ID A0A067CNC1_SAPPC Unreviewed; 329 AA.
AC A0A067CNC1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cytochrome c peroxidase, mitochondrial {ECO:0000256|ARBA:ARBA00040313};
DE EC=1.11.1.5 {ECO:0000256|ARBA:ARBA00039063};
GN ORFNames=SPRG_03385 {ECO:0000313|EMBL:KDO32169.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO32169.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO32169.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO32169.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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.
CC {ECO:0000256|RuleBase:RU004241}.
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DR EMBL; KK583196; KDO32169.1; -; Genomic_DNA.
DR RefSeq; XP_012197352.1; XM_012341962.1.
DR AlphaFoldDB; A0A067CNC1; -.
DR STRING; 695850.A0A067CNC1; -.
DR EnsemblProtists; KDO32169; KDO32169; SPRG_03385.
DR GeneID; 24125898; -.
DR KEGG; spar:SPRG_03385; -.
DR VEuPathDB; FungiDB:SPRG_03385; -.
DR OMA; GAWVNNP; -.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
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 Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 68..320
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 95..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 36400 MW; 7FBEFB3FD009707E CRC64;
MFRTAASRAT RVAARAGAPR LLARSMSVAA RQSSTSKATA MAGAFLVTTG VTASLLQAQE
AKVNLEKIRK EIVDLIDDEP AMGPTFVRLA WHSSGSYSKH DHSGGSKGGT IRNEPEISHG
GNAGLNLAIA RLESVKARHP EISYADLFIY SGVVAIAEMG GPEVPFHLGR KDAKVGEQVT
PDDRLPNADM GSKPSTISHI RDVFTAWAST TARSLRSSAP TRGYSGPWTR AETTFSNEYF
RELIENKWTI KKWKGPEQYE DPTGDLMMLP ADMAFLWDPE FKKYVELYAK DEDLWHKDFA
KAFQKLTENG CDFAKSGWRR YIFFGPRSD
//
