ID F5BT24_EUGGR Unreviewed; 367 AA.
AC F5BT24;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 32.
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};
DE Flags: Fragment;
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039 {ECO:0000313|EMBL:AEA86536.1};
RN [1] {ECO:0000313|EMBL:AEA86536.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Z {ECO:0000313|EMBL:AEA86536.1};
RX PubMed=21444293;
RA Koreny L., Obornik M.;
RT "Sequence evidence for the presence of two tetrapyrrole pathways in Euglena
RT gracilis.";
RL Genome Biol. Evol. 3:359-364(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; JF292585; AEA86536.1; -; mRNA.
DR AlphaFoldDB; F5BT24; -.
DR UniPathway; UPA00251; UER00324.
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:SF40; LYSINE-SPECIFIC HISTONE DEMETHYLASE 2; 1.
DR PANTHER; PTHR42923; 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 2: Evidence at transcript level;
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 4..365
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEA86536.1"
FT NON_TER 367
FT /evidence="ECO:0000313|EMBL:AEA86536.1"
SQ SEQUENCE 367 AA; 39430 MW; 9B54B5729565D5EE CRC64;
VLADGSLPRF VYWEGGGASP KPANLHALPT NLPGDLLDFN LLTIPGKIRA AFGALGFIAP
APPAPYEESV REFVTRHLGE ETFERVIDPF VSGVYAGDPD QLAMRAALKK IHRLEGLGDL
GPGLVSGAIN RFKEVAKEKR ENPADPAWPT YKGGQLGSFR KGLQTLPNAV AQRLGADRVK
TSWALRQLER DGPGFRATFD TPEGPKVVRA KSVSVTAPTR VAAEVCAGLV PAASDLAKVY
SPPVASVTIA YRKEWFKALP GAQPGKPLVG FGHLLPRSMG VRSLGTIWSS SLFPGRAPEG
WELLLTYIGG ARDKGIAEMS VEEIVKQVDA DNHKILLKPD APAGKLLGCR VWQTAIPQYC
RGHLDIL
//