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Database: UniProt
Entry: A0A0A8L2V9_9SACH
LinkDB: A0A0A8L2V9_9SACH
Original site: A0A0A8L2V9_9SACH 
ID   A0A0A8L2V9_9SACH        Unreviewed;       536 AA.
AC   A0A0A8L2V9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Protoporphyrinogen oxidase {ECO:0000256|ARBA:ARBA00044160, ECO:0000256|RuleBase:RU367069};
DE            EC=1.3.3.4 {ECO:0000256|ARBA:ARBA00012867, ECO:0000256|RuleBase:RU367069};
GN   ORFNames=KLDO_g858 {ECO:0000313|EMBL:CDO92540.1};
OS   Kluyveromyces dobzhanskii CBS 2104.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO92540.1, ECO:0000313|Proteomes:UP000031516};
RN   [1] {ECO:0000313|EMBL:CDO92540.1, ECO:0000313|Proteomes:UP000031516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA   Nystedt B., Astrom S.;
RT   "The genome of Kluyveromyces dobzhanskii.";
RL   Submitted (MAR-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDO92540.1}.
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DR   EMBL; CCBQ010000016; CDO92540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8L2V9; -.
DR   OrthoDB; 65450at2759; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000031516; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU367069};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|RuleBase:RU367069}.
FT   DOMAIN          22..530
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   536 AA;  59295 MW;  71DD64DA2F22DC5B CRC64;
     MQPTVSTLPL NAKIAVVGAG VSGLTFTYFL SKLRPDVNVT LYESKERCGG WIHSETINDH
     DGSQVMVEKG PRTLRGVSDG SVIIVETLRD LGKQDVIQYI APNSEANRKF LLDQNDVLTQ
     VPDSPATALK FISGSLGKGF IPGILGEPFR LSKTTRSDES AHSFIKRRFG NEYLSQNVFS
     ALFHGIYAGD IKKLSAKRTI GKMVDMEKTA GSLIKSMLNN TINKYNKRGD TKVKTTELSP
     LLKKFGAATG KSDEDLLSVS LRLKEFPMIG FKTGLECYPK TLTEYITSLP NVTIKHEAAN
     SVLPGKHGKG VIIESDSGDL TFEHARLTIT PNILANMVQF EPVAKKLREV HSNTVLLVNF
     YLPHKDLLSS YHGFGYLVPQ SNQNQEKLLG VIFDSVIEKN FKPVFESESE ASKKVQETKY
     TKVTAMLGGH YLNNEGEQNI PSESIIINSV KSAFMKHLHI DENDLEDGRW EVTVAKDCLP
     QYHVGYDDWV QQTAELIQER YSDNVSLGGM AFSTGPGVPN VIEDAFESAY MLSEAN
//
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