AC   MF_01275;
DC   Protein; auto
TR   HAMAP; MF_01275; -; 1; level=0
XX
Names: Aldedh_Prr
XX
ID   ABDH
DE   RecName: Full=Gamma-aminobutyraldehyde dehydrogenase;
DE            Short=ABALDH;
DE            EC=1.2.1.19;
DE   AltName: Full=1-pyrroline dehydrogenase;
DE   AltName: Full=4-aminobutanal dehydrogenase;
DE   AltName: Full=5-aminopentanal dehydrogenase;
DE            EC=1.2.1.-;
GN   Name=patD;
XX
CC   -!- FUNCTION: Catalyzes the oxidation 4-aminobutanal (gamma-
CC       aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA).
CC       This is the second step in one of two pathways for putrescine
CC       degradation, where putrescine is converted into 4-aminobutanoate via 4-
CC       aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a
CC       L-lysine degradation pathway to succinate that proceeds via cadaverine,
CC       glutarate and L-2-hydroxyglutarate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC         ChEBI:CHEBI:59888; EC=1.2.1.19;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-aminopentanal + H2O + NAD(+) = 5-aminopentanoate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:61632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144896,
CC         ChEBI:CHEBI:356010;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61633;
CC   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC       aminobutanoate from 4-aminobutanal: step 1/1.
CC   -!- PATHWAY: Amino-acid degradation.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: 4-aminobutanal can spontaneously cyclize to 1-pyrroline,
CC       and 5-aminopentanal to 1-piperideine.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. Gamma-
CC       aminobutyraldehyde dehydrogenase subfamily.
XX
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1; trigger=no
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1; trigger=no
DR   Pfam; PF00171; Aldedh; 1; trigger=no
DR   NCBIfam; TIGR03374; ABALDH; 1; trigger=no
XX
KW   NAD
KW   Oxidoreductase
XX
GO   GO:0019145; F:aminobutyraldehyde dehydrogenase activity
GO   GO:0051287; F:NAD binding
GO   GO:0009447; P:putrescine catabolic process
GO   GO:0019477; P:L-lysine catabolic process
XX
FT   From: ABDH_ECOLI (P77674)
FT   BINDING         146..148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: A-x-W
FT   BINDING         172..175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: K-x-x-E
FT   BINDING         225..228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: S-x-x-T
FT   ACT_SITE        246
FT   Condition: E
FT   ACT_SITE        280
FT                   /note="Nucleophile"
FT   Condition: C
FT   BINDING         209
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: D
FT   BINDING         280
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: C
XX
Size: 465-485;
Related: None;
Template: P77674;
Scope:
 Bacteria; Enterobacterales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.20 2023/06/01
//