Basic Information

NamePeroxisomal hydratase-dehydrogenase-epimerase (HDE) (Multifunctional beta-oxidation protein) (MFP) [Includes: 2-enoyl-CoA hydratase (EC 4.2.1.119); (3R)-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12)]
Uniprot IDQ02207
Systematic gene nameYKR009C
Standard gene nameFOX2
Gene namesFOX2 YKR009C YK108
Description from SGDYKR009C FOX2 SGDID:S000001717, Chr XI from 457054-454352, Genome Release 64-3-1, reverse complement, Verified ORF, "3-hydroxyacyl-CoA dehydrogenase and enoyl-CoA hydratase; multifunctional enzyme of the peroxisomal fatty acid beta-oxidation pathway; mutation is functionally complemented by human HSD17B4"
Protein length900
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MPGNLSFKDR VVVITGAGGG LGKVYALAYA SRGAKVVVND LGGTLGGSGH
NSKAADLVVD EIKKAGGIAV ANYDSVNENG EKIIETAIKE FGRVDVLINN
AGILRDVSFA KMTEREFASV VDVHLTGGYK LSRAAWPYMR SQKFGRIINT
ASPAGLFGNF GQANYSAAKM GLVGLAETLA KEGAKYNINV NSIAPLARSR
MTENVLPPHI LKQLGPEKIV PLVLYLTHES TKVSNSIFEL AAGFFGQLRW
ERSSGQIFNP DPKTYTPEAI LNKWKEITDY RDKPFNKTQH PYQLSDYNDL
ITKAKKLPPN EQGSVKIKSL CNKVVVVTGA GGGLGKSHAI WFARYGAKVV
VNDIKDPFSV VEEINKLYGE GTAIPDSHDV VTEAPLIIQT AISKFQRVDI
LVNNAGILRD KSFLKMKDEE WFAVLKVHLF STFSLSKAVW PIFTKQKSGF
IINTTSTSGI YGNFGQANYA AAKAAILGFS KTIALEGAKR GIIVNVIAPH
AETAMTKTIF SEKELSNHFD ASQVSPLVVL LASEELQKYS GRRVIGQLFE
VGGGWCGQTR WQRSSGYVSI KETIEPEEIK ENWNHITDFS RNTINPSSTE
ESSMATLQAV QKAHSSKELD DGLFKYTTKD CILYNLGLGC TSKELKYTYE
NDPDFQVLPT FAVIPFMQAT ATLAMDNLVD NFNYAMLLHG EQYFKLCTPT
MPSNGTLKTL AKPLQVLDKN GKAALVVGGF ETYDIKTKKL IAYNEGSFFI
RGAHVPPEKE VRDGKRAKFA VQNFEVPHGK VPDFEAEIST NKDQAALYRL
SGDFNPLHID PTLAKAVKFP TPILHGLCTL GISAKALFEH YGPYEELKVR
FTNVVFPGDT LKVKAWKQGS VVVFQTIDTT RNVIVLDNAA VKLSQAKSKL

Legend

  • 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

[288, 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)
[288, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[297, 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)
[297, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[319, 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)
[319, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)