Basic Information
Name | S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) (Alcohol dehydrogenase SFA) (EC 1.1.1.1) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (FLD) (GSH-FDH) (EC 1.1.1.-) |
Uniprot ID | P32771 |
Systematic gene name | YDL168W |
Standard gene name | SFA1 |
Gene names | SFA1 SFA YDL168W |
Description from SGD | YDL168W SFA1 SGDID:S000002327, Chr IV from 159604-160764, Genome Release 64-3-1, Verified ORF, "Bifunctional alcohol dehydrogenase and formaldehyde dehydrogenase; formaldehyde dehydrogenase activity is glutathione-dependent; functions in formaldehyde detoxification and formation of long chain and complex alcohols, regulated by Hog1p-Sko1p; protein abundance increases in response to DNA replication stress" |
Protein length | 386 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSAATVGKPI KCIAAVAYDA KKPLSVEEIT VDAPKAHEVR IKIEYTAVCH
TDAYTLSGSD PEGLFPCVLG HEGAGIVESV GDDVITVKPG DHVIALYTAE
CGKCKFCTSG KTNLCGAVRA TQGKGVMPDG TTRFHNAKGE DIYHFMGCST
FSEYTVVADV SVVAIDPKAP LDAACLLGCG VTTGFGAALK TANVQKGDTV
AVFGCGTVGL SVIQGAKLRG ASKIIAIDIN NKKKQYCSQF GATDFVNPKE
DLAKDQTIVE KLIEMTDGGL DFTFDCTGNT KIMRDALEAC HKGWGQSIII
GVAAAGEEIS TRPFQLVTGR VWKGSAFGGI KGRSEMGGLI KDYQKGALKV
EEFITHRRPF KEINQAFEDL HNGDCLRTVL KSDEIK
TDAYTLSGSD PEGLFPCVLG HEGAGIVESV GDDVITVKPG DHVIALYTAE
CGKCKFCTSG KTNLCGAVRA TQGKGVMPDG TTRFHNAKGE DIYHFMGCST
FSEYTVVADV SVVAIDPKAP LDAACLLGCG VTTGFGAALK TANVQKGDTV
AVFGCGTVGL SVIQGAKLRG ASKIIAIDIN NKKKQYCSQF GATDFVNPKE
DLAKDQTIVE KLIEMTDGGL DFTFDCTGNT KIMRDALEAC HKGWGQSIII
GVAAAGEEIS TRPFQLVTGR VWKGSAFGGI KGRSEMGGLI KDYQKGALKV
EEFITHRRPF KEINQAFEDL HNGDCLRTVL KSDEIK
Legend
- X Phoshorylation
- X SUMOylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[2, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[42, SUMO] | Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications) |
[124, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[382, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |