ID PRXC_LEPFU Reviewed; 373 AA. AC P04963; Q92216; Q9HFP2; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 3. DT 27-MAR-2024, entry version 124. DE RecName: Full=Chloroperoxidase; DE EC=1.11.1.10; DE AltName: Full=Chloride peroxidase; DE Short=CPO; DE Flags: Precursor; GN Name=CPO; OS Leptoxyphium fumago (Caldariomyces fumago). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Dothideomycetidae; Capnodiales; Capnodiaceae; Leptoxyphium. OX NCBI_TaxID=5474; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 16373 / DSM 1256 / SC 3815 / VTT D-02910; RX PubMed=3774552; DOI=10.1093/nar/14.20.8061; RA Fang G.-H., Kenigsberg P., Axley M.J., Nuell M., Hager L.P.; RT "Cloning and sequencing of chloroperoxidase cDNA."; RL Nucleic Acids Res. 14:8061-8071(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2828306; DOI=10.1128/jb.170.2.1007-1011.1988; RA Nuell M.J., Fang G.-H., Axley M.J., Kenigsberg P., Hager L.P.; RT "Isolation and nucleotide sequence of the chloroperoxidase gene from RT Caldariomyces fumago."; RL J. Bacteriol. 170:1007-1011(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11278701; DOI=10.1074/jbc.m010571200; RA Conesa A., an de Velde F., van Rantwijk F., Sheldon R.A., RA van den Hondel C.A.M.J.J., Punt P.J.; RT "Expression of the Caldariomyces fumago Chloroperoxidase in Aspergillus RT niger and characterization of the recombinant enzyme."; RL J. Biol. Chem. 276:17635-17640(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-175. RX PubMed=3771564; DOI=10.1016/s0021-9258(18)66829-2; RA Axley M.J., Kenigsberg P., Hager L.P.; RT "Fructose induces and glucose represses chloroperoxidase mRNA levels."; RL J. Biol. Chem. 261:15058-15061(1986). RN [5] RP SEQUENCE REVISION TO C-TERMINUS. RA Hager L.P.; RL Unpublished observations (FEB-1996). RN [6] RP DETERMINATION OF HEME LIGAND. RX PubMed=3198598; DOI=10.1016/s0021-9258(18)37345-9; RA Blanke S.R., Hager L.P.; RT "Identification of the fifth axial heme ligand of chloroperoxidase."; RL J. Biol. Chem. 263:18739-18743(1988). RN [7] RP MUTAGENESIS OF CYS-50. RX PubMed=10535936; DOI=10.1073/pnas.96.22.12412; RA Yi X., Mroczko M., Manoj K.M., Wang X., Hager L.P.; RT "Replacement of the proximal heme thiolate ligand in chloroperoxidase with RT a histidine residue."; RL Proc. Natl. Acad. Sci. U.S.A. 96:12412-12417(1999). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND PYROGLUTAMATE FORMATION AT RP GLN-21. RC STRAIN=ATCC 16373 / DSM 1256 / SC 3815 / VTT D-02910; RX PubMed=8747463; DOI=10.1016/s0969-2126(01)00274-x; RA Sundaramoorthy M., Terner J., Poulos T.L.; RT "The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome RT P450 functional hybrid."; RL Structure 3:1367-1377(1995). CC -!- FUNCTION: Catalyzes peroxidative halogenations involved in the CC biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). CC The enzyme also has potent catalase activity and in the absence of CC halide ion, acts as a peroxidase similar to plant peroxidases. CC -!- CATALYTIC ACTIVITY: CC Reaction=RH + Cl(-) + H2O2 = RCl + 2 H2O.; EC=1.11.1.10; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 Mn(2+) ion per subunit.; CC -!- PTM: N- and O-glycosylated. CC -!- SIMILARITY: Belongs to the chloroperoxidase family. {ECO:0000305}. CC -!- CAUTION: The O-glycosylation on Ser-269 is identified in PubMed:8747463 CC as D-xylose based on weak electron density. Such a modification has not CC been reported in the fungi, and the saccharide is probably D-mannose as CC at the other positions. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA33026.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA28172.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04486; CAA28172.1; ALT_FRAME; mRNA. DR EMBL; M19025; AAA33026.1; ALT_FRAME; Genomic_DNA. DR EMBL; AJ300448; CAC16733.1; -; Genomic_DNA. DR EMBL; M28651; AAA33025.1; -; mRNA. DR PIR; A28557; A28557. DR PDB; 1CPO; X-ray; 1.90 A; A=22-319. DR PDB; 2CIV; X-ray; 1.80 A; A=22-319. DR PDB; 2CIW; X-ray; 1.15 A; A=22-319. DR PDB; 2CIX; X-ray; 1.80 A; A=22-319. DR PDB; 2CIY; X-ray; 1.70 A; A=22-319. DR PDB; 2CIZ; X-ray; 1.30 A; A=22-319. DR PDB; 2CJ0; X-ray; 1.75 A; A=22-319. DR PDB; 2CJ1; X-ray; 1.70 A; A=22-319. DR PDB; 2CJ2; X-ray; 1.60 A; A=22-319. DR PDB; 2CPO; X-ray; 2.10 A; A=22-319. DR PDB; 2J18; X-ray; 