Basic Information
| Name | NAD-dependent malic enzyme, mitochondrial (NAD-ME) (EC 1.1.1.38) |
| Uniprot ID | P36013 |
| Systematic gene name | YKL029C |
| Standard gene name | MAE1 |
| Gene names | MAE1 YKL029C |
| Description from SGD | YKL029C MAE1 SGDID:S000001512, Chr XI from 384725-382716, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial malic enzyme; catalyzes the oxidative decarboxylation of malate to pyruvate, which is a key intermediate in sugar metabolism and a precursor for synthesis of several amino acids" |
| Protein length | 669 |
| Download | sequence (fasta, from Uniprot), modifications (csv format) |
| Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLRTRLSVSV AARSQLTRSL TASRTAPLRR WPIQQSRLYS SNTRSHKATT
TRENTFQKPY SDEEVTKTPV GSRARKIFEA PHPHATRLTV EGAIECPLES
FQLLNSPLFN KGSAFTQEER EAFNLEALLP PQVNTLDEQL ERSYKQLCYL
KTPLAKNDFM TSLRVQNKVL YFALIRRHIK ELVPIIYTPT EGDAIAAYSH
RFRKPEGVFL DITEPDSIEC RLATYGGDKD VDYIVVSDSE GILGIGDQGI
GGVRIAISKL ALMTLCGGIH PGRVLPVCLD VGTNNKKLAR DELYMGNKFS
RIRGKQYDDF LEKFIKAVKK VYPSAVLHFE DFGVKNARRL LEKYRYELPS
FNDDIQGTGA VVMASLIAAL KHTNRDLKDT RVLIYGAGSA GLGIADQIVN
HMVTHGVDKE EARKKIFLMD RRGLILQSYE ANSTPAQHVY AKSDAEWAGI
NTRSLHDVVE NVKPTCLVGC STQAGAFTQD VVEEMHKHNP RPIIFPLSNP
TRLHEAVPAD LMKWTNNNAL VATGSPFPPV DGYRISENNN CYSFPGIGLG
AVLSRATTIT DKMISAAVDQ LAELSPLREG DSRPGLLPGL DTITNTSARL
ATAVILQALE EGTARIEQEQ VPGGAPGETV KVPRDFDECL QWVKAQMWEP
VYRPMIKVQH DPSVHTNQL
TRENTFQKPY SDEEVTKTPV GSRARKIFEA PHPHATRLTV EGAIECPLES
FQLLNSPLFN KGSAFTQEER EAFNLEALLP PQVNTLDEQL ERSYKQLCYL
KTPLAKNDFM TSLRVQNKVL YFALIRRHIK ELVPIIYTPT EGDAIAAYSH
RFRKPEGVFL DITEPDSIEC RLATYGGDKD VDYIVVSDSE GILGIGDQGI
GGVRIAISKL ALMTLCGGIH PGRVLPVCLD VGTNNKKLAR DELYMGNKFS
RIRGKQYDDF LEKFIKAVKK VYPSAVLHFE DFGVKNARRL LEKYRYELPS
FNDDIQGTGA VVMASLIAAL KHTNRDLKDT RVLIYGAGSA GLGIADQIVN
HMVTHGVDKE EARKKIFLMD RRGLILQSYE ANSTPAQHVY AKSDAEWAGI
NTRSLHDVVE NVKPTCLVGC STQAGAFTQD VVEEMHKHNP RPIIFPLSNP
TRLHEAVPAD LMKWTNNNAL VATGSPFPPV DGYRISENNN CYSFPGIGLG
AVLSRATTIT DKMISAAVDQ LAELSPLREG DSRPGLLPGL DTITNTSARL
ATAVILQALE EGTARIEQEQ VPGGAPGETV KVPRDFDECL QWVKAQMWEP
VYRPMIKVQH DPSVHTNQL
Legend
- X K-acetylation
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
| [58, 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) |
| [151, 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) |
| [300, 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) |
| [335, 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) |