AC   MF_02121;
DC   Protein; auto
TR   HAMAP; MF_02121; -; 1; level=0
XX
Names: ASADH
XX
ID   DHAS
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
DE   AltName: Full=Aspartate-beta-semialdehyde dehydrogenase;
GN   Name=asd;
XX
CC   -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC       semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-
CC       4-phosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-
CC         L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 2/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 2/5.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
XX
DR   PROSITE; PS01103; ASD; 1; trigger=no
DR   Pfam; PF01118; Semialdhyde_dh; 1; trigger=no
DR   Pfam; PF02774; Semialdhyde_dhC; 1; trigger=no
DR   NCBIfam; TIGR01745; Asd_gamma; 1; trigger=no
DR   NCBIfam; TIGR01296; Asd_B; 1; trigger=no
DR   NCBIfam; TIGR00978; Asd_EA; 1; trigger=no
DR   PIRSF; PIRSF000148; ASA_dh; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Diaminopimelate biosynthesis
KW   Lysine biosynthesis
KW   Methionine biosynthesis
KW   NADP
KW   Oxidoreductase
KW   Threonine biosynthesis
XX
GO   GO:0004073; F:aspartate-semialdehyde dehydrogenase activity
GO   GO:0050661; F:NADP binding
GO   GO:0071266; P:'de novo' L-methionine biosynthetic process
GO   GO:0009088; P:threonine biosynthetic process
GO   GO:0009089; P:lysine biosynthetic process via diaminopimelate
GO   GO:0019877; P:diaminopimelate biosynthetic process
XX
FT   From: DHAS_ECOLI (P0A9Q9)
FT   BINDING         10..13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [RTS]-G-x-[VG]
FT   BINDING         37..38
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [TRNKS]-S
FT   BINDING         165..166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: S-G
FT   ACT_SITE        135
FT                   /note="Acyl-thioester intermediate"
FT   Condition: C
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         73
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: Q
FT   BINDING         102
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT   Condition: R
FT   BINDING         162
FT                   /ligand="substrate"
FT   Condition: Q
FT   BINDING         193
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: P
FT   BINDING         267
FT                   /ligand="substrate"
FT   Condition: R
case not <OC:Archaea> and not <OC:Spirochaetota>
FT   BINDING         241
FT                   /ligand="substrate"
FT   Optional; Condition: E
FT   BINDING         244
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT   Condition: K
FT   BINDING         350
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [QN]
end case
FT   From: DHAS_METJA (Q57658)
case <OC:Archaea> or <OC:Spirochaetota>
FT   BINDING         210
FT                   /ligand="substrate"
FT   Condition: E
FT   BINDING         213
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT   Condition: K
FT   BINDING         333..334
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: N-T
end case
XX
Size: 337-376;
Related: None;
Template: P0A9Q9; P9WNX5; P44801; P23247; Q9KQG2; Q51344; Q57658; P0A1F8;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in VIBCH
Plasmid: None
Comments: None
XX
# Revision 1.10 2023/06/01
//