ID A5KE11_PLAVS Unreviewed; 712 AA.
AC A5KE11;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=protoporphyrinogen oxidase {ECO:0000256|ARBA:ARBA00012867};
DE EC=1.3.3.4 {ECO:0000256|ARBA:ARBA00012867};
GN ORFNames=PVX_111315 {ECO:0000313|EMBL:EDL42464.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000313|EMBL:EDL42464.1, ECO:0000313|Proteomes:UP000008333};
RN [1] {ECO:0000313|EMBL:EDL42464.1, ECO:0000313|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL42464.1,
RC ECO:0000313|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M.,
RA Crabb B.S., Del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000256|ARBA:ARBA00002600}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005073}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily.
CC {ECO:0000256|ARBA:ARBA00010551}.
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:EDL42464.1}.
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; AAKM01002769; EDL42464.1; -; Genomic_DNA.
DR RefSeq; XP_001608488.1; XM_001608438.1.
DR AlphaFoldDB; A5KE11; -.
DR STRING; 126793.A5KE11; -.
DR EnsemblProtists; EDL42464; EDL42464; PVX_111315.
DR GeneID; 5471292; -.
DR KEGG; pvx:PVX_111315; -.
DR VEuPathDB; PlasmoDB:PVX_111315; -.
DR InParanoid; A5KE11; -.
DR OMA; SADKTNH; -.
DR PhylomeDB; A5KE11; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000008333; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 Pfam; PF13450; NAD_binding_8; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000008333};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 204..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 420..680
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 80114 MW; 95F8D4F3DA092CE5 CRC64;
MRDETTMRDG PTMRDGPTMR DGPTRANASS GVSTPTGTDE GPPMEQHTYD VVIVGGGLFS
CCLHYFLKRK KPNITILILE KEQTLGGYIK TEWLEDQGKN FLCELGPNIF KISDDSYQLL
KELNLLSHVR VLNRKLLRYV YSGGKLHPLR LTIWGYFAFP LISVTNKVKL LYRLLFKRYK
RLSTYDEDIS VEDYMRENFD LQHYNFLLLP LIYGSCGGVG SISAISFFSR NLKLFDSKMN
SLRVWQERAR RGVYPVGPFD PVNRADRVDC LSGGKAGGAA PPPVGLQHSF AQRMNHTYDQ
APSFNSVLYR QDTPSGDTVG GDSVGGDTIG GDTAGGDSLG GEAHSGPVNS GPTKSGSESR
SPERGIPESG IPSNSSLSND ECATERHAGV DAMKGQRSFA DTAPPVEGCL HFVKRIYAKC
KRAVLQVMPL FYPQLAKKGS KAYEQKKKKK ILGKTISLKY GMYEIIDKLK KNINKKYVWT
NEEVDFVEKH NEDTWVCTIK KKHSNKTACI YGRNVILTVN SKTCANIMRK ILPPEMKDNL
VNVQYTNIIS VTVYYHKKDI TLPPNCFGFL SADKTNHILG CFYTSNMFKE RCNDDSVVVL
TLYMGGQNNP NDVYLEEKEI TQIVSKELTK IFHVQNNAQP VILKVKKWFD SIPFYSHNYE
RHLKRFLNEL HNPQYRNLFV DSGWITGTSI SDRIASARDL SEFMAASVLA VK
//
