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P40012 (PPOX_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Short name=PPO
EC=1.3.3.4
Gene names
Name:HEM14
Ordered Locus Names:YER014W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit.

Pathway

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

Subcellular location

Mitochondrion inner membrane. Note: Bound to the mitochondrial inner membrane with its active site facing the cytosolic side. Ref.4

Miscellaneous

Present with 5350 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protoporphyrinogen oxidase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 539539Protoporphyrinogen oxidase
PRO_0000135274

Regions

Nucleotide binding18 – 236FAD By similarity
Nucleotide binding43 – 442FAD By similarity
Nucleotide binding70 – 734FAD By similarity
Nucleotide binding521 – 5233FAD By similarity

Sites

Binding site511FAD; via amide nitrogen By similarity
Binding site3001FAD; via amide nitrogen and carbonyl oxygen By similarity

Experimental info

Mutagenesis4221L → P in HEM14-1; loss of activity.
Mutagenesis4241K → E in HEM14-1; loss of activity.

Sequences

Sequence LengthMass (Da)Tools
P40012 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 5ECCBD1C033BA5B1

FASTA53959,703
        10         20         30         40         50         60 
MLLPLTKLKP RAKVAVVGGG VSGLCFTYFL SKLRPDVEIT LFESQNRTGG WIYSCNTRDM 

        70         80         90        100        110        120 
SGNPIMLEKG PRTLRGVSDG TVLIMDTLKD LGKEAVIQSI DKGCIADKKF LLDPSDKLVQ 

       130        140        150        160        170        180 
VPNSISTTVK FLLNPLGKGL ITGMMGEWFR KKSPHPGQDE SVESICDRRF GNNYISNNMI 

       190        200        210        220        230        240 
SALLRGIYGD DVSLLSAKRT FKKIYYNELK HGSNTQAMID NMRGKSRSKK TENLHQSLTG 

       250        260        270        280        290        300 
CLNDYSNAFG KDRSKLLDLS NTLKKYPMLG LAGGLETFPK IVRNALNEFK NVKIVTGNPV 

       310        320        330        340        350        360 
TQIMKRPANE TTIGLKAKSG DQYETFDHLR LTITPPKIAK LLPKDQNSLS KLLDEIQSNT 

       370        380        390        400        410        420 
IILVNYYLPN KDVIDADLQG FGYLVPKSNK NPGKLLGVIF DSVIERNFKP LFDKLSTNPN 

       430        440        450        460        470        480 
ALNKYTKVTA MIGGCMLNEH GVPVVPSREV TINAVKDALN NHLGISNKDL EAGQWEFTIA 

       490        500        510        520        530 
DRCLPRFHVG YDAWQERAER KLQESYGQTV SVGGMGFSRS PGVPDVIVDG FNDALQLSK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the yeast HEM14 gene coding for protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides."
Camadro J.-M., Labbe P.
J. Biol. Chem. 271:9120-9128(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Purification and properties of protoporphyrinogen oxidase from the yeast Saccharomyces cerevisiae. Mitochondrial location and evidence for a precursor form of the protein."
Camadro J.-M., Thome F., Brouillet N., Labbe P.
J. Biol. Chem. 269:32085-32091(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: ATCC 25657 / D273-10B.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z71381 Genomic DNA. Translation: CAA95981.1.
U18778 Genomic DNA. Translation: AAB64547.1.
BK006939 Genomic DNA. Translation: DAA07665.1.
PIRS50472.
RefSeqNP_010930.1. NM_001178905.1.

3D structure databases

ProteinModelPortalP40012.
SMRP40012. Positions 13-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36746. 32 interactions.
MINTMINT-4483733.
STRING4932.YER014W.

Proteomic databases

MaxQBP40012.
PaxDbP40012.
PeptideAtlasP40012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER014W; YER014W; YER014W.
GeneID856733.
KEGGsce:YER014W.

Organism-specific databases

CYGDYER014w.
SGDS000000816. HEM14.

Phylogenomic databases

eggNOGCOG1232.
GeneTreeENSGT00390000008744.
HOGENOMHOG000093387.
KOK00231.
OMANKITIMM.
OrthoDBEOG7JQBX8.

Enzyme and pathway databases

BioCycYEAST:YER014W-MONOMER.
SABIO-RKP40012.
UniPathwayUPA00251; UER00324.

Gene expression databases

GenevestigatorP40012.

Family and domain databases

Gene3D3.90.660.20. 1 hit.
InterProIPR004572. Protoporphyrinogen_oxidase.
IPR027418. Protoporphyrinogen_oxidase_C.
[Graphical view]
TIGRFAMsTIGR00562. proto_IX_ox. 1 hit.
ProtoNetSearch...

Other

NextBio982849.
PROP40012.

Entry information

Entry namePPOX_YEAST
AccessionPrimary (citable) accession number: P40012
Secondary accession number(s): D3DLR1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways