PPOX_DICDI
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 03-AUG-2022, entry version 97.
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 (Slime mold).
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.DDB0231419; -.
DR PaxDb; Q54DT8; -.
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:0031304; C:intrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; -; 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 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
