ID A0A058ZY55_EUCGR Unreviewed; 531 AA.
AC A0A058ZY55;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=EUGRSUZ_K00558 {ECO:0000313|EMBL:KCW46742.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW46742.1};
RN [1] {ECO:0000313|EMBL:KCW46742.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW46742.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) 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: Plastid, chloroplast
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; KK198763; KCW46742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A058ZY55; -.
DR STRING; 71139.A0A058ZY55; -.
DR EnsemblPlants; KCW46742; KCW46742; EUGRSUZ_K00558.
DR Gramene; KCW46742; KCW46742; EUGRSUZ_K00558.
DR eggNOG; KOG1276; Eukaryota.
DR InParanoid; A0A058ZY55; -.
DR OMA; WFDQWFG; -.
DR UniPathway; UPA00251; UER00324.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IBA:GO_Central.
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 Gene3D; 1.10.3110.10; protoporphyrinogen ix oxidase, domain 3; 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:SF40; PROTOPORPHYRINOGEN OXIDASE 1, CHLOROPLASTIC; 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}.
FT DOMAIN 62..517
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 249..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 56654 MW; 1CE9070054AEB9B6 CRC64;
MAAFATATSA AAASASAAVI RPPRAARAPA GIRCSVAEGP AVSQPRAAGG GLADCVVVGA
GISGLCVAQA LATRHRDRAP DVVVTEARDR VGGNITSVER DGYLWEEGPN SFQPSDPMLT
MAVDSGLKDD LVLGDPNAPR FVLWNGKLRP VPSKPTDLPF FDLMSVGGKL RAGFGALGIR
PPPPGYEELV EEFVRRNLGD EVFERLIEPF CVYAGDPSKL SMKAAFGRVW KLEQIGGSII
GGTFKTIQEK NKAPKAPRDP RLPKPKGQTV GSFRKGLTML PNAIYERLGS KVKLSWKLLS
ITRMDDRGYN LTYETPEGVV SLQTKSVVMT IPSHVASGLL RPLSTAAADA LSKFYYPPVA
AVTLSYPKEA IRSERLIDGE LKGFGQLHPR SQGVETLGCL YSSSLFPNRA PEGRVLLLSY
IGGATNPGIV SKTPGELVEA VDRDLRKMLI NPGAKDPLAL GVRVWPQAIP QFLVGHLDHL
DSAKAALKDI GFQGMFLGGN YVSGVALGRC VEGAYEVAAE VSNFLSLYAY K
//
