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   25-MAY-2022, entry version 91.
DE   RecName: Full=Non-heme chloroperoxidase;
DE            EC=1.11.1.-;
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; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=TK64;
RX   PubMed=8157602; DOI=10.1128/jb.176.8.2339-2347.1994;
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   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   -!- 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; U02635; AAA18642.1; -; Unassigned_DNA.
DR   PIR; A55211; A55211.
DR   PDB; 1A88; X-ray; 1.90 A; A/B/C=2-276.
DR   PDBsum; 1A88; -.
DR   AlphaFoldDB; P49323; -.
DR   SMR; P49323; -.
DR   ESTHER; strli-cpoL; Haloperoxidase.
DR   MEROPS; S33.992; -.
DR   PeroxiBase; 5557; SliHalNPrx.
DR   EvolutionaryTrace; P49323; -.
DR   GO; GO:0016691; F:chloride peroxidase activity; IEA:UniProtKB-EC.
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   3D-structure; Chloride; Direct protein sequencing; Oxidoreductase;
KW   Peroxidase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8157602"
FT   CHAIN           2..276
FT                   /note="Non-heme chloroperoxidase"
FT                   /id="PRO_0000207063"
FT   DOMAIN          24..254
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000250|UniProtKB:P22862"
FT   ACT_SITE        227
FT                   /evidence="ECO:0000250|UniProtKB:P22862"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000250|UniProtKB:P22862"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   STRAND          11..18
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           35..38
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           39..47
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   STRAND          51..55
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           72..86
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           99..109
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   STRAND          114..122
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           140..152
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           154..163
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   TURN            164..170
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           178..190
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           193..205
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           209..214
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   STRAND          219..224
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           236..242
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   STRAND          246..251
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           258..261
FT                   /evidence="ECO:0007829|PDB:1A88"
FT   HELIX           263..275
FT                   /evidence="ECO:0007829|PDB:1A88"
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