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Database: UniProt
Entry: H6C883_EXODN
LinkDB: H6C883_EXODN
Original site: H6C883_EXODN 
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
//
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