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) |
---|---|
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 | T00219 D00003 D00010 D00017 D00027 D00028 D00034 D00476 |
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 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
P0A9Q9 |
Aspartate-semialdehyde dehydrogenase
|
ASA dehydrogenase
ASADH EC 1.2.1.11 |
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. |
---|---|---|
MAP00260 | Glycine, serine and threonine metabolism | |
MAP00300 | Lysine biosynthesis |
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 18051 537519 |
26078 26078 |
18009 18009 |
15836 15836 |
16474 16474 |
15378 15378 |
||||||
PubChem |
439235 5287708 439235 5287708 |
1004 22486802 1004 22486802 |
5886 5886 |
152441 152441 |
5884 5884 |
1038 1038 |
||||||
1brmA01 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1brmB01 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1brmC01 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1brmA02 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1brmB02 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1brmC02 | 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 | ||||||||||
1brmB01 | ||||||||||
1brmC01 | ||||||||||
1brmA02 | CYS 135;GLN 162;ARG 267;HIS 274 | |||||||||
1brmB02 | CYS 135;GLN 162;ARG 267;HIS 274 | |||||||||
1brmC02 | 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. |
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, |
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 |
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Created | Updated |
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2004-03-16 | 2009-02-26 |