Aspartate-semialdehyde dehydrogenase
Details
- Name
- Aspartate-semialdehyde dehydrogenase
- Synonyms
- 1.2.1.11
- ASA dehydrogenase
- Aspartate-beta-semialdehyde dehydrogenase
- Gene Name
- asd
- Organism
- Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
- Amino acid sequence
>lcl|BSEQ0011199|Aspartate-semialdehyde dehydrogenase MKNVGFIGWRGMVGSVLMDRMSQENDFENLNPVFFTTSQAGQKAPVFGGKDAGDLKSAFD IEELKKLDIIVTCQGGDYTNEVYPKLKATGWDGYWVDAASALRMKDDAIIVLDPVNQHVI SEGLKKGIKTFVGGNCTVSLMLMAIGGLFEKDLVEWISVATYQAASGAGAKNMRELLSQM GLLEQAVSSELKDPASSILDIERKVTAKMRADNFPTDNFGAALGGSLIPWIDKLLPETGQ TKEEWKGYAETNKILGLSDNPIPVDGLCVRIGALRCHSQAFTIKLKKDLPLEEIEQIIAS HNEWVKVIPNDKEITLRELTPAKVTGTLSVPVGRLRKLAMGPEYLAAFTVGDQLLWGAAE PVRRILKQLVA
- Number of residues
- 371
- Molecular Weight
- 40538.52
- Theoretical pI
- 5.33
- GO Classification
- Functionsaspartate-semialdehyde dehydrogenase activity / N-acetyl-gamma-glutamyl-phosphate reductase activity / NAD binding / NADP bindingProcesses'de novo' L-methionine biosynthetic process / diaminopimelate biosynthetic process / isoleucine biosynthetic process / lysine biosynthetic process via diaminopimelate / threonine biosynthetic processComponentscytoplasm
- General Function
- Nadp binding
- Specific Function
- Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011200|Aspartate-semialdehyde dehydrogenase (asd) ATGAAAAATGTAGGCTTTATCGGCTGGCGCGGAATGGTGGGTTCCGTATTAATGGATCGT ATGTCGCAGGAAAATGATTTTGAAAATCTTAATCCCGTATTTTTTACAACTTCACAAGCA GGTCAAAAAGCACCTGTTTTTGGTGGCAAGGATGCAGGCGACCTGAAAAGTGCATTCGAT ATTGAAGAACTTAAAAAATTAGACATTATCGTGACTTGCCAAGGTGGCGATTACACCAAT GAAGTCTATCCAAAATTAAAAGCAACAGGTTGGGATGGTTATTGGGTTGATGCCGCTTCT GCGTTGCGTATGAAAGATGATGCAATTATCGTGCTTGATCCAGTAAACCAACACGTGATT TCTGAAGGTTTGAAAAAAGGCATTAAAACTTTCGTGGGCGGTAACTGTACCGTAAGCTTA ATGTTAATGGCTATCGGCGGTCTATTTGAAAAAGATTTGGTGGAATGGATTTCTGTGGCA ACTTATCAAGCGGCTTCAGGTGCTGGCGCAAAAAATATGCGTGAATTACTTTCACAAATG GGTTTATTAGAACAAGCAGTTTCGAGTGAATTAAAAGACCCTGCTTCATCTATTTTAGAT ATTGAACGTAAAGTGACTGCAAAAATGCGTGCTGATAATTTCCCAACGGATAACTTTGGC GCGGCATTAGGTGGTAGCTTAATCCCTTGGATTGACAAACTTCTTCCTGAAACAGGGCAA ACTAAAGAAGAATGGAAAGGTTATGCAGAAACCAATAAAATTTTAGGTTTAAGCGACAAT CCAATTCCTGTTGATGGTTTATGTGTGCGTATCGGTGCATTACGTTGCCATAGCCAAGCG TTTACCATCAAACTGAAAAAAGACTTACCATTAGAAGAAATCGAACAAATTATTGCATCA CATAATGAATGGGTAAAAGTGATTCCAAACGACAAAGAAATCACATTGCGTGAATTAACG CCAGCGAAAGTAACAGGTACATTAAGCGTGCCAGTGGGGCGTTTACGTAAATTGGCTATG GGGCCTGAATATTTGGCAGCTTTTACCGTGGGCGACCAATTATTATGGGGTGCGGCAGAG CCAGTTCGCCGTATTTTAAAACAATTAGTGGCATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P44801 UniProtKB Entry Name DHAS_HAEIN GenBank Protein ID 1573644 GenBank Gene ID L42023 - General References
- Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb JF, Dougherty BA, Merrick JM, et al.: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 1995 Jul 28;269(5223):496-512. [Article]
- Moore RA, Bocik WE, Viola RE: Expression and purification of aspartate beta-semialdehyde dehydrogenase from infectious microorganisms. Protein Expr Purif. 2002 Jun;25(1):189-94. [Article]
- Blanco J, Moore RA, Viola RE: Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase. Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12613-7. Epub 2003 Oct 14. [Article]
- Blanco J, Moore RA, Faehnle CR, Coe DM, Viola RE: The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase. Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1388-95. Epub 2004 Jul 21. [Article]
- Faehnle CR, Blanco J, Viola RE: Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase. Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2320-4. Epub 2004 Nov 26. [Article]