ID   PRXC_PSEPY              Reviewed;         278 AA.
AC   P25026;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 59.
DE   RecName: Full=Non-heme chloroperoxidase;
DE            EC=1.11.1.10;
DE   AltName: Full=Chloride peroxidase;
DE   AltName: Full=Chloroperoxidase P;
DE            Short=CPO-P;
GN   Name=cpo; Synonyms=cpoP;
OS   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   MEDLINE=93345811; 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   MEDLINE=95359188; 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
RT   perform 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   -!- CATALYTIC ACTIVITY: RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the bacterial non-heme bromo- and chloro-
CC       peroxidases family.
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DR   EMBL; M60743; AAA02837.1; -; Unassigned_DNA.
DR   PIR; JN0828; JN0828.
DR   HSSP; P49323; 1A88.
DR   SMR; P25026; 4-278.
DR   PeroxiBase; 5912; PpyrHalNPrx.
DR   GO; GO:0031404; F:chloride ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016691; F:chloride peroxidase activity; IEA:EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003089; 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.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Chloride; Direct protein sequencing;
KW   Oxidoreductase; Peroxidase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    278       Non-heme chloroperoxidase.
FT                                /FTId=PRO_0000207061.
FT   ACT_SITE     97     97
FT   ACT_SITE    229    229
FT   ACT_SITE    258    258
FT   MUTAGEN      97     97       S->A,C: Very low activity.
FT   MUTAGEN     229    229       D->A: Loss of activity.
FT   MUTAGEN     258    258       H->Q: Loss of activity.
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
//