Q8GHB1;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=4-hydroxy-3-prenylphenylpyruvate oxygenase/4-hydroxy-3-prenylbenzoate synthase {ECO:0000303|PubMed:12777382};
DE            EC=1.13.11.83 {ECO:0000269|PubMed:12777382};
DE            EC=1.13.12.23 {ECO:0000269|PubMed:12777382};
DE   AltName: Full=Bifunctional non-heme iron oxygenase {ECO:0000303|PubMed:12777382};
DE   AltName: Full=Clorobiocin biosynthesis protein CloR {ECO:0000303|PubMed:12480894};
GN   Name=cloR {ECO:0000303|PubMed:12480894};
OS   Streptomyces roseochromogenus subsp. oscitans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=149682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=DS 12.976 {ECO:0000312|EMBL:AAN65240.1};
RX   PubMed=12480894; DOI=10.1099/00221287-148-12-3901;
RA   Pojer F., Li S.M., Heide L.;
RT   "Molecular cloning and sequence analysis of the clorobiocin biosynthetic
RT   gene cluster: new insights into the biosynthesis of aminocoumarin
RT   antibiotics.";
RL   Microbiology 148:3901-3911(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND
RP   REACTION MECHANISM.
RC   STRAIN=DS 12.976;
RX   PubMed=12777382; DOI=10.1074/jbc.m303190200;
RA   Pojer F., Kahlich R., Kammerer B., Li S.M., Heide L.;
RT   "CloR, a bifunctional non-heme iron oxygenase involved in clorobiocin
RT   biosynthesis.";
RL   J. Biol. Chem. 278:30661-30668(2003).
CC   -!- FUNCTION: Involved in the biosynthesis of ring A of the aminocoumarin
CC       antibiotic clorobiocin (PubMed:12480894). Catalyzes two consecutive
CC       oxidative decarboxylations of 3-dimethylallyl-4-hydroxyphenylpyruvate
CC       (3DMA-4HPP) to yield 3-dimethylallyl-4-hydroxybenzoate (3DMA-4HB) via
CC       the 3-dimethylallyl-4-hydroxymandelic acid (3DMA-4HMA) intermediate
CC       (PubMed:12777382). {ECO:0000269|PubMed:12480894,
CC       ECO:0000269|PubMed:12777382}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dimethylallyl-4-hydroxyphenylpyruvate + O2 = 3-
CC         dimethylallyl-4-hydroxymandelate + CO2; Xref=Rhea:RHEA:52908,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:74408,
CC         ChEBI:CHEBI:136890; EC=1.13.11.83;
CC         Evidence={ECO:0000269|PubMed:12777382};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dimethylallyl-4-hydroxymandelate + O2 = 3-dimethylallyl-4-
CC         hydroxybenzoate + CO2 + H2O; Xref=Rhea:RHEA:52912, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:74155,
CC         ChEBI:CHEBI:136890; EC=1.13.12.23;
CC         Evidence={ECO:0000269|PubMed:12777382};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:12777382};
CC   -!- ACTIVITY REGULATION: Activated by ascorbate.
CC       {ECO:0000269|PubMed:12777382}.
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:12480894}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12777382}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC       clorobiocin. {ECO:0000269|PubMed:12480894}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. {ECO:0000305}.
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DR   EMBL; AF329398; AAN65240.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GHB1; -.
DR   SMR; Q8GHB1; -.
DR   KEGG; ag:AAN65240; -.
DR   BRENDA; 1.13.11.83; 5951.
DR   BRENDA; 1.13.12.23; 5951.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.225.10; -; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..277
FT                   /note="4-hydroxy-3-prenylphenylpyruvate oxygenase/4-
FT                   hydroxy-3-prenylbenzoate synthase"
FT                   /id="PRO_0000443082"
SQ   SEQUENCE   277 AA;  30496 MW;  AC8883AB954DE28E CRC64;
     MSKALANMPG DDYFRHPPVF DTYAEHRAYL KFRHAVALRH FARLGFDQDG LAGLITVADP
     EHADTYWANP LAHPFSTITP ADLIRVDGDS TETVDGQRRV NIAAFNIHAE IHRARPDVQA
     VIHLHTVYGR AFSAFARKLP PLTQDACPFF EDHEVFDDYT GLVLAKDDGR RIAKQLRGHK
     AILLKNHGLV TVGETLDAAA WWFTLLDTCC HVQLLADAAG GAEPIPAEVA RLTGQQLGSH
     LLGWNSYQPL HEATLARNPD LAAMAPALPP QTPALAR