ID   MSP2_MYCSO              Reviewed;         510 AA.
AC   B0BK72;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Peroxidase 2 {ECO:0000303|PubMed:18038130};
DE            Short=MsP2 {ECO:0000303|PubMed:18038130};
DE            EC=1.11.1.-;
DE   Flags: Precursor;
GN   Name=msp2 {ECO:0000312|EMBL:CAP53935.1};
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:CAP53935.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 59-83; 272-279;
RP   291-309; 316-337 AND 481-491, FUNCTION, COFACTOR, SUBUNIT, AND MASS
RP   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).
CC   -!- FUNCTION: Peroxidase capable of degrading beta-carotene.
CC       {ECO:0000269|PubMed:18038130}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255, ECO:0000269|PubMed:18038130};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC       per monomer. {ECO:0000255, ECO:0000269|PubMed:18038130};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18038130}.
CC   -!- MASS SPECTROMETRY: Mass=52400; 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; AM921679; CAP53935.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0BK72; -.
DR   SMR; B0BK72; -.
DR   PeroxiBase; 6674; MscDyPrx02.
DR   PRIDE; B0BK72; -.
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; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..58
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:18038130"
FT                   /id="PRO_0000386439"
FT   CHAIN           59..510
FT                   /note="Peroxidase 2"
FT                   /evidence="ECO:0000269|PubMed:18038130"
FT                   /id="PRO_0000386440"
FT   ACT_SITE        228
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        59
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="L -> F (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481..482
FT                   /note="VT -> LV (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        489
FT                   /note="V -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  54205 MW;  ED00BFFC3CA1DBB9 CRC64;
     MRLTYLPLFA GIAIQSASAL PDFFKSSVLK PRRTNSLLIN PDAQPDLPTA QQASTAAASV
     GLNLTDIQGD ILIGMKKNKE MFFFFSIADA TAFKSHLDSA ILPLITSTQQ LLTVATQPTT
     AVNLAFSQTG LNALGLASQG LGDSLFASGQ FSGAESLGDP GTSNWVQAFA GTGIHGVFLL
     ASDTIDNVNA ELSQIQSILG TSITEAYRLQ GEARPDDQQG HEHFGFMDGI SNPAIDGFST
     ALPGQAVLSP GLFLLAEDGD GSSSSRPSWA KDGSLLAFRQ LQQRVPEFNK FLADNAALTQ
     GNADLLGARM MGRWKSGAPV DLAPTADDVD LANDPQRNNN FNFTHPDFTE TTDQTHCPFS
     AHIRKTNPRS DFNPLNTANH IIRAGIPYGP EVTDAEASSN TSSTDASLER GLAFVAYQSN
     IGNGFAFIQQ NWVDNANFFF GKTTPPGIDP IIGSNAAQNN FAPNSPRPVS GLDPTDSTTI
     VTLNTDFVVS RGGEYFFSPS LSAIQNTLSV