ID K3UA54_FUSPC Unreviewed; 601 AA.
AC K3UA54;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=FPSE_11592 {ECO:0000313|EMBL:EKJ68221.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ68221.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ68221.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ68221.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(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:EKJ68221.1}.
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DR EMBL; AFNW01000609; EKJ68221.1; -; Genomic_DNA.
DR RefSeq; XP_009262984.1; XM_009264709.1.
DR AlphaFoldDB; K3UA54; -.
DR EnsemblFungi; EKJ68221; EKJ68221; FPSE_11592.
DR GeneID; 20370209; -.
DR KEGG; fpu:FPSE_11592; -.
DR eggNOG; KOG1276; Eukaryota.
DR HOGENOM; CLU_009629_1_0_1; -.
DR OrthoDB; 65450at2759; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000007978; Chromosome 1.
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:UP000007978}.
FT DOMAIN 84..567
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 601 AA; 65815 MW; DB2CF809B3D94B6A CRC64;
MSRSRAESTA AALLSSAARS TTKPHLQVPL RRLNGFRSLS TCSASVLTRR RPIVACKHTQ
SFNDGRRYVS QAKDANIAVI GGGLTGLSAA YYLAKKLPST TKITLYEACD RLGGWIKTDR
VPVDIGGKKG IVSFERGSRS LTSLAGNTFR FDDLVLYDLT LDLGLSLNFP PAKPRYVYYP
DHLVSMPPNV SIFDIIREPL YLESIGAGLG LMINHLRKRH LPAEDESVAD WLYKVTNSRK
GIGNMASAMM HGIYGGDIHK LSARSVLDRI YWGWYLPNPG LHARPMPVPE SLILETLGQD
RQIQKLALEP KSALIDFGDK GMESLPQAIG AALQDQPNVT IKTGEAVKDI QYDEAKQQVQ
INSFSAKNEE KSNSQAYDKV ISTLSAQQIA RLASDKVPSL SAAHSVSVMT VNIWFPQENL
KPPGFGYLIP NSVDPELNPE HALGVFFDSD VGTRSKDEPA GTKLFVLMGG HYYDRPDVTP
PTEEEAIVQA RNLLERHLGI PRDAPAYATA NFAKECIPQH YVGHQGLLRN AHAELKQNFG
GRLAVAGGSF HRIGTIASLR SGYDAAVAAK SGLEATGLEY VENIQEFAVL STELIPVRHF
K
//
