EzCatDB: D00023
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DB codeD00023
CATH domainDomain 13.40.50.720 : Rossmann fold
Domain 23.30.360.10 : Dihydrodipicolinate Reductase; domain 2Catalytic domain
E.C.1.2.1.11
CSA1brm

CATH domainRelated DB codes (homologues)
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2T00219,D00003,D00010,D00017,D00027,D00028,D00034,D00476
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

P0A9Q9
Protein nameAspartate-semialdehyde dehydrogenaseaspartate-semialdehyde dehydrogenase
aspartate semialdehyde dehydrogenase
aspartic semialdehyde dehydrogenase
L-aspartate-beta-semialdehyde:NADP+ oxidoreductase(phosphorylating)
aspartic beta-semialdehyde dehydrogenase
ASA dehydrogenase
SynonymsASA dehydrogenase
ASADH
EC 1.2.1.11
Aspartate-beta-semialdehyde dehydrogenase
RefSeqNP_417891.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492000.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF01118 (Semialdhyde_dh)
PF02774 (Semialdhyde_dhC)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00260Glycine, serine and threonine metabolism
MAP00300Lysine biosynthesis

UniProtKB:Accession NumberP0A9Q9
Entry nameDHAS_ECOLI
ActivityL-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00441C00009C00006C03082C00005C00080
CompoundL-Aspartate 4-semialdehydeOrthophosphateNADP+L-4-Aspartyl phosphateNADPHH+
Typeamino acids,carbohydratephosphate group/phosphate ionamide group,amine group,nucleotideamino acids,carbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotideothers
ChEBI18051
537519
26078
18009
15836
16474
15378
PubChem439235
5287708
1004
22486802
5886
152441
5884
1038
              
1brmA01UnboundUnboundUnboundUnboundUnbound 
1brmB01UnboundUnboundUnboundUnboundUnbound 
1brmC01UnboundUnboundUnboundUnboundUnbound 
1brmA02UnboundUnboundUnboundUnboundUnbound 
1brmB02UnboundUnboundUnboundUnboundUnbound 
1brmC02UnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot;P0A9Q9, literature [3]
pdbCatalytic residues
         
1brmA01 
1brmB01 
1brmC01 
1brmA02CYS 135;GLN 162;ARG 267;HIS 274
1brmB02CYS 135;GLN 162;ARG 267;HIS 274
1brmC02CYS 135;GLN 162;ARG 267;HIS 274

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.995-997

references
[1]
PubMed ID6108787
JournalBiochimie
Year1980
Volume62
Pages739-40
AuthorsThierry JC, Moras D, Eid P, Hirth C
TitleCrystallization of E. coli aspartate beta-semialdehyde dehydrogenase.
[2]
PubMed ID1360028
JournalJ Mol Biol
Year1992
Volume228
Pages300-1
AuthorsKryger G, Petsko GA, Ouyang J, Viola RE
TitleCrystallization and preliminary crystallographic analysis of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli.
[3]
PubMed ID10369777
JournalJ Mol Biol
Year1999
Volume289
Pages991-1002
AuthorsHadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R
TitleStructure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
[4]
PubMed ID12071715
JournalProtein Expr Purif
Year2002
Volume25
Pages189-94
AuthorsMoore RA, Bocik WE, Viola RE
TitleExpression and purification of aspartate beta-semialdehyde dehydrogenase from infectious microorganisms.


createdupdated
2004-03-162009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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