ID   PPOX_DICDI              Reviewed;         532 AA.
AC   Q54DT8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   RecName: Full=Protoporphyrinogen oxidase;
DE            Short=PPO;
DE            EC=1.3.3.4;
GN   Name=ppox; Synonyms=hemG; ORFNames=DDB_G0292040;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC       oxidase family. Protoporphyrinogen oxidase subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000187; EAL61376.1; -; Genomic_DNA.
DR   RefSeq; XP_629784.1; XM_629782.1.
DR   AlphaFoldDB; Q54DT8; -.
DR   SMR; Q54DT8; -.
DR   STRING; 44689.Q54DT8; -.
DR   PaxDb; 44689-DDB0231419; -.
DR   EnsemblProtists; EAL61376; EAL61376; DDB_G0292040.
DR   GeneID; 8628461; -.
DR   KEGG; ddi:DDB_G0292040; -.
DR   dictyBase; DDB_G0292040; hemG.
DR   eggNOG; KOG1276; Eukaryota.
DR   HOGENOM; CLU_009629_1_0_1; -.
DR   InParanoid; Q54DT8; -.
DR   OMA; EHNQAVQ; -.
DR   PhylomeDB; Q54DT8; -.
DR   Reactome; R-DDI-189451; Heme biosynthesis.
DR   UniPathway; UPA00251; UER00324.
DR   PRO; PR:Q54DT8; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; ISS:dictyBase.
DR   GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR   GO; GO:0006783; P:heme biosynthetic process; ISS:dictyBase.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR   NCBIfam; TIGR00562; proto_IX_ox; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Heme biosynthesis; Mitochondrion; Oxidoreductase;
KW   Porphyrin biosynthesis; Reference proteome.
FT   CHAIN           1..532
FT                   /note="Protoporphyrinogen oxidase"
FT                   /id="PRO_0000327793"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         42..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..73
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         511..513
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   532 AA;  59681 MW;  EBB0066495A696A7 CRC64;
     MIQKVGIIGS GISGLSSYYY LRNGINLTSK FSKNNLKINI FEKSNKVGGN IQTRIIQGKN
     KDEKIIVEEG PRSLRALGRG LNTLEFIKRL GISNDIIFSS ANSNGKFVLL DGKPKEIPMT
     SLFDIIKFSF KHSIVSSILK EPFKKVPSQV KEMDPNWDES VHDFFSRRLG KTMTKTFIEP
     TILGIYGGDY TNLSIKSTFK RAALLEPFGG LILGSLFKSK KQKQFELDLD KNEKRLLPSK
     NELTELFDKD TDKTNVFSFK ENGLSRMIQK LKSLIESDSL TKLYLSTSIV EIEKDVTNGT
     LKVTDNKGNQ YQYDQLISTI PLNQLAPMFK KSDSKLYQLL QSVNYTSIAV INLIYKSNKN
     VVKIISDKGF GYLVPSKENQ SVIGVCFDSN TFPEFVNNNN NNNNDNDNGN EKDQSIITVM
     IGGNNGIKDR NDNWIDVTNT SKDKLLDIAL KHLDKVLDIE SSPDFTNVSI YDNGIPHYNI
     GHQNLINEIQ NHITKNYGTT LLLGGNSIDG VGINDSIHKS KQLINSLKLS NN
//