Basic Information
| Name | Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) (Transaminase A) |
| Uniprot ID | Q01802 |
| Systematic gene name | YKL106W |
| Standard gene name | AAT1 |
| Gene names | AAT1 YKL106W YKL461 |
| Description from SGD | YKL106W AAT1 SGDID:S000001589, Chr XI from 237536-238891, Genome Release 64-3-1, Verified ORF, "Mitochondrial aspartate aminotransferase; catalyzes the conversion of oxaloacetate to aspartate in aspartate and asparagine biosynthesis" |
| Protein length | 451 |
| Download | sequence (fasta, from Uniprot), modifications (csv format) |
| Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLRTRLTNCS LWRPYYTSSL SRVPRAPPDK VLGLSEHFKK VKNVNKIDLT
VGIYKDGWGK VTTFPSVAKA QKLIESHLEL NKNLSYLPIT GSKEFQENVM
KFLFKESCPQ FGPFYLAHDR ISFVQTLSGT GALAVAAKFL ALFISRDIWI
PDPSWANHKN IFQNNGFENI YRYSYYKDGQ IDIDGWIEQL KTFAYNNQQE
NNKNPPCIIL HACCHNPTGL DPTKEQWEKI IDTIYELKMV PIVDMAYQGL
ESGNLLKDAY LLRLCLNVNK YPNWSNGIFL CQSFAKNMGL YGERVGSLSV
ITPATANNGK FNPLQQKNSL QQNIDSQLKK IVRGMYSSPP GYGSRVVNVV
LSDFKLKQQW FKDVDFMVQR LHHVRQEMFD RLGWPDLVNF AQQHGMFYYT
RFSPKQVEIL RNNYFVYLTG DGRLSLSGVN DSNVDYLCES LEAVSKMDKL
A
VGIYKDGWGK VTTFPSVAKA QKLIESHLEL NKNLSYLPIT GSKEFQENVM
KFLFKESCPQ FGPFYLAHDR ISFVQTLSGT GALAVAAKFL ALFISRDIWI
PDPSWANHKN IFQNNGFENI YRYSYYKDGQ IDIDGWIEQL KTFAYNNQQE
NNKNPPCIIL HACCHNPTGL DPTKEQWEKI IDTIYELKMV PIVDMAYQGL
ESGNLLKDAY LLRLCLNVNK YPNWSNGIFL CQSFAKNMGL YGERVGSLSV
ITPATANNGK FNPLQQKNSL QQNIDSQLKK IVRGMYSSPP GYGSRVVNVV
LSDFKLKQQW FKDVDFMVQR LHHVRQEMFD RLGWPDLVNF AQQHGMFYYT
RFSPKQVEIL RNNYFVYLTG DGRLSLSGVN DSNVDYLCES LEAVSKMDKL
A
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
| [39, 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) |
| [62, 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) |
| [62, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
| [76, 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) |
| [76, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
| [310, 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) |
| [329, 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) |