ID   PPOC_TOBAC              Reviewed;         548 AA.
AC   O24163;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Protoporphyrinogen oxidase, chloroplastic;
DE            Short=PPO;
DE            EC=1.3.3.4;
DE   AltName: Full=Protoporphyrinogen IX oxidase isozyme I;
DE            Short=PPO I;
DE            Short=PPX I;
DE   Flags: Precursor;
GN   Name=PPXI;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. SR1;
RX   PubMed=9238074; DOI=10.1073/pnas.94.16.8895;
RA   Lermontova I., Kruse E., Mock H.-P., Grimm B.;
RT   "Cloning and characterization of a plastidal and a mitochondrial isoform of
RT   tobacco protoporphyrinogen IX oxidase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:8895-8900(1997).
CC   -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC       to form protoporphyrin-IX. {ECO:0000269|PubMed:9238074}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:9238074}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in expanding premature leaves. Decreased
CC       expression in oldest leaves. Expressed at very low level in roots.
CC       {ECO:0000269|PubMed:9238074}.
CC   -!- INDUCTION: Oscillating expression during diurnal growth. Maximal
CC       expression in the dark period. {ECO:0000269|PubMed:9238074}.
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; Y13465; CAA73865.1; -; mRNA.
DR   PIR; T04058; T04058.
DR   AlphaFoldDB; O24163; -.
DR   SMR; O24163; -.
DR   STRING; 4097.O24163; -.
DR   BindingDB; O24163; -.
DR   ChEMBL; CHEMBL2366455; -.
DR   PRIDE; O24163; -.
DR   BioCyc; MetaCyc:MON-11760; -.
DR   BRENDA; 1.3.3.4; 3645.
DR   UniPathway; UPA00251; UER00324.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IBA:GO_Central.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; FAD; Flavoprotein;
KW   Heme biosynthesis; Oxidoreductase; Plastid; Porphyrin biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..548
FT                   /note="Protoporphyrinogen oxidase, chloroplastic"
FT                   /id="PRO_0000013326"
FT   REGION          265..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78..83
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         101..102
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         123..126
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         522..524
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  59230 MW;  66892E78FB8A3E30 CRC64;
     MTTTPIANHP NIFTHQSSSS PLAFLNRTSF IPFSSISKRN SVNCNGWRTR CSVAKDYTVP
     SSAVDGGPAA ELDCVIVGAG ISGLCIAQVM SANYPNLMVT EARDRAGGNI TTVERDGYLW
     EEGPNSFQPS DPMLTMAVDC GLKDDLVLGD PNAPRFVLWK GKLRPVPSKL TDLAFFDLMS
     IPGKLRAGFG AIGLRPSPPG HEESVEQFVR RNLGGEVFER LIEPFCSGVY AGDPSKLSMK
     AAFGKVWKLE ETGGSIIGGT FKAIKERSST PKAPRDPRLP KPKGQTVGSF RKGLRMLPDA
     ISARLGSKLK LSWKLSSITK SEKGGYHLTY ETPEGVVSLQ SRSIVMTVPS YVASNILRPL
     SVAAADALSN FYYPPVGAVT ITYPQEAIRD ERLVDGELKG FGQLHPRTQG VETLGTIYSS
     SLFPNRAPKG RVLLLNYIGG AKNPEILSKT ESQLVEVVDR DLRKMLIKPK AQDPLVVGVR
     VWPQAIPQFL VGHLDTLSTA KAAMNDNGLE GLFLGGNYVS GVALGRCVEG AYEVASEVTG
     FLSRYAYK