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Database: UniProt
Entry: P28314
LinkDB: P28314
Original site: P28314 
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   01-OCT-2014, entry version 103.
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.
CC       {ECO:0000305}.
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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; PRX2A_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; 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;
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                                {ECO:0000269|PubMed:8112469}.
FT   CARBOHYD    358    358       O-linked (Man...).
FT                                {ECO:0000269|PubMed:8112469}.
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                                {ECO:0000305}.
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
//
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