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-APR-2013, entry version 100.
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;
OC Agaricomycetes; Agaricomycetidae; Agaricales; Psathyrellaceae;
OC Coprinopsis.
OX NCBI_TaxID=5346;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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
RT sequence 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
RP AND 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
RT structure 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
RT provides 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.
RT Characterization by 1H-NMR spectroscopy and comparison with the wild-
RT type enzyme.";
RL Biochemistry 35:14370-14380(1996).
CC -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl
CC radical of the donor + 2 H(2)O.
CC -!- COFACTOR: Binds 2 calcium ions per subunit.
CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC subunit.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
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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 ProteinModelPortal; P28314; -.
DR SMR; P28314; 28-363.
DR mycoCLAP; PRXA_COPCI; -.
DR PeroxiBase; 2403; CcinCIIBA.
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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR010255; Haem_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR Pfam; PF11895; DUF3415; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Peroxidase_super; 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;
KW Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted;
KW Signal.
FT SIGNAL 1 20
FT CHAIN 21 363 Peroxidase.
FT /FTId=PRO_0000023667.
FT ACT_SITE 75 75 Proton acceptor.
FT METAL 76 76 Calcium 1.
FT METAL 94 94 Calcium 1; via carbonyl oxygen.
FT METAL 96 96 Calcium 1.
FT METAL 98 98 Calcium 1.
FT METAL 203 203 Iron (heme axial ligand).
FT METAL 204 204 Calcium 2.
FT METAL 221 221 Calcium 2.
FT METAL 223 223 Calcium 2.
FT METAL 226 226 Calcium 2; via carbonyl oxygen.
FT METAL 228 228 Calcium 2.
FT SITE 71 71 Transition state stabilizer.
FT MOD_RES 21 21 Pyrrolidone carboxylic acid.
FT CARBOHYD 162 162 N-linked (GlcNAc...) (high mannose).
FT CARBOHYD 358 358 O-linked (Man...).
FT DISULFID 31 43
FT DISULFID 42 312
FT DISULFID 62 148
FT DISULFID 276 341
FT VARIANT 99 99 I -> V.
FT CONFLICT 119 119 V -> I (in Ref. 2; CAA50060).
FT STRAND 36 39
FT HELIX 40 42
FT HELIX 45 54
FT TURN 55 60
FT HELIX 64 77
FT HELIX 82 86
FT STRAND 94 96
FT HELIX 98 101
FT HELIX 103 106
FT HELIX 110 112
FT HELIX 116 129
FT HELIX 133 146
FT HELIX 179 189
FT HELIX 193 199
FT HELIX 200 205
FT STRAND 207 211
FT HELIX 213 215
FT STRAND 218 222
FT HELIX 230 235
FT STRAND 244 246
FT STRAND 254 256
FT HELIX 263 270
FT TURN 272 274
FT HELIX 275 280
FT HELIX 285 300
FT TURN 301 303
FT HELIX 306 308
FT STRAND 309 311
FT HELIX 313 315
FT HELIX 334 336
FT STRAND 342 344
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
//
