ID   PRXC_STRLI              Reviewed;         276 AA.
AC   P49323;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-DEC-2008, entry version 54.
DE   RecName: Full=Non-heme chloroperoxidase;
DE            EC=1.11.1.10;
DE   AltName: Full=Chloride peroxidase;
DE   AltName: Full=Chloroperoxidase L;
DE            Short=CPO-L;
GN   Name=cpo; Synonyms=cpoL;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=TK64;
RX   MEDLINE=94209235; PubMed=8157602;
RA   Bantleon R., Altenbuchner J., van Pee K.-H.;
RT   "Chloroperoxidase from Streptomyces lividans: isolation and
RT   characterization of the enzyme and the corresponding gene.";
RL   J. Bacteriol. 176:2339-2347(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RC   STRAIN=TK64;
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.
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DR   EMBL; U02635; AAA18642.1; -; Unassigned_DNA.
DR   PIR; A55211; A55211.
DR   PDB; 1A88; X-ray; 1.90 A; A/B/C=1-276.
DR   PDBsum; 1A88; -.
DR   PeroxiBase; 5557; SliHalNPrx.
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; 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   3D-structure; Chloride; Direct protein sequencing; Oxidoreductase;
KW   Peroxidase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    276       Non-heme chloroperoxidase.
FT                                /FTId=PRO_0000207063.
FT   ACT_SITE     97     97       By similarity.
FT   ACT_SITE    227    227       By similarity.
FT   ACT_SITE    256    256       By similarity.
FT   STRAND        3      5
FT   STRAND       11     18
FT   STRAND       24     28
FT   HELIX        35     38
FT   HELIX        39     47
FT   STRAND       51     55
FT   HELIX        72     86
FT   STRAND       90     96
FT   HELIX        99    109
FT   STRAND      114    122
FT   HELIX       140    152
FT   HELIX       154    163
FT   TURN        164    170
FT   HELIX       178    190
FT   HELIX       193    205
FT   HELIX       209    214
FT   STRAND      219    224
FT   STRAND      228    230
FT   TURN        233    235
FT   HELIX       236    242
FT   STRAND      246    251
FT   HELIX       258    261
FT   HELIX       263    275
SQ   SEQUENCE   276 AA;  29914 MW;  CF8977B0C1FA53B0 CRC64;
     MGTVTTSDGT NIFYKDWGPR DGLPVVFHHG WPLSADDWDN QMLFFLSHGY RVIAHDRRGH
     GRSDQPSTGH DMDTYAADVA ALTEALDLRG AVHIGHSTGG GEVARYVARA EPGRVAKAVL
     VSAVPPVMVK SDTNPDGLPL EVFDEFRAAL AANRAQFYID VPSGPFYGFN REGATVSQGL
     IDHWWLQGMM GAANAHYECI AAFSETDFTD DLKRIDVPVL VAHGTDDQVV PYADAAPKSA
     ELLANATLKS YEGLPHGMLS THPEVLNPDL LAFVKS
//