ID   PPOX_MACFA              Reviewed;         477 AA.
AC   Q60HD5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Protoporphyrinogen oxidase;
DE            Short=PPO;
DE            EC=1.3.3.4;
GN   Name=PPOX; ORFNames=QccE-13968;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC       to form protoporphyrin-IX. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX;
CC         Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC   -!- SUBUNIT: Monomer. Homodimer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC       {ECO:0000250}. Note=Bound to the mitochondrial inner membrane with its
CC       active site facing the cytosolic side. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC       oxidase family. Protoporphyrinogen oxidase subfamily. {ECO:0000305}.
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DR   EMBL; AB125192; BAD51980.1; -; mRNA.
DR   AlphaFoldDB; Q60HD5; -.
DR   SMR; Q60HD5; -.
DR   STRING; 9541.XP_005541261.1; -.
DR   eggNOG; KOG1276; Eukaryota.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; ISS:UniProtKB.
DR   GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Heme biosynthesis; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..477
FT                   /note="Protoporphyrinogen oxidase"
FT                   /id="PRO_0000135271"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..60
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         449
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         454..456
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  50613 MW;  5665D8871470AEA5 CRC64;
     MGRTVVVLGG GISGLAASYH LSRAPCPPKV VLVEGSERLG GWIRSVRGPN GAIFELGPRG
     IRPAGALGAR TLLLVSELGL DSEVLPVRGD HPAAQNRFLY VGGALHALPT GLRGLLRPSP
     PFSKPLFWAG LRELTKPRGK EPDETVHSFA QRRLGPEVAS LAMDSLCRGV FAGNSRELSI
     RSCFPSLFQA EQTHRSVLLG LLLGAGRTPQ PDSALIRQAL AERWSQWSLR GGLEMLPQAL
     ETHLTSRGVS VLRGQPVCGL SLQAEGRWKV SLRDSSLEAD HVISAIPASV LSELLPAEAA
     PLARALSAIT AVSVAVVNLQ YQGAHLPVQG FGHLVPSSED PGVLGIVYDS VAFPEQDGSP
     PGLRVTVMLG GSWLQTLEAS GCVLSQELFQ QRAQEAAAAQ LGLKELPSHC LVHLHKNCIP
     QYTLGHWQKL ESARQFLAAH RLPLTLAGAS YEGVAVNDCI ESGRQAAVSV LGTEPNG