HAMAP rule MF_01275
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01275 |
| Accession | MF_01275 |
| Dates | 29-NOV-2006 (Created)
03-SEP-2024 (Last updated, Version 22) |
| Name | Aldedh_Prr |
| Scope(s) |
Bacteria Enterobacterales |
| Template(s) | P77674; [ Recover all ] |
| Triggered by |
HAMAP; MF_01275 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | ABDH |
| Protein name | RecName: Full=Gamma-aminobutyraldehyde dehydrogenase; Short=ABALDH; EC=1.2.1.19; AltName: Full=1-pyrroline dehydrogenase; AltName: Full=4-aminobutanal dehydrogenase; AltName: Full=5-aminopentanal dehydrogenase; EC=1.2.1.-; |
| Gene name | Name=patD; |
Comments
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| FUNCTION | Catalyzes the oxidation 4-aminobutanal (gamma- aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4- aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. |
| CATALYTIC ACTIVITY | Reaction=4-aminobutanal + NAD(+) + H2O = 4-aminobutanoate + NADH + 2 H(+); Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; |
| CATALYTIC ACTIVITY | Reaction=5-aminopentanal + NAD(+) + H2O = 5-aminopentanoate + NADH + 2 H(+); Xref=Rhea:RHEA:61632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144896, ChEBI:CHEBI:356010; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61633; |
| PATHWAY | Amine and polyamine degradation; putrescine degradation; 4- aminobutanoate from 4-aminobutanal: step 1/1. |
| PATHWAY | Amino-acid degradation. |
| SUBUNIT | Homotetramer. |
| MISCELLANEOUS | 4-aminobutanal can spontaneously cyclize to 1-pyrroline, and 5-aminopentanal to 1-piperideine. |
| SIMILARITY | Belongs to the aldehyde dehydrogenase family. Gamma- aminobutyraldehyde dehydrogenase subfamily. |
Keywords
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Gene Ontology
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| GO:0019145; Molecular function:aminobutyraldehyde dehydrogenase (NAD+) activity |
| GO:0051287; Molecular function:NAD binding |
| GO:0009447; Biological process:putrescine catabolic process |
| GO:0019477; Biological process:L-lysine catabolic process |
Cross-references
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| PROSITE | PS00070; ALDEHYDE_DEHYDR_CYS; 1; |
| PROSITE | PS00687; ALDEHYDE_DEHYDR_GLU; 1; |
| Pfam | PF00171; Aldedh; 1; |
| NCBIfam | TIGR03374; ABALDH; 1; |
Features
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| From: ABDH_ECOLI (P77674) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 146 | 148 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
A-x-W | ||||||||
| BINDING | 172 | 175 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
K-x-x-E | ||||||||
| BINDING | 225 | 228 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
S-x-x-T | ||||||||
| ACT_SITE | 246 | 246 | E | |||||||||
| ACT_SITE | 280 | 280 | /note="Nucleophile" | C | ||||||||
| BINDING | 209 | 209 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
D | ||||||||
| BINDING | 280 | 280 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
C | ||||||||
Additional information
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| Size range | 465-485 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |