ID PERX_TOBAC Reviewed; 324 AA. AC P11965; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 24-JUL-2007, entry version 65. DE Lignin-forming anionic peroxidase precursor (EC 1.11.1.7) (TOPA). OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=16593885; RA Lagrimini L.M., Burkhart W., Moyer M., Rothstein S.; RT "Molecular cloning of complementary DNA encoding the lignin-forming RT peroxidase from tobacco: molecular analysis and tissue-specific RT expression."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7542-7546(1987). CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, CC biosynthesis and degradation of lignin, suberization, auxin CC catabolism, response to environmental stresses such as wounding, CC pathogen attack and oxidative stress. These functions might be CC dependent on each isozyme/isoform in each plant tissue. CC -!- FUNCTION: Plays an integral role in secondary cell wall CC biosynthesis by the polymerization of cinnamyl alcohols into CC lignin and by forming rigid cross-links between cellulose, pectin, CC hydroxy-proline-rich glycoproteins, and lignin. CC -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized 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 (By similarity). CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant CC (class III) peroxidase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02979; AAA34108.1; -; mRNA. DR PIR; A39889; A39889. DR HSSP; Q42578; 1PA2. DR PeroxiBase; 1; NtPrx09. DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac. DR InterPro; IPR000823; Peroxidase_pln. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 2: Evidence at transcript level; KW Calcium; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; KW Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; KW Signal. FT SIGNAL 1 22 FT CHAIN 23 324 Lignin-forming anionic peroxidase. FT /FTId=PRO_0000023756. FT ACT_SITE 64 64 Proton acceptor (By similarity). FT METAL 65 65 Calcium 1 (By similarity). FT METAL 68 68 Calcium 1 (via carbonyl oxygen) (By FT similarity). FT METAL 70 70 Calcium 1 (via carbonyl oxygen) (By FT similarity). FT METAL 72 72 Calcium 1 (By similarity). FT METAL 74 74 Calcium 1 (By similarity). FT METAL 189 189 Iron (heme axial ligand) (By similarity). FT METAL 190 190 Calcium 2 (By similarity). FT METAL 242 242 Calcium 2 (By similarity). FT METAL 245 245 Calcium 2 (By similarity). FT METAL 250 250 Calcium 2 (By similarity). FT BINDING 159 159 Substrate; via carbonyl oxygen (By FT similarity). FT SITE 60 60 Transition state stabilizer (By FT similarity). FT MOD_RES 23 23 Pyrrolidone carboxylic acid (By FT similarity). FT CARBOHYD 35 35 N-linked (GlcNAc...) (Potential). FT CARBOHYD 150 150 N-linked (GlcNAc...) (Potential). FT CARBOHYD 207 207 N-linked (GlcNAc...) (Potential). FT DISULFID 33 111 By similarity. FT DISULFID 66 71 By similarity. FT DISULFID 117 320 By similarity. FT DISULFID 196 228 By similarity. SQ SEQUENCE 324 AA; 34674 MW; 0F1F03927F47A669 CRC64; MSFLRFVGAI LFLVAIFGAS NAQLSATFYD TTCPNVTSIV RGVMDQRQRT DARAGAKIIR LHFHDCFVNG CDGSILLDTD GTQTEKDAPA NVGAGGFDIV DDIKTALENV CPGVVSCADI LALASEIGVV LAKGPSWQVL FGRKDSLTAN RSGANSDIPS PFETLAVMIP QFTNKGMDLT DLVALSGAHT FGRARCGTFE QRLFNFNGSG NPDLTVDATF LQTLQGICPQ GGNNGNTFTN LDISTPNDFD NDYFTNLQSN QGLLQTDQEL FSTSGSATIA IVNRYAGSQT QFFDDFVSSM IKLGNISPLT GTNGQIRTDC KRVN // ID PER_COPCI Reviewed; 363 AA. AC P28314; P28315; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 13-NOV-2007, entry version 72. DE Peroxidase precursor (EC 1.11.1.7). GN Name=CIP1; OS Coprinus cinereus (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=IFO 8371; RX MEDLINE=93238741; PubMed=8477731; 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 PROTEIN SEQUENCE OF 161-185. RX MEDLINE=92247803; 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 [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND GLYCOSYLATION AT ASN-162 RP AND SER-358. RX MEDLINE=94156050; 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 [4] RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS). RX MEDLINE=22661670; 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 [5] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANT. RX MEDLINE=22661671; 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 [6] RP STRUCTURE BY NMR OF MUTANT ASN-265. RX MEDLINE=97074497; 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: Donor + H(2)O(2) = oxidized 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X69457; CAA49216.1; -; mRNA. 