MSP1_MYCSO
ID MSP1_MYCSO Reviewed; 513 AA.
AC B0BK71;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Dye-decolorizing peroxidase msp1;
DE EC=1.11.1.19 {ECO:0000269|PubMed:23111597};
DE EC=1.11.1.7 {ECO:0000269|PubMed:23111597};
DE AltName: Full=Peroxidase 1 {ECO:0000303|PubMed:18038130};
DE Short=MsP1 {ECO:0000303|PubMed:18038130};
DE Flags: Precursor;
GN Name=msp1 {ECO:0000312|EMBL:CAP53934.1};
OS Mycetinis scorodonius (Garlic mushroom) (Marasmius scorodonius).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Omphalotaceae; Mycetinis.
OX NCBI_TaxID=182058;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAP53934.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 56-83; 390-402;
RP 460-470 AND 495-508, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MASS SPECTROMETRY.
RC STRAIN=CBS 137.86 {ECO:0000269|PubMed:18038130};
RX PubMed=18038130; DOI=10.1007/s00253-007-1261-9;
RA Scheibner M., Huelsdau B., Zelena K., Nimtz M., de Boer L., Berger R.G.,
RA Zorn H.;
RT "Novel peroxidases of Marasmius scorodonius degrade beta-carotene.";
RL Appl. Microbiol. Biotechnol. 77:1241-1250(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23111597; DOI=10.1007/s00253-012-4521-2;
RA Liers C., Pecyna M.J., Kellner H., Worrich A., Zorn H., Steffen K.T.,
RA Hofrichter M., Ullrich R.;
RT "Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and
RT litter-degrading agaricomycetes compared to other fungal and plant heme-
RT peroxidases.";
RL Appl. Microbiol. Biotechnol. 97:5839-5849(2013).
CC -!- FUNCTION: Manganese-independent peroxidase that is able to convert a
CC large number of compounds, but its physiological substrate is not known
CC (PubMed:23111597). In addition to classic peroxidase substrates (e.g.
CC 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5
CC (PubMed:23111597). Also degrades beta-carotene (PubMed:18038130).
CC {ECO:0000269|PubMed:18038130, ECO:0000269|PubMed:23111597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-
CC amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2
CC H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563,
CC ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278;
CC EC=1.11.1.19; Evidence={ECO:0000269|PubMed:23111597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC Evidence={ECO:0000269|PubMed:23111597};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P31545, ECO:0000269|PubMed:18038130};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per monomer. {ECO:0000250|UniProtKB:P31545,
CC ECO:0000269|PubMed:18038130};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=406 nm {ECO:0000269|PubMed:23111597};
CC Kinetic parameters:
CC KM=5 uM for H(2)O(2) {ECO:0000269|PubMed:23111597};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18038130}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18038130}.
CC -!- MASS SPECTROMETRY: Mass=64200; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18038130};
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000255}.
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DR EMBL; AM921678; CAP53934.1; -; Genomic_DNA.
DR AlphaFoldDB; B0BK71; -.
DR SMR; B0BK71; -.
DR PeroxiBase; 6675; MscDyPrx01.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0016121; P:carotene catabolic process; IDA:UniProtKB.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR006314; Dyp_peroxidase.
DR Pfam; PF04261; Dyp_perox; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR PROSITE; PS51404; DYP_PEROXIDASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..55
FT /evidence="ECO:0000255, ECO:0000269|PubMed:18038130"
FT /id="PRO_0000386441"
FT CHAIN 56..513
FT /note="Dye-decolorizing peroxidase msp1"
FT /id="PRO_0000386442"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:I2DBY1"
FT BINDING 365
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:I2DBY1"
FT CONFLICT 74
FT /note="G -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 54972 MW; D927B31021AD235E CRC64;
MKLFSASVFA AIIASHYASA TAHIRAPNVK PRRTNSLLTA PPQQPPLPSA QQAASASSSA
GLNLTDIQGD ILIGMKKNKE LFFFFSITDA ATFKAKLGSD ILELITSTNQ LLAVATQPIT
AVNVAFSSTG LKALGITDDL KDPVFEAGML SNAVSDLSDP GTGNWVPGFV GTSVHGVFLL
ASDTIDNVNT ELANIQTILN GSITEIHRLQ GEARPGDQQG HEHFGFMDGI SNPAVDGFTP
PAEIRPGQAL IPPGIMLLGE ANDTFQNDRP PWAKDGSFLV FRQMQQRAPE FNKFLQDHAL
NMPNMTSEQG ADLLGARIVG RWKSDAPIDL TPLVDDPVLA ADNQRNNNFD FSDATNQTRC
PFSAHIRKAN PRGDLGGINK FPNQHIIRAG IPYGPEVTDA EKASNSSSTD PSLERGLAFV
AYQSNIQNGF VFLQKNWVDN TNFFRPGTGV DPLIGTNSRN SGTDAPNTPR VVSGLDPNNA
TSTIEIGIDF VVSRGGEYFF SPSLSAIRTV LSV
