ID H0ECS5_GLAL7 Unreviewed; 659 AA.
AC H0ECS5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=M7I_0220 {ECO:0000313|EMBL:EHL03579.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL03579.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHL03579.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
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:EHL03579.1}.
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DR EMBL; AGUE01000006; EHL03579.1; -; Genomic_DNA.
DR AlphaFoldDB; H0ECS5; -.
DR HOGENOM; CLU_009629_1_0_1; -.
DR InParanoid; H0ECS5; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000005446; 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:UP000005446}.
FT DOMAIN 127..618
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 659 AA; 72617 MW; 9C3D8291046F126C CRC64;
MCKFNPCLNP SCVYKHIDGQ KRGKFEDKVW VANGGKEHVS ERKFVDENEM EEELIKPETG
SEEAKFNNIS AAPVDVVTTT YLKRTEDRYA PSIFDELLKK PIVHNLLKKP QYDENSKPEF
AVLGGGITGL STAHYLTKNI PHANVTIYES TDRLGGWLSS ERVAVDGGDI VFEQGPRSLR
PNENGSGLTV MELIQDLDLQ DQILTTPKDS ASARNRYIYY PDKLVKLPGP GTNLFTNLFS
VLTSPALNWI PMALWREYNN PGRPPSMDDE SLYDFLLRRL GTSEAADKAL SAGLHGIYAG
DITQLSVKSL MPLVWSMERK FGSIMKGWRE LGPRIAWKNT ADVELGVELI GKIEPSIFVR
LSQSSVFSFK EGIGAIPVAL EKSLRANPKV QFKKGVWVKS LSFDHETENI KITTSENVPP
ALYTKVISTL SGPNTSSIIP QDGTALRSPN QPQTHLKPLA DIHSVTVMVV NLYFPSTTVL
PVHGFGYLIP RAIPFDQNPE CALGVVFDSD TIGNQDTVEG TKLTVMLGGH WWDGMDSYPE
SEEGVIMARN VIARHLGITD EPTATKAGLH KNCIPQYTVG HEARLLAAHD ELKEKFGGGL
AVAGNSYAGV GLSDCVRGAR DLVMGLAYKN KKMTGLENVQ THTQYRALPA PPPLPALKY
//