Basic Information

NameD-2-hydroxyglutarate--pyruvate transhydrogenase DLD2 (D-2HG--pyruvate transhydrogenase DLD2) (EC 1.1.99.40) (Actin-interacting protein 2) (D-lactate dehydrogenase [cytochrome] 2, mitochondrial) (EC 1.1.2.4) (D-lactate ferricytochrome C oxidoreductase) (D-LCR)
Uniprot IDP46681
Systematic gene nameYDL178W
Standard gene nameDLD2
Gene namesDLD2 AIP2 YDL178W
Description from SGDYDL178W DLD2 SGDID:S000002337, Chr IV from 139522-141114, Genome Release 64-3-1, Verified ORF, "D-2-hydroxyglutarate dehydrogenase, and minor D-lactate dehydrogenase; mitochondrial matrix protein that oxidizes D-2-hydroxyglutarate (D-2HG), an oncometabolite, to alpha-ketoglutarate with a minor role in lactate catabolism; located in the mitochondrial matrix"
Protein length530
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLRNILVRST GSNFKFAGRY MKSSALLGYY RRVNYYSTKI QTRLTSENYP
DVHRDPRFKK LTSDDLNYFK SILSEQEILR ASESEDLSFY NEDWMRKYKG
QSKLVLRPKS VEKVSLILNY CNDEKIAVVP QGGNTGLVGG SVPIFDELIL
SLANLNKIRD FDPVSGILKC DAGVILENAN NYVMEQNYMF PLDLGAKGSC
HVGGVVATNA GGLRLLRYGS LHGSVLGLEV VMPNGQIVNS MHSMRKDNTG
YDLKQLFIGS EGTIGIITGV SILTVPKPKA FNVSYLSVES FEDVQKVFVR
ARQELSEILS AFEFMDAKSQ VLAKSQLKDA AFPLEDEHPF YILIETSGSN
KDHDDSKLET FLENVMEEGI VTDGVVAQDE TELQNLWKWR EMIPEASQAN
GGVYKYDVSL PLKDLYSLVE ATNARLSEAE LVGDSPKPVV GAIGYGHVGD
GNLHLNVAVR EYNKNIEKTL EPFVYEFVSS KHGSVSAEHG LGFQKKNYIG
YSKSPEEVKM MKDLKVHYDP NGILNPYKYI

Legend

  • X K-Succinylation
  • 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

[60, 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)
[74, 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)
[74, 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)
[74, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (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)
[268, 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)
[271, 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)
[274, 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)
[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)