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 PeroxiBase; 2403; CcinCII01. DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac. DR InterPro; IPR001621; Ligninase. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00462; LIGNINASE. DR PRINTS; PR00458; PEROXIDASE. 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; Glycoprotein; Heme; KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; KW Pyrrolidone carboxylic acid; Secreted; 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 STRAND 36 38 FT HELIX 40 42 FT HELIX 43 54 FT TURN 55 60 FT HELIX 64 77 FT HELIX 82 86 FT STRAND 94 97 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 230 234 FT STRAND 244 246 FT STRAND 254 256 FT HELIX 263 270 FT TURN 272 274 FT HELIX 275 280 FT HELIX 285 299 FT TURN 300 303 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 // ID LIG2_PHACH Reviewed; 371 AA. AC P49012; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-NOV-2007, entry version 67. DE Ligninase LG2 precursor (EC 1.11.1.14) (Diarylpropane peroxidase) DE (Lignin peroxidase). GN Name=GLG2; Synonyms=LIP2; OS Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum OS pruinosum). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Corticiales; Corticiaceae; Phanerochaete. OX NCBI_TaxID=5306; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-48. RC STRAIN=ATCC 201542 / OGC101; RX MEDLINE=92077421; PubMed=1743510; DOI=10.1016/0378-1119(91)90304-T; RA Ritch T.G. Jr., Nipper V.J., Akileswaran L., Smith A.J., Pribnow D.G., RA Gold M.H.; RT "Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium RT is synthesized as a preproenzyme."; RL Gene 107:119-126(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 201542 / OGC101; RX MEDLINE=92380494; PubMed=1511887; DOI=10.1016/0378-1119(92)90250-S; RA Ritch T.G. Jr., Gold M.H.; RT "Characterization of a highly expressed lignin peroxidase-encoding RT gene from the basidiomycete Phanerochaete chrysosporium."; RL Gene 118:73-80(1992). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=93179455; PubMed=8440725; RA Poulos T.L., Edwards S.L., Wariishi H., Gold M.H.; RT "Crystallographic refinement of lignin peroxidase at 2 A."; RL J. Biol. Chem. 268:4429-4440(1993). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND HYDROXYLATION AT TRP-199. RC STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; RX MEDLINE=99150427; PubMed=10024453; DOI=10.1006/jmbi.1998.2507; RA Choinowski T., Blodig W., Winterhalter K.H., Piontek K.; RT "The crystal structure of lignin peroxidase at 1.70-A resolution RT reveals a hydroxy group on the cbeta of tryptophan 171: a novel RT radical site formed during the redox cycle."; RL J. Mol. Biol. 286:809-827(1999). CC -!- FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)- CC C(beta) cleavage of the propyl side chains of lignin. CC -!- CATALYTIC ACTIVITY: 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + CC H(2)O(2) = 3,4-dimethoxybenzaldehyde + 1-(3,4- CC dimethoxyphenyl)ethane-1,2-diol + 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 -!- PATHWAY: Lignin degradation; first step. CC -!- DEVELOPMENTAL STAGE: Ligninases are expressed during secondary CC metabolism, and are triggered by nutrient limitation. CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M74229; AAA33735.1; -; mRNA. DR EMBL; M92644; AAA33738.1; -; Genomic_DNA. DR PIR; JC1268; JC1268. DR PDB; 1LGA; X-ray; 2.03 A; A/B=29-371. DR PDB; 1LLP; X-ray; 1.70 A; A=29-371. DR PeroxiBase; 2409; PcLiPE_OGC101. DR LinkHub; P49012; -. DR GO; GO:0016690; F:diarylpropane peroxidase activity; IEA:EC. DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac. DR InterPro; IPR001621; Ligninase. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00462; LIGNINASE. DR PRINTS; PR00458; PEROXIDASE. 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; Cleavage on pair of basic residues; KW Direct protein sequencing; Glycoprotein; Heme; Hydroxylation; Iron; KW Lignin degradation; Metal-binding; Oxidoreductase; Peroxidase; Signal; KW Zymogen. FT SIGNAL 1 21 FT PROPEP 22 28 FT /FTId=PRO_0000023762. FT CHAIN 29 371 Ligninase LG2. FT /FTId=PRO_0000023763. 