Aspartate-semialdehyde dehydrogenase (P0A9Q9)

Identification
Name:Aspartate-semialdehyde dehydrogenase
Synonyms:
  • ASA dehydrogenase
  • ASADH
Gene Name:asd
Enzyme Class:
Biological Properties
General Function:Involved in aspartate-semialdehyde dehydrogenase activity
Specific Function:L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartate-semialdehyde + 1.0NADP + 1.0Phosphate ↔ 1.0L-Aspartyl-4-phosphate + 1.0Hydrogen ion + 1.0NADPH
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0NADPH+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartyl-4-phosphate + 1.0NADPH + 1.0Hydrogen ion + 1.0NADPH → 1.0Phosphate + 1.0NADP + 1.0L-Aspartate-semialdehyde
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartate-semialdehyde + 1.0NADP + 1.0Phosphate ↔ 1.0L-Aspartyl-4-phosphate + 1.0Hydrogen ion + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB12249L-Aspartate-semialdehydeMetaboCard
ECMDB12250L-Aspartyl-4-phosphateMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
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
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
Gene Properties
Blattner:b3433
Gene OrientationCounterclockwise
Centisome Percentage:76.98
Left Sequence End3571798
Right Sequence End3572901
Gene Sequence:
>1104 bp
ATGAGTGACAGCCAGACGCTGGTGGTAAAACTCGGCACCAGTGTGCTAACAGGCGGATCG
CGCCGTCTGAACCGTGCCCATATCGTTGAACTTGTTCGCCAGTGCGCGCAGTTACATGCC
GCCGGGCATCGGATTGTTATTGTGACGTCGGGCGCGATCGCCGCCGGACGTGAGCACCTG
GGTTACCCGGAACTGCCAGCGACCATCGCCTCGAAACAACTGCTGGCGGCGGTAGGGCAG
AGTCGACTGATTCAACTGTGGGAACAGCTGTTTTCGATTTATGGCATTCACGTCGGGCAA
ATGCTGCTGACCCGTGCTGATATGGAAGACCGTGAACGCTTCCTGAACGCCCGCGACACC
CTGCGAGCGTTGCTCGATAACAATATCGTTCCGGTAATCAATGAGAACGATGCTGTCGCT
ACGGCAGAGATTAAGGTCGGCGATAACGATAACCTTTCTGCGCTGGCGGCGATTCTTGCG
GGTGCCGATAAACTGTTGCTGCTGACCGATCAAAAAGGTTTGTATACCGCTGACCCGCGC
AGCAATCCGCAGGCAGAACTGATTAAAGATGTTTACGGCATTGATGACGCACTGCGCGCG
ATTGCCGGTGACAGCGTTTCAGGCCTCGGAACTGGCGGCATGAGTACCAAATTGCAGGCC
GCTGACGTGGCTTGCCGTGCGGGTATCGACACCATTATTGCCGCGGGCAGCAAGCCGGGC
GTTATTGGTGATGTGATGGAAGGCATTTCCGTCGGTACGCTGTTCCATGCCCAGGCGACT
CCGCTTGAAAACCGTAAACGCTGGATTTTCGGTGCGCCGCCGGCGGGTGAAATCACGGTA
GATGAAGGGGCAACTGCCGCCATTCTGGAACGCGGCAGCTCCCTGTTGCCGAAAGGCATT
AAAAGCGTGACTGGCAATTTCTCGCGTGGTGAAGTCATCCGCATTTGCAACCTCGAAGGC
CGCGATATCGCCCACGGCGTCAGTCGTTACAACAGCGATGCATTACGCCGTATTGCCGGA
CACCACTCGCAAGAAATTGATGCAATACTGGGATATGAATACGGCCCGGTTGCCGTTCAC
CGTGATGACATGATTACCCGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:367
Protein Molecular Weight:40018
Protein Theoretical pI:5
PDB File:1GL3
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aspartate-semialdehyde dehydrogenase
MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDL
EALKALDIIVTCQGGDYTNEIYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVIT
DGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMG
HLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSR
EEWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNP
WAKVVPNDREITMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLR
RMLRQLA
References
External Links:
ResourceLink
Uniprot ID:P0A9Q9
Uniprot Name:DHAS_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674394
PDB ID:1GL3
Ecogene ID:EG10088
Ecocyc:EG10088
ColiBase:b3433
Kegg Gene:b3433
EchoBASE ID:EB0086
CCDB:DHAS_ECOLI
BacMap:16131307
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