PPOM_TOBAC
ID PPOM_TOBAC Reviewed; 504 AA.
AC O24164;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protoporphyrinogen oxidase, mitochondrial;
DE EC=1.3.3.4;
DE AltName: Full=PX-2;
DE AltName: Full=Protoporphyrinogen IX oxidase isozyme II;
DE Short=PPO II;
DE Short=PPX II;
GN Name=PPXII; Synonyms=PPOX2;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun NN;
RX PubMed=9808719; DOI=10.1104/pp.118.3.751;
RA Watanabe N., Che F., Iwano M., Takayama S., Nakano T., Yoshida S.,
RA Isogai A.;
RT "Molecular characterization of photomixotrophic cultured tobacco cells
RT resistant to protoporphyrinogen oxidase-inhibiting herbicides.";
RL Plant Physiol. 118:751-758(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SR1;
RA Horikoshi M., Mametsuka K., Hirooka T.;
RT "The molecular basis of photobleaching herbicide resistance in Tobacco.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR
RP AND FAD, IDENTIFICATION BY MASS SPECTROMETRY, AND COFACTOR.
RX PubMed=15057273; DOI=10.1038/sj.emboj.7600189;
RA Koch M., Breithaupt C., Kiefersauer R., Freigang J., Huber R.,
RA Messerschmidt A.;
RT "Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem
RT and chlorophyll biosynthesis.";
RL EMBO J. 23:1720-1728(2004).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000269|PubMed:9238074}.
CC -!- FUNCTION: Provides precursor for the mitochondrial and plastidic heme
CC synthesis and the predominant chlorophyll synthesis in plastids.
CC {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;
CC Evidence={ECO:0000269|PubMed:15057273};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15057273};
CC -!- ACTIVITY REGULATION: Inhibited by the herbicide acifluorfen.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9238074}.
CC -!- DEVELOPMENTAL STAGE: Expressed in expanding premature leaves. Decreased
CC expression in oldest leaves. Also detected 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; Y13466; CAA73866.1; -; mRNA.
DR EMBL; AB020500; BAA34712.1; -; mRNA.
DR EMBL; AF044129; AAD02291.1; -; mRNA.
DR PIR; T04076; T04076.
DR RefSeq; NP_001312887.1; NM_001325958.1.
DR PDB; 1SEZ; X-ray; 2.90 A; A/B=1-504.
DR PDBsum; 1SEZ; -.
DR AlphaFoldDB; O24164; -.
DR SMR; O24164; -.
DR STRING; 4097.O24164; -.
DR BindingDB; O24164; -.
DR ChEMBL; CHEMBL1926489; -.
DR PRIDE; O24164; -.
DR GeneID; 107815753; -.
DR KEGG; nta:107815753; -.
DR PhylomeDB; O24164; -.
DR BioCyc; MetaCyc:MON-11759; -.
DR BRENDA; 1.3.3.4; 3645.
DR UniPathway; UPA00251; UER00324.
DR EvolutionaryTrace; O24164; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; -; 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 3D-structure; FAD; Flavoprotein; Heme biosynthesis; Mitochondrion;
KW Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..504
FT /note="Protoporphyrinogen oxidase, mitochondrial"
FT /id="PRO_0000135273"
FT REGION 213..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20..25
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15057273"
FT BINDING 43..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15057273"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15057273"
FT BINDING 65..68
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15057273"
FT BINDING 264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15057273"
FT BINDING 473..475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15057273"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:1SEZ"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 331..342
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 386..395
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 406..421
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 428..440
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 446..459
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:1SEZ"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:1SEZ"
FT HELIX 475..493
FT /evidence="ECO:0007829|PDB:1SEZ"
SQ SEQUENCE 504 AA; 55407 MW; B85B55EC881DC00A CRC64;
MAPSAGEDKH SSAKRVAVIG AGVSGLAAAY KLKIHGLNVT VFEAEGKAGG KLRSVSQDGL
IWDEGANTMT ESEGDVTFLI DSLGLREKQQ FPLSQNKRYI ARNGTPVLLP SNPIDLIKSN
FLSTGSKLQM LLEPILWKNK KLSQVSDSHE SVSGFFQRHF GKEVVDYLID PFVAGTCGGD
PDSLSMHHSF PELWNLEKRF GSVILGAIRS KLSPKNEKKQ GPPKTSANKK RQRGSFSFLG
GMQTLTDAIC KDLREDELRL NSRVLELSCS CTEDSAIDSW SIISASPHKR QSEEESFDAV
IMTAPLCDVK SMKIAKRGNP FLLNFIPEVD YVPLSVVITT FKRENVKYPL EGFGVLVPSK
EQQHGLKTLG TLFSSMMFPD RAPNNVYLYT TFVGGSRNRE LAKASRTELK EIVTSDLKQL
LGAEGEPTYV NHLYWSKAFP LYGHNYDSVL DAIDKMEKNL PGLFYAGNHR GGLSVGKALS
SGCNAADLVI SYLESVSTDS KRHC
