Basic Information

NameHomocitrate dehydratase, mitochondrial (EC 4.2.1.-) (Aconitase 2)
Uniprot IDP39533
Systematic gene nameYJL200C
Standard gene nameACO2
Gene namesACO2 YJL200C J0327
Description from SGDYJL200C ACO2 SGDID:S000003736, Chr X from 58813-56444, Genome Release 64-3-1, reverse complement, Verified ORF, "Putative mitochondrial aconitase isozyme; similarity to Aco1p, an aconitase required for the TCA cycle; expression induced during growth on glucose, by amino acid starvation via Gcn4p, and repressed on ethanol"
Protein length789
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLSSANRFYI KRHLATHANM FPSVSKNFQT KVPPYAKLLT NLDKIKQITN
NAPLTLAEKI LYSHLCDPEE SITSSDLSTI RGNKYLKLNP DRVAMQDASA
QMALLQFMTT GLNQTSVPAS IHCDHLIVGK DGETKDLPSS IATNQEVFDF
LESCAKRYGI QFWGPGSGII HQIVLENFSA PGLMMLGTDS HTPNAGGLGA
IAIGVGGADA VDALTGTPWE LKAPKILGVK LTGKLNGWST PKDVITKLAG
LLTVRGGTGY IVEYFGEGVS TLSCTGMATI CNMGAEIGAT TSTFPYQEAH
KRYLQATNRA EVAEAADVAL NKFNFLRADK DAQYDKVIEI DLSAIEPHVN
GPFTPDLSTP ISQYAEKSLK ENWPQKVSAG LIGSCTNSSY QDMSRVVDLV
KQASKAGLKP RIPFFVTPGS EQIRATLERD GIIDIFQENG AKVLANACGP
CIGQWNREDV SKTSKETNTI FTSFNRNFRA RNDGNRNTMN FLTSPEIVTA
MSYSGDAQFN PLTDSIKLPN GKDFKFQPPK GDELPKRGFE HGRDKFYPEM
DPKPDSNVEI KVDPNSDRLQ LLEPFKPWNG KELKTNVLLK VEGKCTTDHI
SAAGVWLKYK GHLENISYNT LIGAQNKETG EVNKAYDLDG TEYDIPGLMM
KWKSDGRPWT VIAEHNYGEG SAREHAALSP RFLGGEILLV KSFARIHETN
LKKQGVLPLT FANESDYDKI SSGDVLETLN LVDMIAKDGN NGGEIDVKIT
KPNGESFTIK AKHTMSKDQI DFFKAGSAIN YIGNIRRNE

Legend

  • X K-Succinylation
  • X Phoshorylation
  • X K-acetylation

Structure

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


Use imported representation

Loading structure from server... It may take a while.

If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.

References

[44, 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)
[239, 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)
[354, 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)
[388, 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)
[388, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[401, 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)
[462, 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)
[590, 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)
[594, 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)
[610, 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)
[699, Phos]Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications)
[699, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[710, 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)
[710, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[715, 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)
[715, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)