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LIGB_PHACH
ID   LIGB_PHACH              Reviewed;         372 AA.
AC   P31838;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ligninase B;
DE            EC=1.11.1.14 {ECO:0000269|PubMed:3240864};
DE   AltName: Full=Diarylpropane peroxidase;
DE   AltName: Full=Lignin peroxidase;
DE   Flags: Precursor;
GN   Name=LIPB;
OS   Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerodontia.
OX   NCBI_TaxID=2822231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC   F-1767;
RX   PubMed=2011531; DOI=10.1093/nar/19.3.599;
RA   Gaskell J., Dieperink E., Cullen D.;
RT   "Genomic organization of lignin peroxidase genes of Phanerochaete
RT   chrysosporium.";
RL   Nucleic Acids Res. 19:599-603(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 29-58, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=3240864; DOI=10.1016/0378-1119(88)90111-4;
RA   Walther L., Kaelin M., Reiser J., Suter F., Fritsche B., Saloheimo M.,
RA   Leisola M., Teeri T., Knowles J.K.C., Fiechter A.;
RT   "Molecular analysis of a Phanerochaete chrysosporium lignin peroxidase
RT   gene.";
RL   Gene 70:127-137(1988).
CC   -!- FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta)
CC       cleavage of the propyl side chains of lignin.
CC       {ECO:0000269|PubMed:3240864}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol +
CC         H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O;
CC         Xref=Rhea:RHEA:48004, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17071, ChEBI:CHEBI:17098, ChEBI:CHEBI:28591,
CC         ChEBI:CHEBI:86963; EC=1.11.1.14;
CC         Evidence={ECO:0000269|PubMed:3240864};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-
CC         dimethoxyphenyl)methanol radical + 2 H2O; Xref=Rhea:RHEA:30271,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:62150,
CC         ChEBI:CHEBI:88143; EC=1.11.1.14;
CC         Evidence={ECO:0000269|PubMed:3240864};
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 subunit.
CC       {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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=85 uM for H(2)O(2) {ECO:0000269|PubMed:3240864};
CC         KM=83 uM for (3,4-dimethoxyphenyl)methanol
CC         {ECO:0000269|PubMed:3240864};
CC       pH dependence:
CC         Optimum pH is 2.3. {ECO:0000269|PubMed:3240864};
CC   -!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X54257; CAA38178.1; -; Genomic_DNA.
DR   PIR; A32322; A32322.
DR   PIR; B32322; B32322.
DR   PIR; PS0010; PS0010.
DR   PIR; S13564; OPJGBP.
DR   PIR; S69246; S69246.
DR   AlphaFoldDB; P31838; -.
DR   SMR; P31838; -.
DR   CAZy; AA2; Auxiliary Activities 2.
DR   VEuPathDB; FungiDB:AGR57_14163; -.
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:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway.
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   Calcium; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW   Lignin degradation; Metal-binding; Oxidoreductase; Peroxidase; Signal;
KW   Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..28
FT                   /evidence="ECO:0000269|PubMed:3240864"
FT                   /id="PRO_0000023774"
FT   CHAIN           29..372
FT                   /note="Ligninase B"
FT                   /id="PRO_0000023775"
FT   REGION          350..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        75
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT                   ECO:0000255|PROSITE-ProRule:PRU10012"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         98
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         204
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         222
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         224
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         229
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   SITE            71
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   DISULFID        42..313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   DISULFID        62..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   DISULFID        277..345
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ   SEQUENCE   372 AA;  39530 MW;  E0DD2CF40425D9D5 CRC64;
     MAFKQLFAAI SLALSLSAAN AAAVIEKRAT CSNGKTVGDA SCCAWFDVLD DIQQNLFHGG
     QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM IFDDIETAFH PNIGLDEIVK
     LQKPFVQKHG VTPGAFIAFA GAVALSNCPG APQMNFFTGR APATQPAPDG LVPEPFHTVD
     QIINRVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQLRG
     TAFPGSGGNQ GEVESPLPGE IRIQSDHTIA RDSRTACEWQ SFVNNQSKLV DDFQFIFLAL
     TQLGQDPNAM TDCSDVIPQS KPIPGNLPFS FFPAGKTIKD VEQACAETPF PTLTTLPGPE
     TSVQRIPPPP GA
 
 
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