PPOX_YEAST
ID PPOX_YEAST Reviewed; 539 AA.
AC P40012; D3DLR1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protoporphyrinogen oxidase {ECO:0000303|PubMed:8621563};
DE Short=PPO {ECO:0000303|PubMed:8621563};
DE EC=1.3.3.4 {ECO:0000269|PubMed:7798202};
GN Name=HEM14 {ECO:0000303|PubMed:8621563}; OrderedLocusNames=YER014W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF LEU-422 AND
RP LYS-424.
RX PubMed=8621563; DOI=10.1074/jbc.271.15.9120;
RA Camadro J.-M., Labbe P.;
RT "Cloning and characterization of the yeast HEM14 gene coding for
RT protoporphyrinogen oxidase, the molecular target of diphenyl ether-type
RT herbicides.";
RL J. Biol. Chem. 271:9120-9128(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 25657 / D273-10B;
RX PubMed=7798202; DOI=10.1016/s0021-9258(18)31604-1;
RA Camadro J.-M., Thome F., Brouillet N., Labbe P.;
RT "Purification and properties of protoporphyrinogen oxidase from the yeast
RT Saccharomyces cerevisiae. Mitochondrial location and evidence for a
RT precursor form of the protein.";
RL J. Biol. Chem. 269:32085-32091(1994).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000269|PubMed:7798202,
CC ECO:0000269|PubMed:8621563}.
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 Evidence={ECO:0000269|PubMed:7798202};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P32397};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 uM for protoporphyrinogen IX {ECO:0000269|PubMed:7798202};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:7798202};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000269|PubMed:7798202}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:7798202}. Note=Bound to the mitochondrial inner
CC membrane with its active site facing the cytosolic side.
CC {ECO:0000269|PubMed:7798202}.
CC -!- MISCELLANEOUS: Present with 5350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily. {ECO:0000305}.
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DR EMBL; Z71381; CAA95981.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64547.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07665.1; -; Genomic_DNA.
DR PIR; S50472; S50472.
DR RefSeq; NP_010930.1; NM_001178905.1.
DR AlphaFoldDB; P40012; -.
DR SMR; P40012; -.
DR BioGRID; 36746; 37.
DR MINT; P40012; -.
DR STRING; 4932.YER014W; -.
DR SwissPalm; P40012; -.
DR MaxQB; P40012; -.
DR PaxDb; P40012; -.
DR PRIDE; P40012; -.
DR EnsemblFungi; YER014W_mRNA; YER014W; YER014W.
DR GeneID; 856733; -.
DR KEGG; sce:YER014W; -.
DR SGD; S000000816; HEM14.
DR VEuPathDB; FungiDB:YER014W; -.
DR eggNOG; KOG1276; Eukaryota.
DR GeneTree; ENSGT00390000008744; -.
DR HOGENOM; CLU_009629_1_2_1; -.
DR InParanoid; P40012; -.
DR OMA; WFDQWFG; -.
DR BioCyc; YEAST:YER014W-MON; -.
DR Reactome; R-SCE-189451; Heme biosynthesis.
DR SABIO-RK; P40012; -.
DR UniPathway; UPA00251; UER00324.
DR PRO; PR:P40012; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40012; protein.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IDA:SGD.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:SGD.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Heme biosynthesis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..539
FT /note="Protoporphyrinogen oxidase"
FT /id="PRO_0000135274"
FT BINDING 18..23
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 43..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 70..73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 521..523
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT MUTAGEN 422
FT /note="L->P: In HEM14-1; loss of activity."
FT /evidence="ECO:0000269|PubMed:8621563"
FT MUTAGEN 424
FT /note="K->E: In HEM14-1; loss of activity."
FT /evidence="ECO:0000269|PubMed:8621563"
SQ SEQUENCE 539 AA; 59703 MW; 5ECCBD1C033BA5B1 CRC64;
MLLPLTKLKP RAKVAVVGGG VSGLCFTYFL SKLRPDVEIT LFESQNRTGG WIYSCNTRDM
SGNPIMLEKG PRTLRGVSDG TVLIMDTLKD LGKEAVIQSI DKGCIADKKF LLDPSDKLVQ
VPNSISTTVK FLLNPLGKGL ITGMMGEWFR KKSPHPGQDE SVESICDRRF GNNYISNNMI
SALLRGIYGD DVSLLSAKRT FKKIYYNELK HGSNTQAMID NMRGKSRSKK TENLHQSLTG
CLNDYSNAFG KDRSKLLDLS NTLKKYPMLG LAGGLETFPK IVRNALNEFK NVKIVTGNPV
TQIMKRPANE TTIGLKAKSG DQYETFDHLR LTITPPKIAK LLPKDQNSLS KLLDEIQSNT
IILVNYYLPN KDVIDADLQG FGYLVPKSNK NPGKLLGVIF DSVIERNFKP LFDKLSTNPN
ALNKYTKVTA MIGGCMLNEH GVPVVPSREV TINAVKDALN NHLGISNKDL EAGQWEFTIA
DRCLPRFHVG YDAWQERAER KLQESYGQTV SVGGMGFSRS PGVPDVIVDG FNDALQLSK
