Basic Information

Name3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC 3.1.2.4) (3-hydroxyisobutyryl-coenzyme A hydrolase) (HIB-CoA hydrolase) (HIBYL-CoA-H) (Mitochondrial small ribosomal subunit protein mS47)
Uniprot IDP28817
Systematic gene nameYDR036C
Standard gene nameEHD3
Gene namesEHD3 MRP5 YDR036C YD9673.08C
Description from SGDYDR036C EHD3 SGDID:S000002443, Chr IV from 524713-523211, Genome Release 64-3-1, reverse complement, Verified ORF, "3-hydroxyisobutyryl-CoA hydrolase; member of a family of enoyl-CoA hydratase/isomerases; non-tagged protein is detected in highly purified mitochondria in high-throughput studies; phosphorylated; mutation affects fluid-phase endocytosis"
Protein length500
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLRNTLKCAQ LSSKYGFKTT TRTFMTTQPQ LNVTDAPPVL FTVQDTARVI
TLNRPKKLNA LNAEMSESMF KTLNEYAKSD TTNLVILKSS NRPRSFCAGG
DVATVAIFNF NKEFAKSIKF FTDEYSLNFQ IATYLKPIVT FMDGITMGGG
VGLSIHTPFR IATENTKWAM PEMDIGFFPD VGSTFALPRI VTLANSNSQM
ALYLCLTGEV VTGADAYMLG LASHYVSSEN LDALQKRLGE ISPPFNNDPQ
SAYFFGMVNE SIDEFVSPLP KDYVFKYSNE KLNVIEACFN LSKNGTIEDI
MNNLRQYEGS AEGKAFAQEI KTKLLTKSPS SLQIALRLVQ ENSRDHIESA
IKRDLYTAAN MCMNQDSLVE FSEATKHKLI DKQRVPYPWT KKEQLFVSQL
TSITSPKPSL PMSLLRNTSN VTWTQYPYHS KYQLPTEQEI AAYIEKRTND
DTGAKVTERE VLNHFANVIP SRRGKLGIQS LCKIVCERKC EEVNDGLRWK

Legend

  • X Phoshorylation
  • X K-Succinylation

Structure

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


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References

[34, Phos]Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications)
[34, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[56, 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)
[57, 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)
[78, 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)
[88, 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)
[321, 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)
[326, Phos]Reinders J, Wagner K, Zahedit RP, et al (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Molecular and Cellular Proteomics 6:1896–1906. (Publication) (All modifications)
[326, 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)
[326, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[328, Phos]Reinders J, Wagner K, Zahedit RP, et al (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Molecular and Cellular Proteomics 6:1896–1906. (Publication) (All modifications)
[328, 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)
[328, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[378, 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)
[457, Phos]Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications)
[457, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)