Basic Information

NameProtoporphyrinogen oxidase (PPO) (EC 1.3.3.4)
Uniprot IDP40012
Systematic gene nameYER014W
Standard gene nameHEM14
Gene namesHEM14 YER014W
Description from SGDYER014W HEM14 SGDID:S000000816, Chr V from 182600-184219, Genome Release 64-3-1, Verified ORF, "Protoporphyrinogen oxidase; a mitochondrial enzyme that catalyzes the seventh step in the heme biosynthetic pathway, converting protoporphyrinogen IX to protoporphyrin IX; inhibited by diphenyl ether-type herbicides"
Protein length539
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLLPLTKLKP RAKVAVVGGG VSGLCFTYFL SKLRPDVEIT LFESQNRTGG
WIYSCNTRDM SGNPIMLEKG PRTLRGVSDG TVLIMDTLKD LGKEAVIQSI
DKGCIADKKF LLDPSDKLVQ VPNSISTTVK FLLNPLGKGL ITGMMGEWFR
KKSPHPGQDE SVESICDRRF GNNYISNNMI SALLRGIYGD DVSLLSAKRT
FKKIYYNELK HGSNTQAMID NMRGKSRSKK TENLHQSLTG CLNDYSNAFG
KDRSKLLDLS NTLKKYPMLG LAGGLETFPK IVRNALNEFK NVKIVTGNPV
TQIMKRPANE TTIGLKAKSG DQYETFDHLR LTITPPKIAK LLPKDQNSLS
KLLDEIQSNT IILVNYYLPN KDVIDADLQG FGYLVPKSNK NPGKLLGVIF
DSVIERNFKP LFDKLSTNPN ALNKYTKVTA MIGGCMLNEH GVPVVPSREV
TINAVKDALN NHLGISNKDL EAGQWEFTIA DRCLPRFHVG YDAWQERAER
KLQESYGQTV SVGGMGFSRS PGVPDVIVDG FNDALQLSK

Legend

  • X K-acetylation
  • X K-benzoylation
  • X K-Succinylation
  • X SUMOylation
  • X Multiple modifications
  • X Phoshorylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


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References

[69, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[89, K-bz]Wang, D., Yan, F., Wu, P., Ge, K., Li, M., Li, T., Gao, Y., Peng, C., Chen, Y. (2022). Global profiling of regulatory elements in the histone benzoylation pathway. Nature Communications 13(1):1369 (Publication) (All modifications)
[109, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)
[130, SUMO]Paasch, F., den Brave, F., Psakhye, I., Pfander, B., Jentsch, S. (2018). Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. J Biol Chem 293: 599-609. (Publication) (All modifications)
[203, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)
[210, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)
[210, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[266, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[266, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[266, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[277, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[277, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[277, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[318, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)
[340, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)