1.75 A; A=22-319. DR PDB; 2J19; X-ray; 1.75 A; A=22-319. DR PDB; 2J5M; X-ray; 1.75 A; A=22-319. DR PDB; 7RST; X-ray; 1.69 A; A=21-319. DR PDBsum; 1CPO; -. DR PDBsum; 2CIV; -. DR PDBsum; 2CIW; -. DR PDBsum; 2CIX; -. DR PDBsum; 2CIY; -. DR PDBsum; 2CIZ; -. DR PDBsum; 2CJ0; -. DR PDBsum; 2CJ1; -. DR PDBsum; 2CJ2; -. DR PDBsum; 2CPO; -. DR PDBsum; 2J18; -. DR PDBsum; 2J19; -. DR PDBsum; 2J5M; -. DR PDBsum; 7RST; -. DR AlphaFoldDB; P04963; -. DR SMR; P04963; -. DR PeroxiBase; 4070; CfuHalPrx. DR GlyCosmos; P04963; 14 sites, No reported glycans. DR BRENDA; 1.11.1.10; 1053. DR EvolutionaryTrace; P04963; -. DR GO; GO:0016691; F:chloride peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.489.10; Chloroperoxidase-like; 1. DR InterPro; IPR000028; Chloroperoxidase. DR InterPro; IPR036851; Chloroperoxidase-like_sf. DR PANTHER; PTHR33577:SF9; PEROXIDASE STCC; 1. DR PANTHER; PTHR33577; STERIGMATOCYSTIN BIOSYNTHESIS PEROXIDASE STCC-RELATED; 1. DR Pfam; PF01328; Peroxidase_2; 1. DR SUPFAM; SSF47571; Cloroperoxidase; 2. DR PROSITE; PS51405; HEME_HALOPEROXIDASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Chloride; Cleavage on pair of basic residues; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heme; Iron; KW Manganese; Metal-binding; Oxidoreductase; Peroxidase; KW Pyrrolidone carboxylic acid; Signal. FT SIGNAL 1..20 FT CHAIN 21..319 FT /note="Chloroperoxidase" FT /id="PRO_0000023631" FT PROPEP 322..373 FT /id="PRO_0000023632" FT ACT_SITE 204 FT BINDING 50 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT BINDING 125 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 126 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 129 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT MOD_RES 21 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:8747463" FT CARBOHYD 33 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 114 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 237 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 259 FT /note="O-linked (Man) threonine" FT CARBOHYD 260 FT /note="O-linked (Man) serine" FT CARBOHYD 262 FT /note="O-linked (Man) serine" FT CARBOHYD 263 FT /note="O-linked (Man) serine" FT CARBOHYD 269 FT /note="O-linked (Man) serine" FT /evidence="ECO:0000305" FT CARBOHYD 271 FT /note="O-linked (Man) threonine" FT CARBOHYD 272 FT /note="O-linked (Man) serine" FT CARBOHYD 273 FT /note="O-linked (Man) threonine" FT CARBOHYD 296 FT /note="O-linked (Man...) threonine" FT CARBOHYD 304 FT /note="O-linked (Man...) threonine" FT CARBOHYD 314 FT /note="O-linked (Man...) threonine" FT DISULFID 100..108 FT MUTAGEN 50 FT /note="C->H: Retains most of the chlorination, FT peroxidation, epoxidation, and catalase activities." FT /evidence="ECO:0000269|PubMed:10535936" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:2CIW" FT TURN 27..31 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 51..58 FT /evidence="ECO:0007829|PDB:2CIW" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 71..82 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 86..104 FT /evidence="ECO:0007829|PDB:2CIW" FT STRAND 111..115 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:2CIW" FT TURN 121..124 FT /evidence="ECO:0007829|PDB:2CIW" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 153..162 FT /evidence="ECO:0007829|PDB:2CIW" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:2CIW" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 171..188 FT /evidence="ECO:0007829|PDB:2CIW" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 198..212 FT /evidence="ECO:0007829|PDB:2CIW" FT TURN 218..222 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 228..237 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:2CIW" FT HELIX 255..267 FT /evidence="ECO:0007829|PDB:2CIW" FT TURN 311..314 FT /evidence="ECO:0007829|PDB:1CPO" SQ SEQUENCE 373 AA; 40504 MW; B90085902112E83D CRC64; MFSKVLPFVG AVAALPHSVR QEPGSGIGYP YDNNTLPYVA PGPTDSRAPC PALNALANHG YIPHDGRAIS RETLQNAFLN HMGIANSVIE LALTNAFVVC EYVTGSDCGD SLVNLTLLAE PHAFEHDHSF SRKDYKQGVA NSNDFIDNRN FDAETFQTSL DVVAGKTHFD YADMNEIRLQ RESLSNELDF PGWFTESKPI QNVESGFIFA LVSDFNLPDN DENPLVRIDW WKYWFTNESF PYHLGWHPPS PAREIEFVTS ASSAVLAASV TSTPSSLPSG AIGPGAEAVP LSFASTMTPF LLATNAPYYA QDPTLGPNDK REAAPAATTS MAVFKNPYLE AIGTQDIKNQ QAYVSSKAAA MASAMAANKA RNL //