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Database: UniProt
Entry: H2KPX6_CLOSI
LinkDB: H2KPX6_CLOSI
Original site: H2KPX6_CLOSI 
ID   H2KPX6_CLOSI            Unreviewed;       509 AA.
AC   H2KPX6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=CLF_102762 {ECO:0000313|EMBL:GAA33006.1};
OS   Clonorchis sinensis (Chinese liver fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX   NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA33006.1, ECO:0000313|Proteomes:UP000008909};
RN   [1] {ECO:0000313|EMBL:GAA33006.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Henan {ECO:0000313|EMBL:GAA33006.1};
RX   PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA   Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA   Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA   Yu X.;
RT   "The draft genome of the carcinogenic human liver fluke Clonorchis
RT   sinensis.";
RL   Genome Biol. 12:R107-R107(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Henan;
RA   Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA   Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA   Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA   Wu Z., Yu X.;
RT   "The genome and transcriptome sequence of Clonorchis sinensis provide
RT   insights into the carcinogenic liver fluke.";
RL   Submitted (OCT-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; DF142943; GAA33006.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2KPX6; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000008909; 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:UP000008909}.
FT   DOMAIN          15..502
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   509 AA;  56060 MW;  399B9B4A2D00D58D CRC64;
     MATRLPHYCI VGGGISGLST AYFISLVRPP GSCRLTVLEA ENKFGGWIHS MKNPRTGAVY
     ELGPHSARAV GPTSKLLLRL ALSLDLHNSL LWMRSDEDAV RRFIYVGGSL AEISPFRLHK
     EKPFTRTHIG MFARRLFASR PPHKSDWSVD EFLRTRFDDE LADYLGSAMM RGIYAGDSRE
     LSARACLPKL VETEENGPNL VLGMLLSAIR PSKSSSSSVA IPSEIDSKLP EIDSILPSKT
     FAWSLHNGMQ TITDRLAQKI RDLGPHVTLQ ANACVRGISH SRGKFSVQWG DEQNLHANLH
     DIDALFLCCP SYQSAELLKE LASPLVISRL RKDKLPWANV AATVVELDRK SAQPPVRGFG
     HLVPRTEDPH ILGIVYDSVA FPGLDSPNGS SVRYTVMLTP PSDWLSCGQC IDEKIEKKAL
     DALKEHLKFQ NLEVLGSKST LLRDCIPQYP LGHIENIRAA REELRSSLSQ QSFNSSAIHL
     VGSSYDGVGL GDVVYSALKA VCCELNLSV
//
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