ID LIG6_PHACH Reviewed; 372 AA. AC P50622; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 05-OCT-2016, entry version 88. DE RecName: Full=Ligninase LG6; DE EC=1.11.1.14 {ECO:0000250|UniProtKB:P06181}; DE AltName: Full=Diarylpropane peroxidase; DE AltName: Full=Lignin peroxidase; DE Flags: Precursor; GN Name=GLG6; OS Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum OS pruinosum). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete. OX NCBI_TaxID=5306; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / RC VKM F-1767; RX PubMed=2268360; DOI=10.1016/S0006-291X(05)80884-8; RA Naidu P.S., Zhang Y.Z., Reddy C.A.; RT "Characterization of a new lignin peroxidase gene (GLG6) from RT Phanerochaete chrysosporium."; RL Biochem. Biophys. Res. Commun. 173:994-1000(1990). CC -!- FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)- CC C(beta) cleavage of the propyl side chains of lignin. CC {ECO:0000250|UniProtKB:P06181}. CC -!- CATALYTIC ACTIVITY: 1-(3,4-dimethoxyphenyl)-2-(2- CC methoxyphenoxy)propane-1,3-diol + H(2)O(2) = 3,4- CC dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H(2)O. CC {ECO:0000250|UniProtKB:P06181}. CC -!- CATALYTIC ACTIVITY: 2 (3,4-dimethoxyphenyl)methanol + H(2)O(2) = 2 CC (3,4-dimethoxyphenyl)methanol radical + 2 H(2)O. CC {ECO:0000250|UniProtKB:P06181}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per CC subunit. {ECO:0000255|PROSITE-ProRule:PRU00297}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00297}; CC -!- PATHWAY: Secondary metabolite metabolism; lignin degradation. 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; M80213; AAA33737.1; -; mRNA. DR ProteinModelPortal; P50622; -. DR CAZy; AA2; Auxiliary Activities 2. DR PeroxiBase; 2415; PcLiP06. DR eggNOG; ENOG410II1B; Eukaryota. DR eggNOG; ENOG410ZS1R; LUCA. DR BioCyc; MetaCyc:MONOMER-14342; -. DR UniPathway; UPA00892; -. DR GO; GO:0016690; F:diarylpropane peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. 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; 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 2: Evidence at transcript level; KW Calcium; Cleavage on pair of basic residues; Disulfide bond; KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation; KW Metal-binding; Oxidoreductase; Peroxidase; Signal; Zymogen. FT SIGNAL 1 21 {ECO:0000255}. FT PROPEP 22 28 {ECO:0000255}. FT /FTId=PRO_0000023770. FT CHAIN 29 372 Ligninase LG6. FT /FTId=PRO_0000023771. FT ACT_SITE 75 75 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00297, ECO:0000255|PROSITE- FT ProRule:PRU10012}. FT METAL 76 76 Calcium 1. {ECO:0000255|PROSITE- FT ProRule:PRU00297}. FT METAL 94 94 Calcium 1; via carbonyl oxygen. FT {ECO:0000255|PROSITE-ProRule:PRU00297}. FT METAL 96 96 Calcium 1. {ECO:0000255|PROSITE- FT ProRule:PRU00297}. FT METAL 98 98 Calcium 1. {ECO:0000255|PROSITE- FT ProRule:PRU00297}. FT METAL 204 204 Iron (heme axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00297}. FT METAL 205 205 Calcium 2. {ECO:0000255|PROSITE- FT ProRule:PRU00297}. FT METAL 222 222 Calcium 2. {ECO:0000255|PROSITE- FT ProRule:PRU00297}. FT METAL 224 224 Calcium 2. {ECO:0000255|PROSITE- FT ProRule:PRU00297}. FT METAL 227 227 Calcium 2; via carbonyl oxygen. FT {ECO:0000255|PROSITE-ProRule:PRU00297}. FT METAL 229 229 Calcium 2. {ECO:0000255|PROSITE- FT ProRule:PRU00297}. FT SITE 71 71 Transition state stabilizer. FT {ECO:0000255|PROSITE-ProRule:PRU00297}. FT CARBOHYD 285 285 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 31 43 {ECO:0000255|PROSITE-ProRule:PRU00297}. FT DISULFID 62 148 {ECO:0000255|PROSITE-ProRule:PRU00297}. FT DISULFID 277 345 {ECO:0000255|PROSITE-ProRule:PRU00297}. SQ SEQUENCE 372 AA; 39259 MW; B192A93351F8CC16 CRC64; MALKQLAAAV ALALSIQAAQ GAAVKEKRAT CSNGATVGDA SSCAWFDVLD DIQQNLFNGA QCGAEAHESI RLVFHDAIAI SPALESQGKF GGGGADGSII LFDDIETNFH PNIGLDEIVN LQKPFIQKHG VTPGDFIAFA GAVAMSNCPG APQMNFFTGR APATQAAPDG LVPEPFHTVD QIISRVNDAG EFDELELVWM LSAHSVAAAN DVDPTIQGLA FDSTPGVFDS QFFVETQLRG TAFPGSGGNQ GEVESPLPGE MRLQSDSSIA RDSRTACEWQ SFVNNQSKLV SDFQFIFLAL TQLGENPDAM TDCSDVIPIS KPVPNNVPFS FFPAGKTMAD VEQACAETPF PTLTTLPGPE TSVQRIQPPP GA //