Basic Information

NameArginine biosynthesis bifunctional protein ArgJ, mitochondrial (Extracellular mutant protein 40) [Cleaved into: Arginine biosynthesis bifunctional protein ArgJ alpha chain; Arginine biosynthesis bifunctional protein ArgJ beta chain] [Includes: Glutamate N-acetyltransferase (GAT) (EC 2.3.1.35) (Ornithine acetyltransferase) (OATase) (Ornithine transacetylase); Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS)]
Uniprot IDQ04728
Systematic gene nameYMR062C
Standard gene nameARG7
Gene namesARG7 ECM40 YMR062C YM9916.01C
Description from SGDYMR062C ARG7 SGDID:S000004666, Chr XIII from 396379-395054, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial ornithine acetyltransferase; catalyzes the fifth step in arginine biosynthesis; also possesses acetylglutamate synthase activity, regenerates acetylglutamate while forming ornithine"
Protein length441
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MRISSTLLQR SKQLIDKYAL YVPKTGSFPK GFEVGYTASG VKKNGSLDLG
VILNTNKSRP STAAAVFTTN KFKAAPVLTS KKVLETARGK NINAIVVNSG
CANSVTGDLG MKDAQVMIDL VNDKIGQKNS TLVMSTGVIG QRLQMDKIST
GINKIFGEEK FGSDFNSWLN VAKSICTTDT FPKLVTSRFK LPSGTEYTLT
GMAKGAGMIC PNMATLLGFI VTDLPIESKA LQKMLTFATT RSFNCISVDG
DMSTNDTICM LANGAIDTKE INEDSKDFEQ VKLQVTEFAQ RLAQLVVRDG
EGSTKFVTVN VKNALHFEDA KIIAESISNS MLVKTALYGQ DANWGRILCA
IGYAKLNDLK SLDVNKINVS FIATDNSEPR ELKLVANGVP QLEIDETRAS
EILALNDLEV SVDLGTGDQA AQFWTCDLSH EYVTINGDYR S

Legend

  • X Phoshorylation
  • X K-acetylation
  • X Multiple modifications
  • 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

[5, 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)
[5, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[24, 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)
[46, 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)
[46, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[154, 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)
[154, 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)
[174, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[276, K-succ]Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications)
[276, 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)
[360, K-succ]Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications)
[360, 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)