DB code: D00023

CATH domain 3.40.50.720 : Rossmann fold
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 Catalytic domain
E.C. 1.2.1.11
CSA 1brm
M-CSA 1brm
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 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
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 T00219 D00003 D00010 D00017 D00027 D00028 D00034 D00476

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0A9Q9 Aspartate-semialdehyde dehydrogenase
ASA dehydrogenase
ASADH
EC 1.2.1.11
Aspartate-beta-semialdehyde dehydrogenase
NP_417891.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492000.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01118 (Semialdhyde_dh)
PF02774 (Semialdhyde_dhC)
[Graphical View]

KEGG enzyme name
aspartate-semialdehyde dehydrogenase
aspartate semialdehyde dehydrogenase
aspartic semialdehyde dehydrogenase
L-aspartate-beta-semialdehyde:NADP+ oxidoreductase(phosphorylating)
aspartic beta-semialdehyde dehydrogenase
ASA dehydrogenase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A9Q9 DHAS_ECOLI L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH. Homodimer.

KEGG Pathways
Map code Pathways E.C.
MAP00300 Lysine biosynthesis
MAP00260 Glycine, serine and threonine metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00441 C00009 C00006 C03082 C00005 C00080
E.C.
Compound L-Aspartate 4-semialdehyde Orthophosphate NADP+ L-4-Aspartyl phosphate NADPH H+
Type amino acids,carbohydrate phosphate group/phosphate ion amide group,amine group,nucleotide amino acids,carbohydrate,phosphate group/phosphate ion amide group,amine group,nucleotide others
ChEBI 18051
537519
26078
18009
15836
16474
15378
PubChem 439235
5287708
1004
22486802
5886
152441
5884
1038
1brmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1brmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1brmC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1brmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1brmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1brmC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P0A9Q9, literature [3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1brmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1brmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1brmC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1brmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 135;GLN 162;ARG 267;HIS 274
1brmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 135;GLN 162;ARG 267;HIS 274
1brmC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 135;GLN 162;ARG 267;HIS 274

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.995-997

References
[1]
Resource
Comments
Medline ID
PubMed ID 6108787
Journal Biochimie
Year 1980
Volume 62
Pages 739-40
Authors Thierry JC, Moras D, Eid P, Hirth C
Title Crystallization of E. coli aspartate beta-semialdehyde dehydrogenase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1360028
Journal J Mol Biol
Year 1992
Volume 228
Pages 300-1
Authors Kryger G, Petsko GA, Ouyang J, Viola RE
Title Crystallization and preliminary crystallographic analysis of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10369777
Journal J Mol Biol
Year 1999
Volume 289
Pages 991-1002
Authors Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R
Title Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 12071715
Journal Protein Expr Purif
Year 2002
Volume 25
Pages 189-94
Authors Moore RA, Bocik WE, Viola RE
Title Expression and purification of aspartate beta-semialdehyde dehydrogenase from infectious microorganisms.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-16 2009-02-26