PER_COPCI
ID PER_COPCI Reviewed; 363 AA.
AC P28314; P28315; Q12575;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peroxidase;
DE EC=1.11.1.7;
DE Flags: Precursor;
GN Name=CIP1;
OS Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=5346;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND PYROGLUTAMATE
RP FORMATION AT GLN-21.
RC STRAIN=NBRC 8371;
RX PubMed=8477731; DOI=10.1111/j.1432-1033.1993.tb17800.x;
RA Baunsgaard L., Dalboege H., Houen G., Rasmussen E.M., Welinder K.G.;
RT "Amino acid sequence of Coprinus macrorhizus peroxidase and cDNA sequence
RT encoding Coprinus cinereus peroxidase. A new family of fungal
RT peroxidases.";
RL Eur. J. Biochem. 213:605-611(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 8371;
RA Dalboege H.;
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 161-185.
RX PubMed=1576150; DOI=10.1016/0167-4838(92)90244-8;
RA Kjalke M., Andersen M.B., Schneider P., Christensen B., Schuelein M.,
RA Welinder K.G.;
RT "Comparison of structure and activities of peroxidases from Coprinus
RT cinereus, Coprinus macrorhizus and Arthromyces ramosus.";
RL Biochim. Biophys. Acta 1120:248-256(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND GLYCOSYLATION AT ASN-162 AND
RP SER-358.
RX PubMed=8112469; DOI=10.1016/0014-5793(94)80433-8;
RA Petersen J.F.W., Kadziola A., Larsen S.;
RT "Three-dimensional structure of a recombinant peroxidase from Coprinus
RT cinereus at 2.6-A resolution.";
RL FEBS Lett. 339:291-296(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS).
RX PubMed=12777760; DOI=10.1107/s0907444903006772;
RA Houborg K., Harris P., Petersen J., Rowland P., Poulsen J.-C.N.,
RA Schneider P., Vind J., Larsen S.;
RT "Impact of the physical and chemical environment on the molecular structure
RT of Coprinus cinereus peroxidase.";
RL Acta Crystallogr. D 59:989-996(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANT.
RX PubMed=12777761; DOI=10.1107/s0907444903006784;
RA Houborg K., Harris P., Poulsen J.-C.N., Schneider P., Svendsen A.,
RA Larsen S.;
RT "The structure of a mutant enzyme of Coprinus cinereus peroxidase provides
RT an understanding of its increased thermostability.";
RL Acta Crystallogr. D 59:997-1003(2003).
RN [7]
RP STRUCTURE BY NMR OF MUTANT ASN-265.
RX PubMed=8916924; DOI=10.1021/bi961582t;
RA Veitch N.C., Gao Y., Welinder K.G.;
RT "The Asp245-->Asn mutant of Coprinus cinereus peroxidase. Characterization
RT by 1H-NMR spectroscopy and comparison with the wild-type enzyme.";
RL Biochemistry 35:14370-14380(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {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; X69457; CAA49216.1; -; mRNA.
DR EMBL; X70789; CAA50060.1; -; Genomic_DNA.
DR PIR; S31780; S31780.
DR PDB; 1H3J; X-ray; 2.00 A; A/B=22-363.
DR PDB; 1LY8; X-ray; 2.05 A; A/B=21-363.
DR PDB; 1LY9; X-ray; 2.00 A; A/B=21-363.
DR PDB; 1LYC; X-ray; 1.57 A; A/B=21-363.
DR PDB; 1LYK; X-ray; 2.00 A; A/B=21-363.
DR PDBsum; 1H3J; -.
DR PDBsum; 1LY8; -.
DR PDBsum; 1LY9; -.
DR PDBsum; 1LYC; -.
DR PDBsum; 1LYK; -.
DR AlphaFoldDB; P28314; -.
DR SMR; P28314; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; PRX2A_COPCI; -.
DR PeroxiBase; 2403; CcinCIIBA.
DR iPTMnet; P28314; -.
DR VEuPathDB; FungiDB:CC1G_02104; -.
DR VEuPathDB; FungiDB:CC2G_002487; -.
DR EvolutionaryTrace; P28314; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00692; ligninase; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF11895; Peroxidase_ext; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..20
FT CHAIN 21..363
FT /note="Peroxidase"
FT /id="PRO_0000023667"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 203
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 71
FT /note="Transition state stabilizer"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8477731"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:8112469"
FT CARBOHYD 358
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:8112469"
FT DISULFID 31..43
FT DISULFID 42..312
FT DISULFID 62..148
FT DISULFID 276..341
FT VARIANT 99
FT /note="I -> V"
FT CONFLICT 119
FT /note="V -> I (in Ref. 2; CAA50060)"
FT /evidence="ECO:0000305"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:1LYC"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:1LYC"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:1LYC"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1LYC"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:1LYC"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1LYC"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:1LYC"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 285..300
FT /evidence="ECO:0007829|PDB:1LYC"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1LYC"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1LYC"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1LYC"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1H3J"
SQ SEQUENCE 363 AA; 37640 MW; E56EB53B963C3DB5 CRC64;
MKLSLLSTFA AVIIGALALP QGPGGGGSVT CPGGQSTSNS QCCVWFDVLD DLQTNFYQGS
KCESPVRKIL RIVFHDAIGF SPALTAAGQF GGGGADGSII AHSNIELAFP ANGGLTDTVE
ALRAVGINHG VSFGDLIQFA TAVGMSNCPG SPRLEFLTGR SNSSQPSPPS LIPGPGNTVT
AILDRMGDAG FSPDEVVDLL AAHSLASQEG LNSAIFRSPL DSTPQVFDTQ FYIETLLKGT
TQPGPSLGFA EELSPFPGEF RMRSDALLAR DSRTACRWQS MTSSNEVMGQ RYRAAMAKMS
VLGFDRNALT DCSDVIPSAV SNNAAPVIPG GLTVDDIEVS CPSEPFPEIA TASGPLPSLA
PAP
