PRXC_LEPFU
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 03-AUG-2022, entry version 121.
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RL Unpublished observations (FEB-1996).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};
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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 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 AlphaFoldDB; P04963; -.
DR SMR; P04963; -.
DR PeroxiBase; 4070; CfuHalPrx.
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; -; 1.
DR InterPro; IPR000028; Chloroperoxidase.
DR InterPro; IPR036851; Chloroperoxidase-like_sf.
DR Pfam; PF01328; Peroxidase_2; 1.
DR SUPFAM; SSF47571; SSF47571; 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
