PPOX_SCHPO
ID PPOX_SCHPO Reviewed; 490 AA.
AC Q10062;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protoporphyrinogen oxidase;
DE Short=PPO;
DE EC=1.3.3.4;
GN Name=hem14; ORFNames=SPAC1F5.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX.
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; CU329670; CAA92235.1; -; Genomic_DNA.
DR PIR; T38088; T38088.
DR RefSeq; NP_592866.1; NM_001018266.2.
DR AlphaFoldDB; Q10062; -.
DR SMR; Q10062; -.
DR STRING; 4896.SPAC1F5.07c.1; -.
DR MaxQB; Q10062; -.
DR PaxDb; Q10062; -.
DR EnsemblFungi; SPAC1F5.07c.1; SPAC1F5.07c.1:pep; SPAC1F5.07c.
DR GeneID; 2541631; -.
DR KEGG; spo:SPAC1F5.07c; -.
DR PomBase; SPAC1F5.07c; hem14.
DR VEuPathDB; FungiDB:SPAC1F5.07c; -.
DR eggNOG; KOG1276; Eukaryota.
DR HOGENOM; CLU_009629_1_0_1; -.
DR InParanoid; Q10062; -.
DR OMA; WFDQWFG; -.
DR PhylomeDB; Q10062; -.
DR Reactome; R-SPO-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00324.
DR PRO; PR:Q10062; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; ISS:PomBase.
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..490
FT /note="Protoporphyrinogen oxidase"
FT /id="PRO_0000116445"
FT BINDING 7..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 32..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 61..64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 466..468
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 490 AA; 53462 MW; CB679F6A437547AA CRC64;
MSIAICGGGI AGLSTAFYLA RLIPKCTIDL YEKGPRLGGW LQSVKIPCAD SPTGTVLFEQ
GPRTLRPAGV AGLANLDLIS KLGIEDKLLR ISSNSPSAKN RYIYYPDRLN EIPSSILGSI
KSIMQPALRP MPLAMMLEPF RKSKRDSTDE SVGSFMRRRF GKNVTDRVMS AMINGIYAGD
LNDLSMHSSM FGFLAKIEKK YGNITLGLIR ALLAREILSP AEKALKAALL AEPKTAELSN
SMKSTSMFAF KEGIETITLS IADELKKMPN VKIHLNKPAK TLVPHKTQSL VDVNGQAYEY
VVFANSSRNL ENLISCPKME TPTSSVYVVN VYYKDPNVLP IRGFGLLIPS CTPNNPNHVL
GIVFDSEQNN PENGSKVTVM MGGSAYTKNT SLIPTNPEEA VNNALKALQH TLKISSKPTL
TNATLQQNCI PQYRVGHQDN LNSLKSWIEK NMGGRILLTG SWYNGVSIGD CIMNGHSTAR
KLASLMNSSS
