ID A0A1B7MSW7_9AGAM Unreviewed; 374 AA.
AC A0A1B7MSW7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=K503DRAFT_696509 {ECO:0000313|EMBL:OAX35696.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX35696.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX35696.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX35696.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|ARBA:ARBA00003917}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00035967};
CC -!- SUBUNIT: Forms a one-to-one complex with cytochrome c.
CC {ECO:0000256|ARBA:ARBA00038574}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00005997}.
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DR EMBL; KV448476; OAX35696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7MSW7; -.
DR STRING; 1314800.A0A1B7MSW7; -.
DR InParanoid; A0A1B7MSW7; -.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000092154; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:RHEA.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd00691; ascorbate_peroxidase; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR002207; Peroxidase_I.
DR InterPro; IPR019794; Peroxidases_AS.
DR PANTHER; PTHR31356:SF58; CYTOCHROME C PEROXIDASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051};
KW Reference proteome {ECO:0000313|Proteomes:UP000092154};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 166..374
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
SQ SEQUENCE 374 AA; 41361 MW; 652CAF924B6D73DC CRC64;
MSFAAFRAPL RRQLFSASFR RAELRTSSFR KYSTNPPPAA KSSTGLYVGL GAIAVGGGLA
YYLYASSSDT AKETSTALKS AAQSAKAATK LAPTKEDYQK VYNRIAEIID DADDYDYGSF
GPVVLRLAWH ASGTYDKATG TGGSNYATMR FEPEALHGAN AGLRVARDLM EKVKKEFDWI
SYGDLWTLAG VAAVQEMAGP KVPWRPGRID GFAAQATPDG RLPDASQGAP HIRDIFYRMG
FDDQEIVALC GAHALGRCHA DRSGFDGPWT FSPTTFSNDF YKLLFDEKWV WKKWGGPKQL
EDKKTKSLMM LPTDYVLTQD KSFKKYAKAY ADDADLFFKD FSAAFSKLLE LGVPTQQFVS
SEPWVMQTVD EQKS
//
