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O24164 (PPOM_TOBAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protoporphyrinogen oxidase, mitochondrial

EC=1.3.3.4
Alternative name(s):
PX-2
Protoporphyrinogen IX oxidase isozyme II
Short name=PPO II
Short name=PPX II
Gene names
Name:PPXII
Synonyms:PPOX2
OrganismNicotiana tabacum (Common tobacco)
Taxonomic identifier4097 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Ref.1

Provides precursor for the mitochondrial and plastidic heme synthesis and the predominant chlorophyll synthesis in plastids. Ref.1

Catalytic activity

Protoporphyrinogen-IX + 3 O2 = protoporphyrin-IX + 3 H2O2.

Cofactor

Binds 1 FAD per subunit. Ref.4

Enzyme regulation

Inhibited by the herbicide acifluorfen.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.

Subcellular location

Mitochondrion Ref.1.

Developmental stage

Expressed in expanding premature leaves. Decreased expression in oldest leaves. Also detected in roots. Ref.1

Induction

Oscillating expression during diurnal growth. Maximal expression in the dark period. Ref.1

Sequence similarities

Belongs to the protoporphyrinogen oxidase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Cellular componentMitochondrion
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoxygen-dependent protoporphyrinogen oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504Protoporphyrinogen oxidase, mitochondrial
PRO_0000135273

Regions

Nucleotide binding20 – 256FAD
Nucleotide binding43 – 442FAD
Nucleotide binding65 – 684FAD
Nucleotide binding473 – 4753FAD

Sites

Binding site511FAD
Binding site2641FAD; via amide nitrogen and carbonyl oxygen

Secondary structure

......................................................................................... 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O24164 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B85B55EC881DC00A

FASTA50455,407
        10         20         30         40         50         60 
MAPSAGEDKH SSAKRVAVIG AGVSGLAAAY KLKIHGLNVT VFEAEGKAGG KLRSVSQDGL 

        70         80         90        100        110        120 
IWDEGANTMT ESEGDVTFLI DSLGLREKQQ FPLSQNKRYI ARNGTPVLLP SNPIDLIKSN 

       130        140        150        160        170        180 
FLSTGSKLQM LLEPILWKNK KLSQVSDSHE SVSGFFQRHF GKEVVDYLID PFVAGTCGGD 

       190        200        210        220        230        240 
PDSLSMHHSF PELWNLEKRF GSVILGAIRS KLSPKNEKKQ GPPKTSANKK RQRGSFSFLG 

       250        260        270        280        290        300 
GMQTLTDAIC KDLREDELRL NSRVLELSCS CTEDSAIDSW SIISASPHKR QSEEESFDAV 

       310        320        330        340        350        360 
IMTAPLCDVK SMKIAKRGNP FLLNFIPEVD YVPLSVVITT FKRENVKYPL EGFGVLVPSK 

       370        380        390        400        410        420 
EQQHGLKTLG TLFSSMMFPD RAPNNVYLYT TFVGGSRNRE LAKASRTELK EIVTSDLKQL 

       430        440        450        460        470        480 
LGAEGEPTYV NHLYWSKAFP LYGHNYDSVL DAIDKMEKNL PGLFYAGNHR GGLSVGKALS 

       490        500 
SGCNAADLVI SYLESVSTDS KRHC 

« Hide

References

[1]"Cloning and characterization of a plastidal and a mitochondrial isoform of tobacco protoporphyrinogen IX oxidase."
Lermontova I., Kruse E., Mock H.-P., Grimm B.
Proc. Natl. Acad. Sci. U.S.A. 94:8895-8900(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, SUBCELLULAR LOCATION.
Strain: cv. SR1.
[2]"Molecular characterization of photomixotrophic cultured tobacco cells resistant to protoporphyrinogen oxidase-inhibiting herbicides."
Watanabe N., Che F., Iwano M., Takayama S., Nakano T., Yoshida S., Isogai A.
Plant Physiol. 118:751-758(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Samsun NN.
[3]"The molecular basis of photobleaching herbicide resistance in Tobacco."
Horikoshi M., Mametsuka K., Hirooka T.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. SR1.
[4]"Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis."
Koch M., Breithaupt C., Kiefersauer R., Freigang J., Huber R., Messerschmidt A.
EMBO J. 23:1720-1728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR AND FAD, IDENTIFICATION BY MASS SPECTROMETRY, COFACTOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13466 mRNA. Translation: CAA73866.1.
AB020500 mRNA. Translation: BAA34712.1.
AF044129 mRNA. Translation: AAD02291.1.
PIRT04076.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SEZX-ray2.90A/B1-504[»]
ProteinModelPortalO24164.
SMRO24164. Positions 13-497.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBO24164.
ChEMBLCHEMBL1926489.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11759.
UniPathwayUPA00251; UER00324.

Family and domain databases

Gene3D3.90.660.20. 1 hit.
InterProIPR002937. Amino_oxidase.
IPR004572. Protoporphyrinogen_oxidase.
IPR027418. Protoporphyrinogen_oxidase_C.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00562. proto_IX_ox. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO24164.

Entry information

Entry namePPOM_TOBAC
AccessionPrimary (citable) accession number: O24164
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways