| Identification |
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| Name: | Aspartate-semialdehyde dehydrogenase |
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| Synonyms: | |
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| Gene Name: | asd |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in aspartate-semialdehyde dehydrogenase activity |
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| Specific Function: | L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | - Lysine biosynthesis PW000771
- Secondary Metabolites: threonine biosynthesis from aspartate PW000976
- threonine biosynthesis PW000817
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| KEGG Pathways: | - Cysteine and methionine metabolism ec00270
- Glycine, serine and threonine metabolism ec00260
- Lysine biosynthesis ec00300
- Metabolic pathways eco01100
- Microbial metabolism in diverse environments ec01120
- Monobactam biosynthesis eco00261
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| KEGG Reactions: | |
1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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| SMPDB Reactions: | |
1.0 | + | 1.0NADPH | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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| Metabolites: | |
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| GO Classification: | | Component |
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| cell part | | cytoplasm | | intracellular part | | Function |
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| aspartate-semialdehyde dehydrogenase activity | | binding | | catalytic activity | | NAD or NADH binding | | NADP or NADPH binding | | nucleotide binding | | oxidoreductase activity | | oxidoreductase activity, acting on the aldehyde or oxo group of donors | | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor | | protein binding | | protein dimerization activity | | Process |
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| aspartate family amino acid metabolic process | | cellular amino acid and derivative metabolic process | | cellular amino acid biosynthetic process | | cellular amino acid metabolic process | | cellular metabolic process | | lysine biosynthetic process | | lysine biosynthetic process via diaminopimelate | | lysine metabolic process | | metabolic process | | oxidation reduction |
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| Gene Properties |
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| Blattner: | b3433 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 76.98 |
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| Left Sequence End | 3571798 |
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| Right Sequence End | 3572901 |
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| Gene Sequence: | >1104 bp
ATGAGTGACAGCCAGACGCTGGTGGTAAAACTCGGCACCAGTGTGCTAACAGGCGGATCG
CGCCGTCTGAACCGTGCCCATATCGTTGAACTTGTTCGCCAGTGCGCGCAGTTACATGCC
GCCGGGCATCGGATTGTTATTGTGACGTCGGGCGCGATCGCCGCCGGACGTGAGCACCTG
GGTTACCCGGAACTGCCAGCGACCATCGCCTCGAAACAACTGCTGGCGGCGGTAGGGCAG
AGTCGACTGATTCAACTGTGGGAACAGCTGTTTTCGATTTATGGCATTCACGTCGGGCAA
ATGCTGCTGACCCGTGCTGATATGGAAGACCGTGAACGCTTCCTGAACGCCCGCGACACC
CTGCGAGCGTTGCTCGATAACAATATCGTTCCGGTAATCAATGAGAACGATGCTGTCGCT
ACGGCAGAGATTAAGGTCGGCGATAACGATAACCTTTCTGCGCTGGCGGCGATTCTTGCG
GGTGCCGATAAACTGTTGCTGCTGACCGATCAAAAAGGTTTGTATACCGCTGACCCGCGC
AGCAATCCGCAGGCAGAACTGATTAAAGATGTTTACGGCATTGATGACGCACTGCGCGCG
ATTGCCGGTGACAGCGTTTCAGGCCTCGGAACTGGCGGCATGAGTACCAAATTGCAGGCC
GCTGACGTGGCTTGCCGTGCGGGTATCGACACCATTATTGCCGCGGGCAGCAAGCCGGGC
GTTATTGGTGATGTGATGGAAGGCATTTCCGTCGGTACGCTGTTCCATGCCCAGGCGACT
CCGCTTGAAAACCGTAAACGCTGGATTTTCGGTGCGCCGCCGGCGGGTGAAATCACGGTA
GATGAAGGGGCAACTGCCGCCATTCTGGAACGCGGCAGCTCCCTGTTGCCGAAAGGCATT
AAAAGCGTGACTGGCAATTTCTCGCGTGGTGAAGTCATCCGCATTTGCAACCTCGAAGGC
CGCGATATCGCCCACGGCGTCAGTCGTTACAACAGCGATGCATTACGCCGTATTGCCGGA
CACCACTCGCAAGAAATTGATGCAATACTGGGATATGAATACGGCCCGGTTGCCGTTCAC
CGTGATGACATGATTACCCGTTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 367 |
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| Protein Molecular Weight: | 40018 |
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| Protein Theoretical pI: | 5 |
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| PDB File: | 1GL3 |
| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Aspartate-semialdehyde dehydrogenase
MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDL
EALKALDIIVTCQGGDYTNEIYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVIT
DGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMG
HLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSR
EEWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNP
WAKVVPNDREITMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLR
RMLRQLA |
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| References |
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| External Links: | |
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| General Reference: | - Alvarez, E., Ramon, F., Magan, C., Diez, E. (2004). "L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme." Biochim Biophys Acta 1696:23-29. Pubmed: 14726201
- Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hadfield, A., Kryger, G., Ouyang, J., Petsko, G. A., Ringe, D., Viola, R. (1999). "Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis." J Mol Biol 289:991-1002. Pubmed: 10369777
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Haziza, C., Stragier, P., Patte, J. C. (1982). "Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal." EMBO J 1:379-384. Pubmed: 6143662
- Karsten, W. E., Viola, R. E. (1992). "Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli." Biochim Biophys Acta 1121:234-238. Pubmed: 1350921
- Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
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