HAMAP rule MF_00804
General rule information
[?]
| Accession | MF_00804 |
| Dates | 20-JAN-2005 (Created)
3-SEP-2024 (Last updated, Version 27) |
| Name | BADH |
| Scope(s) |
Bacteria Pseudomonadota |
| Template(s) | P17445 (BETB_ECOLI); Q9HTJ1 (BETB_PSEAE); Q3JLL8 (BETB_BURP1); [ Recover all ] |
| Triggered by |
HAMAP; MF_00804 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Identifier | BETB |
| Protein name | RecName: Full=Betaine aldehyde dehydrogenase; Short=BADH; EC=1.2.1.8; |
| Gene name | Name=betB; |
Comments
[?]
| FUNCTION | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. |
| CATALYTIC ACTIVITY | Reaction=betaine aldehyde + NAD(+) + H2O = glycine betaine + NADH + 2 H(+); Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306; |
| COFACTOR | Name=K(+); Xref=ChEBI:CHEBI:29103; Note=Binds 2 potassium ions per subunit.; |
| PATHWAY | Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. |
| SUBUNIT | Dimer of dimers. |
| SIMILARITY | Belongs to the aldehyde dehydrogenase family. |
Keywords
[?]
Gene Ontology
[?]
| GO:0008802; Molecular function:betaine-aldehyde dehydrogenase (NAD+) activity |
| GO:0019285; Biological process:glycine betaine biosynthetic process from choline |
Cross-references
[?]
| Pfam | PF00171; Aldedh; 1; |
| NCBIfam | TIGR01804; BADH; 1; |
| PROSITE | PS00070; ALDEHYDE_DEHYDR_CYS; 1; |
| PROSITE | PS00687; ALDEHYDE_DEHYDR_GLU; 1; |
Features
[?]
| From: BETB_ECOLI (P17445) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 150 | 152 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-A-W | ||||||||
| BINDING | 176 | 179 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
K-P-S-E | ||||||||
| BINDING | 230 | 233 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-x(2)-[ST] | ||||||||
| ACT_SITE | 162 | 162 | /note="Charge relay system" | K | ||||||||
| ACT_SITE | 252 | 252 | /note="Proton acceptor" | E | ||||||||
| ACT_SITE | 286 | 286 | /note="Nucleophile" | C | ||||||||
| ACT_SITE | 464 | 464 | /note="Charge relay system" | E | ||||||||
| BINDING | 26 | 26 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" /ligand_label="1" |
[TS] | ||||||||
| BINDING | 27 | 27 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" /ligand_label="1" |
[IV] | ||||||||
| BINDING | 93 | 93 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" /ligand_label="1" |
[DN] | ||||||||
| BINDING | 180 | 180 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" /ligand_label="1" |
I | ||||||||
| BINDING | 246 | 246 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" /ligand_label="2" |
[LVI] | ||||||||
| BINDING | 457 | 457 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" /ligand_label="2" |
K | ||||||||
| BINDING | 460 | 460 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" /ligand_label="2" |
G | ||||||||
| BINDING | 254 | 254 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G | ||||||||
| BINDING | 286 | 286 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" /note="covalent" |
C | ||||||||
| BINDING | 387 | 387 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
E | ||||||||
| SITE | 248 | 248 | /note="Seems to be a necessary countercharge to the potassium cations" | [ED] | ||||||||
| MOD_RES | 286 | 286 | /note="Cysteine sulfenic acid (-SOH)" | C | ||||||||
Additional information
[?]
| Size range | 481-493 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | BetB from P.aeruginosa can use NADP(+) with similar efficiency to NAD(+), a property that can be used by the bacterium to produce the NADPH needed to combat the oxidative stress imposed by the host defenses. |