Basic Information

Name5-aminolevulinate synthase, mitochondrial (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase)
Uniprot IDP09950
Systematic gene nameYDR232W
Standard gene nameHEM1
Gene namesHEM1 CYD1 YDR232W YD9934.16
Description from SGDYDR232W HEM1 SGDID:S000002640, Chr IV from 927452-929098, Genome Release 64-3-1, Verified ORF, "5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p"
Protein length548
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MQRSIFARFG NSSAAVSTLN RLSTTAAPHA KNGYATATGA GAAAATATAS
STHAAAAAAA AANHSTQESG FDYEGLIDSE LQKKRLDKSY RYFNNINRLA
KEFPLAHRQR EADKVTVWCS NDYLALSKHP EVLDAMHKTI DKYGCGAGGT
RNIAGHNIPT LNLEAELATL HKKEGALVFS SCYVANDAVL SLLGQKMKDL
VIFSDELNHA SMIVGIKHAN VKKHIFKHND LNELEQLLQS YPKSVPKLIA
FESVYSMAGS VADIEKICDL ADKYGALTFL DEVHAVGLYG PHGAGVAEHC
DFESHRASGI ATPKTNDKGG AKTVMDRVDM ITGTLGKSFG SVGGYVAASR
KLIDWFRSFA PGFIFTTTLP PSVMAGATAA IRYQRCHIDL RTSQQKHTMY
VKKAFHELGI PVIPNPSHIV PVLIGNADLA KQASDILINK HQIYVQAINF
PTVARGTERL RITPTPGHTN DLSDILINAV DDVFNELQLP RVRDWESQGG
LLGVGESGFV EESNLWTSSQ LSLTNDDLNP NVRDPIVKQL EVSSGIKQ

Legend

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

Structure

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


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References

[23, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[23, 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)
[23, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[24, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[24, 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)
[24, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[25, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[25, 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)
[25, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[142, 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)
[196, 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)
[312, 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)
[402, SUMO]Paasch, F., den Brave, F., Psakhye, I., Pfander, B., Jentsch, S. (2018). Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. J Biol Chem 293: 599-609. (Publication) (All modifications)