Basic Information

NameHomoaconitase, mitochondrial (EC 4.2.1.36) (Homoaconitate hydratase)
Uniprot IDP49367
Systematic gene nameYDR234W
Standard gene nameLYS4
Gene namesLYS4 LYS3 YDR234W YD8419.01 YD9934.18
Description from SGDYDR234W LYS4 SGDID:S000002642, Chr IV from 931129-933210, Genome Release 64-3-1, Verified ORF, "Homoaconitase; catalyzes the conversion of homocitrate to homoisocitrate, which is a step in the lysine biosynthesis pathway"
Protein length693
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLRSTTFTRS FHSSRAWLKG QNLTEKIVQS YAVNLPEGKV VHSGDYVSIK
PAHCMSHDNS WPVALKFMGL GATKIKNPSQ IVTTLDHDIQ NKSEKNLTKY
KNIENFAKKH HIDHYPAGRG IGHQIMIEEG YAFPLNMTVA SDSHSNTYGG
LGSLGTPIVR TDAAAIWATG QTWWQIPPVA QVELKGQLPQ GVSGKDIIVA
LCGLFNNDQV LNHAIEFTGD SLNALPIDHR LTIANMTTEW GALSGLFPVD
KTLIDWYKNR LQKLGTNNHP RINPKTIRAL EEKAKIPKAD KDAHYAKKLI
IDLATLTHYV SGPNSVKVSN TVQDLSQQDI KINKAYLVSC TNSRLSDLQS
AADVVCPTGD LNKVNKVAPG VEFYVAAASS EIEADARKSG AWEKLLKAGC
IPLPSGCGPC IGLGAGLLEP GEVGISATNR NFKGRMGSKD ALAYLASPAV
VAASAVLGKI SSPAEVLSTS EIPFSGVKTE IIENPVVEEE VNAQTEAPKQ
SVEILEGFPR EFSGELVLCD ADNINTDGIY PGKYTYQDDV PKEKMAQVCM
ENYDAEFRTK VHPGDIVVSG FNFGTGSSRE QAATALLAKG INLVVSGSFG
NIFSRNSINN ALLTLEIPAL IKKLREKYQG APKELTRRTG WFLKWDVADA
KVVVTEGSLD GPVILEQKVG ELGKNLQEII VKGGLEGWVK SQL

Legend

  • X K-acetylation
  • 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

[76, 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)
[79, 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)
[95, 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)
[101, 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)
[108, 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)
[258, 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)
[275, 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, 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)
[321, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[674, 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)