ID   PRXC_PSEFL              Reviewed;         274 AA.
AC   O31158;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Non-heme chloroperoxidase;
DE            EC=1.11.1.10;
DE   AltName: Full=Chloride peroxidase;
DE   AltName: Full=Chloroperoxidase F;
DE            Short=CPO-F;
GN   Name=cpo; Synonyms=cpoF;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BL914;
RX   MEDLINE=96349119; PubMed=8760926;
RA   Kirner S., Krauss S., Sury G., Lam S.T., Ligon J.M., van Pee K.-H.;
RT   "The non-haem chloroperoxidase from Pseudomonas fluorescens and its
RT   relationship to pyrrolnitrin biosynthesis.";
RL   Microbiology 142:2129-2135(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RC   STRAIN=BL914;
RX   MEDLINE=98307994; PubMed=9642069; DOI=10.1006/jmbi.1998.1802;
RA   Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H.,
RA   Hecht H.-J.;
RT   "Structural investigation of the cofactor-free chloroperoxidases.";
RL   J. Mol. Biol. 279:889-900(1998).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF031153; AAB86577.1; -; Genomic_DNA.
DR   PDB; 1A8S; X-ray; 1.80 A; A=2-274.
DR   PDBsum; 1A8S; -.
DR   PeroxiBase; 5914; PfHalNPrx03_BL914.
DR   BRENDA; 1.11.1.10; 329.
DR   GO; GO:0031404; F:chloride ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016691; F:chloride peroxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloride; Oxidoreductase; Peroxidase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    274       Non-heme chloroperoxidase.
FT                                /FTId=PRO_0000207060.
FT   ACT_SITE     95     95       By similarity.
FT   ACT_SITE    225    225       By similarity.
FT   ACT_SITE    254    254       By similarity.
FT   STRAND        3      5
FT   STRAND       11     18
FT   STRAND       20     26
FT   HELIX        33     36
FT   HELIX        37     45
FT   STRAND       49     53
FT   HELIX        70     83
FT   STRAND       88     94
FT   HELIX        97    108
FT   STRAND      113    120
FT   HELIX       138    161
FT   STRAND      164    166
FT   HELIX       176    188
FT   HELIX       191    203
FT   HELIX       207    211
FT   STRAND      217    222
FT   STRAND      226    228
FT   TURN        231    233
FT   HELIX       234    240
FT   STRAND      245    249
FT   HELIX       256    259
FT   HELIX       261    273
SQ   SEQUENCE   274 AA;  29651 MW;  00E2CF31A99E460F CRC64;
     MTTFTTRDGT QIYYKDWGSG QPIVFSHGWP LNADSWESQM IFLAAQGYRV IAHDRRGHGR
     SSQPWSGNDM DTYADDLAQL IEHLDLRDAV LFGFSTGGGE VARYIGRHGT ARVAKAGLIS
     AVPPLMLKTE ANPGGLPMEV FDGIRQASLA DRSQLYKDLA SGPFFGFNQP GAKSSAGMVD
     WFWLQGMAAG HKNAYDCIKA FSETDFTEDL KKIDVPTLVV HGDADQVVPI EASGIASAAL
     VKGSTLKIYS GAPHGLTDTH KDQLNADLLA FIKG
//