ID A0A1X0RZH9_RHIZD Unreviewed; 373 AA.
AC A0A1X0RZH9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=BCV71DRAFT_227526 {ECO:0000313|EMBL:ORE17446.1};
OS Rhizopus microsporus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=58291 {ECO:0000313|EMBL:ORE17446.1, ECO:0000313|Proteomes:UP000242381};
RN [1] {ECO:0000313|EMBL:ORE17446.1, ECO:0000313|Proteomes:UP000242381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11559 {ECO:0000313|EMBL:ORE17446.1,
RC ECO:0000313|Proteomes:UP000242381};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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; KV921355; ORE17446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0RZH9; -.
DR VEuPathDB; FungiDB:BCV72DRAFT_259688; -.
DR OMA; QRKWNGP; -.
DR Proteomes; UP000242381; 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:UP000242381};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 168..373
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
SQ SEQUENCE 373 AA; 41445 MW; 5F3137740F293F2F CRC64;
MNSISSSLLK NISSRTASRP IVTSTSALSA NVRHAGAVRA SLMHQRGYTS SATPKKGSSG
RLAFLTLATL GGIGGYYYTS AQAIKTKTIP VTTTKKDIDY EKIYKEIAEM LDENPDYDDG
SYGPVLVRLA WHASGTYDKE TKTGGSNGAT MRFEPESAHA ANNGLAIARD LLEKIHQKYP
EISYGDLWTL AGVCAIQELG GPTIPWRPGR QDAFEAKSCT PDGRLPDATK KEDHIRDVFY
RMGFNDQEIV ALTGAHALGR CHPERSGFDG PWQEAPTIFS NEYFKAISGR KWIKKTLPHG
GWQWVDENNT DVMMLPAEIS MYNDKEFKKY FDLYAKDEQK FFEDFAAAFV KLLELGVPFK
GDEKVYRFKA TTA
//
