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Database: UniProt
Entry: D8PWQ6_SCHCM
LinkDB: D8PWQ6_SCHCM
Original site: D8PWQ6_SCHCM 
ID   D8PWQ6_SCHCM            Unreviewed;       502 AA.
AC   D8PWQ6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=SCHCODRAFT_50115 {ECO:0000313|EMBL:EFJ01081.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFJ01081.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
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; GL377303; EFJ01081.1; -; Genomic_DNA.
DR   RefSeq; XP_003035983.1; XM_003035937.1.
DR   AlphaFoldDB; D8PWQ6; -.
DR   STRING; 578458.D8PWQ6; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_02525011; -.
DR   eggNOG; KOG1276; Eukaryota.
DR   HOGENOM; CLU_009629_1_1_1; -.
DR   InParanoid; D8PWQ6; -.
DR   OMA; EHNQAVQ; -.
DR   OrthoDB; 65450at2759; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000007431; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140907; F:flavin-dependent halogenase activity; IEA:UniProt.
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:UP000007431}.
FT   DOMAIN          13..350
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          483..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  54904 MW;  1ECD3F18CF8A6113 CRC64;
     MAPHHIAVLG GGLTGLSSAY HLSHRFPNAL ITLVERSTRV GGWAESERVS LKDPKDGSEA
     SILIEGGPRT LRPTAKSVLE LVTRLDLLDD LILVPRTSPS AKNKYFHMPG QPGLLAVPSS
     FKGLISSPLG ACLTRAVAKE AMAFSNRDDL KDESFDSFLC RRFTAEFAEK VGSALVHGIF
     AADSRKLSVR AAFPVLWEAE EYGWGSVVRG FIRGRREEDV EESYYISNPV QKAMEETAVF
     SFRNGMDTVA RATEHHLSKL KNVTILKGAD VKSLGVNSKD KSIEVQIRPT HVVSTLPLPA
     LHRVLTPTSN LPHLTTNPYS TVTVYNLIFR TDTPTPIHPA GFGYLIPRPP GGYEQPQANK
     EGILGCVFDS CALSAQDVMP GPTKYTKMTV MTGGPYQNKP PALDTVLQAL ARHLDWPEVY
     EPVYTRVREN RDCIPVPAPG HLERVAELRR VLKEGEWQGR MEVVGAGVGG VSVGDCVEAG
     RWVGEGWGPS TPQMEDDECD DE
//
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