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 204 204 Iron (heme axial ligand). FT METAL 205 205 Calcium 2. FT METAL 222 222 Calcium 2. FT METAL 224 224 Calcium 2. FT METAL 227 227 Calcium 2 (via carbonyl oxygen). FT METAL 229 229 Calcium 2. FT SITE 71 71 Transition state stabilizer. FT MOD_RES 199 199 3-hydroxytryptophan. FT CARBOHYD 285 285 N-linked (GlcNAc...) (Potential). FT DISULFID 31 43 FT DISULFID 42 313 FT DISULFID 62 148 FT DISULFID 277 345 FT HELIX 40 43 FT HELIX 44 55 FT TURN 58 60 FT HELIX 64 77 FT HELIX 82 85 FT STRAND 87 89 FT STRAND 94 97 FT HELIX 98 101 FT HELIX 103 106 FT HELIX 110 112 FT HELIX 115 129 FT HELIX 133 146 FT HELIX 179 190 FT HELIX 194 200 FT HELIX 201 206 FT STRAND 208 213 FT STRAND 219 223 FT HELIX 231 235 FT STRAND 255 258 FT HELIX 264 269 FT TURN 273 275 FT HELIX 276 281 FT TURN 282 284 FT HELIX 286 301 FT TURN 302 304 FT HELIX 307 309 FT STRAND 310 312 FT HELIX 314 316 FT STRAND 325 327 FT HELIX 338 340 FT STRAND 346 348 FT STRAND 357 359 SQ SEQUENCE 371 AA; 39329 MW; F6AAB123EDC92123 CRC64; MAFKQLFAAI TVALSLTAAN AAVVKEKRAT CANGKTVGDA SCCAWFDVLD DIQANMFHGG QCGAEAHESI RLVFHDSIAI SPAMEAKGKF GGGGADGSIM IFDTIETAFH PNIGLDEVVA MQKPFVQKHG VTPGDFIAFA GAVALSNCPG APQMNFFTGR KPATQPAPDG LVPEPFHTVD QIIARVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG TLFPGSGGNQ GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVGNQSKLV DDFQFIFLAL TQLGQDPNAM TDCSDVIPLS KPIPGNGPFS FFPPGKSHSD IEQACAETPF PSLVTLPGPA TSVARIPPHK A // ID LIG3_PHACH Reviewed; 372 AA. AC P21764; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 24-JUL-2007, entry version 63. DE Ligninase LG3 precursor (EC 1.11.1.14) (Diarylpropane peroxidase) DE (Lignin peroxidase). GN Name=GLG3; Synonyms=LIP; OS Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum OS pruinosum). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Corticiales; Corticiaceae; Phanerochaete. OX NCBI_TaxID=5306; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; RX MEDLINE=91088334; PubMed=2129560; DOI=10.1093/nar/18.23.7173; RA Naidu P.S., Reddy C.A.; RT "Nucleotide sequence of a new lignin peroxidase gene GLG3 from the RT white-rot fungus, Phanerochaete chrysosporium."; RL Nucleic Acids Res. 18:7173-7173(1990). CC -!- FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)- CC C(beta) cleavage of the propyl side chains of lignin. CC -!- CATALYTIC ACTIVITY: 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + CC H(2)O(2) = 3,4-dimethoxybenzaldehyde + 1-(3,4- CC dimethoxyphenyl)ethane-1,2-diol + H(2)O. CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per CC subunit (By similarity). CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- PATHWAY: Lignin degradation; first step. CC -!- DEVELOPMENTAL STAGE: Ligninases are expressed during secondary CC metabolism, and are triggered by nutrient limitation. CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X51590; CAA35939.1; -; Genomic_DNA. DR PIR; A32322; A32322. DR PIR; B32322; B32322. DR PIR; PS0010; PS0010. DR PIR; S13723; OPJG3P. DR PIR; S69246; S69246. DR HSSP; P06181; 1B80. DR SMR; P21764; 24-372. DR PeroxiBase; 2482; PcLiPI. DR GO; GO:0016690; F:diarylpropane peroxidase activity; IEA:EC. DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac. DR InterPro; IPR001621; Ligninase. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00462; LIGNINASE. DR PRINTS; PR00458; PEROXIDASE. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 2: Evidence at transcript level; KW Cleavage on pair of basic residues; Glycoprotein; Heme; KW Hydrogen peroxide; Iron; Lignin degradation; Metal-binding; KW Oxidoreductase; Peroxidase; Signal; Zymogen. FT SIGNAL 1 21 Potential. FT PROPEP 22 28 FT /FTId=PRO_0000023764. FT CHAIN 29 372 Ligninase LG3. FT /FTId=PRO_0000023765. FT ACT_SITE 75 75 Proton acceptor (By similarity). FT METAL 76 76 Calcium 1 (By similarity). FT METAL 94 94 Calcium 1 (via carbonyl oxygen) (By FT similarity). FT METAL 96 96 Calcium 1 (By similarity). FT METAL 98 98 Calcium 1 (By similarity). FT METAL 204 204 Iron (heme axial ligand) (By similarity). FT METAL 205 205 Calcium 2 (By similarity). FT METAL 222 222 Calcium 2 (By similarity). FT METAL 224 224 Calcium 2 (By similarity). FT METAL 227 227 Calcium 2 (via carbonyl oxygen) (By FT similarity). FT METAL 229 229 Calcium 2 (By similarity). FT SITE 71 71 Transition state stabilizer (By FT similarity). FT CARBOHYD 285 285 N-linked (GlcNAc...) (Potential). FT DISULFID 31 43 By similarity. FT DISULFID 62 148 By similarity. FT DISULFID 277 345 By similarity. SQ SEQUENCE 372 AA; 39536 MW; DA0293178F4E2A4A CRC64; MAFKQLFAAI SLALSLSAAN AAAVIEKRAT CSNGKTVGDA SSCAWFDVLD DIQQNLFHGG QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM IFDDIETAFH PNIGLDEIVK LQKPFVQKHG CTPGDFIAFA GAVALSNCPG APQMNFFTGR APATQAAPDG LVPEPFHTVD QIINRVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQLRG TAFPGSGGNQ GEVESPLPGE IRIQSDHTIA RDSRTACEWQ SFVNNQSKLV DDFQFIFLAL TQLGQDPNAM TDCSDVIPQS KPIPGNLPFS FFPAGKTIKD VEQACAETPF PTLTTLPGPE TSVQRIPPPP GA //