ID   A0A135V1S4_9PEZI        Unreviewed;       615 AA.
AC   A0A135V1S4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=CSAL01_04417 {ECO:0000313|EMBL:KXH66579.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH66579.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH66579.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH66579.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-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:KXH66579.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JFFI01000641; KXH66579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135V1S4; -.
DR   STRING; 1209931.A0A135V1S4; -.
DR   OrthoDB; 65450at2759; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000070121; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT   DOMAIN          84..565
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   615 AA;  67730 MW;  559784C2CDB5EA87 CRC64;
     MVLRRADNAF MALLRSYHSQ RFCNAALGAC GRSAAAAVVP ARRSFSASIV VARQEQRQSR
     KEAEPIFSKN IQVPTDIAVI GGGIAGLTTA HYLAKLLPET SNITIYEAGD RLGGWINTQE
     LEVEVNGKKS NVRFERGPRT LRGMGKDTWK FDDLVLFDLI RDLQMQGEYL GIKSPPRYIY
     YPDHLVEMHP RNVFREAAFK GIIPGFLNLM WRRQKAREEV KPIDMSVADF IATYTGRPEL
     VDNLASAMIH GIWGGDADKL SMRSFMPGPW HRFFDKPFPE DNWLSFPRSE VGVLATLGAD
     EGLRSYLKTA QKDQLVFFEK GMSSLPDTIA EHLRKRKNVT FKMGEPVTGL EYDRKGKKVM
     LSSPNSTSPT AYDKVISTIT SKALYAATGD VVPSLANSPN VSIMAVNLWY PQPNLNASHP
     GVGYLVPRAT DSNLEGLLGV FFDSDVVPRA PDEPEGTKFF VLMGGHYFDG LPEGALPTEA
     EGIEMAKAVL ERHLGIPQST PAFAMASLAK DCIPQHHVGH SQRMAHASYE LRDAFKGQLA
     VAGGSYTGIG VMGALRAGYD VAVHIAQSAQ AHVGDTGLEQ FEGGAMFEKF ARTRSSIKAI
     GRDIDAEIGW KNYIR
//