PPOC_SPIOL
ID PPOC_SPIOL Reviewed; 562 AA.
AC Q9LRI8;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Protoporphyrinogen oxidase 1, chloroplastic {ECO:0000305};
DE EC=1.3.3.4 {ECO:0000250|UniProtKB:P55826};
DE AltName: Full=SO-POX1 {ECO:0000303|PubMed:10982422};
DE Flags: Precursor;
GN Name=POX1 {ECO:0000303|PubMed:10982422};
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-68, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Leaf;
RX PubMed=10982422; DOI=10.1104/pp.124.1.59;
RA Che F.S., Watanabe N., Iwano M., Inokuchi H., Takayama S., Yoshida S.,
RA Isogai A.;
RT "Molecular characterization and subcellular localization of
RT protoporphyrinogen oxidase in spinach chloroplasts.";
RL Plant Physiol. 124:59-70(2000).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000250|UniProtKB:P55826}.
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:0000250|UniProtKB:P55826};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O24164};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O24164};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000305}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:10982422}; Peripheral membrane protein
CC {ECO:0000305}; Stromal side {ECO:0000269|PubMed:10982422}. Plastid,
CC chloroplast inner membrane {ECO:0000269|PubMed:10982422}; Peripheral
CC membrane protein {ECO:0000305}; Stromal side
CC {ECO:0000269|PubMed:10982422}. Note=Preferentially associates with the
CC stromal side of the thylakoid membrane, but also localizes on the
CC stromal side of the inner envelope membrane.
CC {ECO:0000269|PubMed:10982422}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily. {ECO:0000305}.
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; AB029492; BAA96808.1; -; mRNA.
DR AlphaFoldDB; Q9LRI8; -.
DR SMR; Q9LRI8; -.
DR KEGG; ag:BAA96808; -.
DR UniPathway; UPA00251; UER00324.
DR UniPathway; UPA00668; -.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:UniProtKB.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055035; C:plastid thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; FAD; Flavoprotein;
KW Heme biosynthesis; Membrane; Oxidoreductase; Plastid;
KW Plastid inner membrane; Porphyrin biosynthesis; Thylakoid; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10982422"
FT CHAIN 49..562
FT /note="Protoporphyrinogen oxidase 1, chloroplastic"
FT /id="PRO_0000443726"
FT REGION 274..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O24164"
FT BINDING 115..116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O24164"
FT BINDING 137..140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O24164"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O24164"
FT BINDING 536..538
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O24164"
SQ SEQUENCE 562 AA; 59929 MW; 638DCF6E63D259C4 CRC64;
MSAMALSSTM ALSLPQSSMS LSHCRHNRIT ILIPSSSLRR RGGSSIRCST ISTSNSAAAA
NYQNKNIGTN GVDGGGGGGG VLDCVIVGGG ISGLCIAQAL STKYSNLSTN FIVTEAKDRV
GGNITTMEAD GYLWEEGPNS FQPSDAVLTM AVDSGLKEEL VLGDPNSPRF VLWNGKLRPV
PSKLTDLPFF DLMSFPGKIR AGLGALGLRP SPPAHEESVE QFVRRNLGDE VFERLIEPFC
SGVYAGDPSK LSMKAAFGRV WVLEQKGGSI IGGTLKTIQE RKDNPKPPRD PRLPKPKGQT
VGSFRKGLSM LPTAISERLG NKVKVSWTLS GIAKSSNGEY NLTYETPDGL VSVRTKSVVM
TVPSYVASSL LRPLSDVAAE SLSKFHYPPV AAVSLSYPKE AIRSECLIDG ELKGFGQLHS
RSQGVETLGT IYSSSLFPGR APPGRTLILN YIGGDTNPGI LDKTKDELAE AVDRDLRRIL
INPNAKAPRV LGVRVWPQAI PQFLIGHFDL LDAAKAALTD GGHKGLFLGG NYVSGVALGR
CIEGAYESAA EVVDFLSQYS DK
