ID   PRXC_BURPY              Reviewed;         278 AA.
AC   P25026;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Non-heme chloroperoxidase;
DE            EC=1.11.1.-;
DE   AltName: Full=Chloride peroxidase;
DE   AltName: Full=Chloroperoxidase P;
DE            Short=CPO-P;
GN   Name=cpo; Synonyms=cpoP;
OS   Burkholderia pyrrocinia (Pseudomonas pyrrocinia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=60550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8344520; DOI=10.1016/0378-1119(93)90356-8;
RA   Wolfframm C., Lingens F., Mutzel R., van Pee K.-H.;
RT   "Chloroperoxidase-encoding gene from Pseudomonas pyrrocinia: sequence,
RT   expression in heterologous hosts, and purification of the enzyme.";
RL   Gene 130:131-135(1993).
RN   [2]
RP   MUTAGENESIS.
RX   PubMed=7632719; DOI=10.1016/0167-4838(95)00055-y;
RA   Pelletier I., Altenbuchner J., Mattes R.;
RT   "A catalytic triad is required by the non-heme haloperoxidases to perform
RT   halogenation.";
RL   Biochim. Biophys. Acta 1250:149-157(1995).
CC   -!- FUNCTION: Chlorinates and brominates suitable organic compounds.
CC       Involved in the biosynthesis of the antibiotic pyrrolnitrin.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Bacterial non-heme
CC       haloperoxidase / perhydrolase family. {ECO:0000305}.
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DR   EMBL; M60743; AAA02837.1; -; Unassigned_DNA.
DR   PIR; JN0828; JN0828.
DR   AlphaFoldDB; P25026; -.
DR   SMR; P25026; -.
DR   ESTHER; psepy-prxc; Haloperoxidase.
DR   PeroxiBase; 5912; PpyrHalNPrx.
DR   GO; GO:0016691; F:chloride peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Chloride; Direct protein sequencing;
KW   Oxidoreductase; Peroxidase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..278
FT                   /note="Non-heme chloroperoxidase"
FT                   /id="PRO_0000207061"
FT   DOMAIN          24..259
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        97
FT   ACT_SITE        229
FT   ACT_SITE        258
FT   MUTAGEN         97
FT                   /note="S->A,C: Very low activity."
FT                   /evidence="ECO:0000269|PubMed:7632719"
FT   MUTAGEN         229
FT                   /note="D->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:7632719"
FT   MUTAGEN         258
FT                   /note="H->Q: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:7632719"
SQ   SEQUENCE   278 AA;  30454 MW;  BD7BEA57466BE463 CRC64;
     MPYVTTKDNV EIFYKDWGPK DAQPIVFHHG WPLSGDDWDA QMLFFVQKGY RVIAHDRRGH
     GRSAQVSDGH DMDHYAADAF AVVEALDLRN AVHIGHSTGG GEVARYVAND GQPAGRVAKA
     VLVSAVPPLM LKTESNPEGL PIEVFDGFRK ALADNRAQFF LDVPTGPFYG FNRAGATVHQ
     GVIRNWWRQG MEGSAKAHYD GIKAFSETDQ TEDLKSITVP TLVLHGEDDQ IVPIADAALK
     SIKLLQNGTL KTYPGYSHGM LTVNADVLNA DLLAFVQA