ID A0A316UNH3_9BASI Unreviewed; 343 AA.
AC A0A316UNH3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=BDZ90DRAFT_233126 {ECO:0000313|EMBL:PWN26494.1};
OS Jaminaea rosea.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Jaminaea.
OX NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN26494.1, ECO:0000313|Proteomes:UP000245884};
RN [1] {ECO:0000313|EMBL:PWN26494.1, ECO:0000313|Proteomes:UP000245884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN26494.1,
RC ECO:0000313|Proteomes:UP000245884};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819671; PWN26494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UNH3; -.
DR STRING; 1569628.A0A316UNH3; -.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000245884; Unassembled WGS sequence.
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 InterPro; IPR019793; Peroxidases_heam-ligand_BS.
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; PS00435; PEROXIDASE_1; 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:UP000245884};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 64..343
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 166..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 37884 MW; 33920065E526DAE4 CRC64;
MLGWSVVGIV AATGAFLYLG REDKKSALGV GESEGISKTK GAKHKAGAAS ASDLSAGTKA
DYQKVYNAIA DRLEQEGYDD GSYGPVLVRL AWHSSGTYCK DTKTGGSNGA TMRFAPESDH
GANAGLKAAR DFLEPVKAMF PWVTYSDLWT LAGVVAVQEM GGPQIAWRPG RSDREQEHCA
PDGRLPDGDK EQDHLRFIFY RMGFNDQEIV ALSGAHALGR CHTDRSGFEG PWTHSPISFT
NQYYDLLLNE KWNWKKWNGP KQYIDKNTGG LMMLTTDMAL IKDKSFRPWV EKYAKDEEAF
FADFSNVFAK LLELGVPEEN FKAAEADHSG KPYKLKSTAD QEN
//
