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Database: UniProt
Entry: G2YMJ2_BOTF4
LinkDB: G2YMJ2_BOTF4
Original site: G2YMJ2_BOTF4 
ID   G2YMJ2_BOTF4            Unreviewed;       614 AA.
AC   G2YMJ2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=BofuT4_P137640.1 {ECO:0000313|EMBL:CCD52840.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD52840.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; FQ790345; CCD52840.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2YMJ2; -.
DR   STRING; 999810.G2YMJ2; -.
DR   eggNOG; KOG1276; Eukaryota.
DR   HOGENOM; CLU_009629_1_0_1; -.
DR   InParanoid; G2YMJ2; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000008177; Unplaced contigs.
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:UP000008177}.
FT   DOMAIN          100..588
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          63..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  68387 MW;  56A4C5BCFCE0907F CRC64;
     MRMRLPESPL LAPLRRCYNI PQCQVVRLRR RNVLGSCTRA YSYQTRPQLH TRERSKPLLK
     YYSSHAQSNP PTRKSAEVIS ENKSSEEWKE PSVAILGGGI TGLATAYYLT QMAPHLKVTL
     YESSERLGGW LRTKHIDVGD GEVVFEQGPR TLRPNTPAGF VTLNLIRDLG LSDEVIKTNK
     LSAAALNRFV YYPDRLVCMP EPSQGIYAIA WKMLTEPVFK GMHRLLFEYK RPRRPAELDD
     ESVGSFLARR TGGTDIPDNL VSAVFHGIYA GDIYKLSAKS IMPSQWGMEG AFGSISAGIS
     QMAKFKNATA EDADLEEKER SSFTDNERAI INETSVYTFR RGIGTLSEAL DSSLRNNPNV
     KIKLGEDVGK IEYDGQSEGI KIYTAQAGES STNHSYVIST LSGRTLSTLT TPSDDSLLPS
     LAKTEAVTVM VVNLYYRDED LLPERGFGYL IPRSIPFDQN PEFALGVVFD SDATVGQDTV
     PGTKVTVMLG GHWWDDFETY PSEEEGAAMA KAVLKRHLKI DQEPEMVHAS LQKDCIPQYT
     VGHEQRLKQA HYELLSAYKG RLAVAGNSYT GVGVNDCIKA AKVVAGDVAR GNDVTGLEKF
     AEQKWWEKMI KREQ
//
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