ID H6C883_EXODN Unreviewed; 641 AA.
AC H6C883;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Protoporphyrinogen oxidase {ECO:0000256|ARBA:ARBA00012867, ECO:0000256|RuleBase:RU367069};
DE EC=1.3.3.4 {ECO:0000256|ARBA:ARBA00012867, ECO:0000256|RuleBase:RU367069};
GN ORFNames=HMPREF1120_08276 {ECO:0000313|EMBL:EHY60310.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY60310.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY60310.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY60310.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000256|ARBA:ARBA00002600,
CC ECO:0000256|RuleBase:RU367069}.
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:0000256|ARBA:ARBA00000672,
CC ECO:0000256|RuleBase:RU367069};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU367069};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU367069};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005073, ECO:0000256|RuleBase:RU367069}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU367069}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily.
CC {ECO:0000256|ARBA:ARBA00010551, ECO:0000256|RuleBase:RU367069}.
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DR EMBL; JH226136; EHY60310.1; -; Genomic_DNA.
DR RefSeq; XP_009160771.1; XM_009162523.1.
DR AlphaFoldDB; H6C883; -.
DR STRING; 858893.H6C883; -.
DR GeneID; 20312915; -.
DR VEuPathDB; FungiDB:HMPREF1120_08276; -.
DR eggNOG; KOG1276; Eukaryota.
DR HOGENOM; CLU_009629_1_0_1; -.
DR InParanoid; H6C883; -.
DR OMA; WFDQWFG; -.
DR OrthoDB; 65450at2759; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU367069};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU367069};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133,
KW ECO:0000256|RuleBase:RU367069};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367069};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU367069};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 67..603
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 641 AA; 70440 MW; EA8AEEFDB5D9A70C CRC64;
MRLGGRNALL SHAVKPWSRS RATATAAHLR LQSRSYSTPP PSIVGNAPLR DSPNPNAKSV
AILGGGITGL AAAWNLQRNI PGVKVIIYEK SHVLGGWVQS ERIPVQDGHI LFEWGPRTLR
PALSSLSGAA TVDLIAQLGI VDSLVPIAKD SPAAANRFIY YPDHPVVMPG PGLGLWGLIS
RLLKLRREPI FNGVLQGLLV EPYVAPRNPS VKDESVGDFL ARRFGKPLAD NFASAFFQGI
YAGDIYKLSA RTTLPLLWHL EGRYTENEVG VLLQFAALRY QGRALIPKTD AFFTDVYART
EAAAASVARE SYTSMKALAL MLLRQASVYT FTDGLSKMTV ALADRLSDSP NVELRTSSPV
DDVTYDKKKA KVSVRSGNRI DNFDYVVSTL GPGMTNKFLS STASTRGAAL EPQVTKACER
NGKGVTVMVV NLYYPTPDML PQYIRGFGYL IPRTVPLEEN PERALGVIFG SETSGRPDTL
VYPLRHDGTK AQDTGPGTKI TVMLGGHWWD GWAPSDLPSE EQAIEMAKAL LLRHLGVDGY
PEVAKAQLNR NCIPQYPVGY RDDMATIHKS LMCEFDGRFK VAGPWWQGGV GMGDSIRKAR
EVSWMIEQQW DDRTGLEHYD GEDEWYVWDS NAKQLVKDPA T
//