VPS1_PLEER
ID VPS1_PLEER Reviewed; 370 AA.
AC Q9UVP6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Versatile peroxidase VPS1;
DE EC=1.11.1.16 {ECO:0000269|PubMed:10187820};
DE AltName: Full=Versatile solid phase peroxidase 1;
DE Flags: Precursor;
GN Name=vps1; Synonyms=ps1;
OS Pleurotus eryngii (Boletus of the steppes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 32-51.
RC STRAIN=ATCC 90787 / CBS 613.91 / IJFM A169 / KCTC 26061; TISSUE=Mycelium;
RX PubMed=11004397; DOI=10.1111/j.1574-6968.2000.tb09316.x;
RA Camarero S., Ruiz-Duenas F.J., Sarkar S., Martinez M.J., Martinez A.T.;
RT "The cloning of a new peroxidase found in lignocellulose cultures of
RT Pleurotus eryngii and sequence comparison with other fungal peroxidases.";
RL FEMS Microbiol. Lett. 191:37-43(2000).
RN [2]
RP PROTEIN SEQUENCE OF 32-40, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND 3D-STRUCTURE MODELING OF
RP 32-370.
RC STRAIN=ATCC 90787 / CBS 613.91 / IJFM A169 / KCTC 26061; TISSUE=Mycelium;
RX PubMed=10187820; DOI=10.1074/jbc.274.15.10324;
RA Camarero S., Sarkar S., Ruiz-Duenas F.J., Martinez M.J., Martinez A.T.;
RT "Description of a versatile peroxidase involved in the natural degradation
RT of lignin that has both manganese peroxidase and lignin peroxidase
RT substrate interaction sites.";
RL J. Biol. Chem. 274:10324-10330(1999).
CC -!- FUNCTION: A versatile ligninolytic peroxidase that combines the
CC substrate specificity characteristics of the two other ligninolytic
CC peroxidases, manganese peroxidase and lignin peroxidase.
CC {ECO:0000269|PubMed:10187820}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-
CC diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin;
CC Xref=Rhea:RHEA:22396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:18346, ChEBI:CHEBI:28591,
CC ChEBI:CHEBI:53650; EC=1.11.1.16;
CC Evidence={ECO:0000269|PubMed:10187820};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+);
CC Xref=Rhea:RHEA:22776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29035, ChEBI:CHEBI:29041;
CC EC=1.11.1.16; Evidence={ECO:0000269|PubMed:10187820};
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=48 uM for manganese {ECO:0000269|PubMed:10187820};
CC KM=9 uM for H(2)O(2) (in manganese oxidation)
CC {ECO:0000269|PubMed:10187820};
CC KM=2 uM for H(2)O(2) (in manganese-independent oxidations)
CC {ECO:0000269|PubMed:10187820};
CC KM=17 uM for methoxyhydroquinone {ECO:0000269|PubMed:10187820};
CC KM=200 uM for syringol {ECO:0000269|PubMed:10187820};
CC KM=3500 uM for veratryl alcohol {ECO:0000269|PubMed:10187820};
CC KM=2 uM for reactive black 5 {ECO:0000269|PubMed:10187820};
CC pH dependence:
CC Optimum pH is 5 for manganese oxidation reaction, and around 3 for
CC all the manganese-independent reactions.
CC {ECO:0000269|PubMed:10187820};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; AF175710; AAD54310.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UVP6; -.
DR SMR; Q9UVP6; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; VPO2C_PLEER; -.
DR PeroxiBase; 2302; PerVP02.
DR KEGG; ag:AAD54310; -.
DR BRENDA; 1.11.1.16; 4910.
DR SABIO-RK; Q9UVP6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016689; F:manganese peroxidase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052750; F:reactive-black-5:hydrogen-peroxide oxidoreductase activity; IEA:UniProtKB-EC.
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-KW.
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; Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Lignin degradation; Manganese; Metal-binding;
KW Organic radical; Oxidoreductase; Peroxidase; Secreted; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..31
FT /evidence="ECO:0000269|PubMed:10187820,
FT ECO:0000269|PubMed:11004397"
FT /id="PRO_0000308169"
FT CHAIN 32..370
FT /note="Versatile peroxidase VPS1"
FT /id="PRO_5000056981"
FT ACT_SITE 78
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT ACT_SITE 201
FT /note="Tryptophan radical intermediate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 206
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 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 210..214
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
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 226
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 BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 74
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 45..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 65..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 279..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 370 AA; 39046 MW; 86DA6F99C79D08B9 CRC64;
MAFAKLSAFV LALGATVALG ESPTHRCLNK RVTCATGQTT ANEACCALFP ILDDIQTNLF
DGAQCGEEVH ESLRLTFHDA IAFSPALTNA GQFGGGGADG SMIIFSDTEP NFHANLGIDE
IVEAQKPFIA RHNISAADFI QFAGAIGVSN CAGAPRLNFF LGRPDATQIP PDGLVPEPFD
DVTKILSRMG DAGFSTVEVV WLLASHTIAA ADHVDPSIPG TPFDSTPSTF DSQFFLETML
QGTAFPGTPG NQGEVESPLA GEMRLQSDFL LARDSRSACE WQSMVNNMPK IQNRFTQVMK
KLSLLGHNQA DLIDCSDVIP VPKTLTKAAT FPAGKSQADV EIVCNAAATP FPALASDPGP
VTAVPPVPPS
