AC   MF_00804;
DC   Protein; auto
TR   HAMAP; MF_00804; -; 1; level=0
XX
Names: BADH
XX
ID   BETB
DE   RecName: Full=Betaine aldehyde dehydrogenase;
DE            Short=BADH;
DE            EC=1.2.1.8;
GN   Name=betB;
XX
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC       betaine. Catalyzes the irreversible oxidation of betaine aldehyde to
CC       the corresponding acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.8;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC       Note=Binds 2 potassium ions per subunit.;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine from betaine aldehyde: step 1/1.
CC   -!- SUBUNIT: Dimer of dimers.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
XX
DR   Pfam; PF00171; Aldedh; 1; trigger=no
DR   NCBIfam; TIGR01804; BADH; 1; trigger=no
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1; trigger=no
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1; trigger=no
XX
KW   NAD
KW   NADP
KW   Oxidoreductase
KW   Oxidation
KW   Metal-binding
KW   Potassium
XX
GO   GO:0008802; F:betaine-aldehyde dehydrogenase activity
GO   GO:0019285; P:glycine betaine biosynthetic process from choline
XX
FT   From: BETB_ECOLI (P17445)
FT   BINDING         150..152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: G-A-W
FT   BINDING         176..179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: K-P-S-E
FT   BINDING         230..233
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: G-x(2)-[ST]
FT   ACT_SITE        162
FT                   /note="Charge relay system"
FT   Condition: K
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT   Condition: E
FT   ACT_SITE        286
FT                   /note="Nucleophile"
FT   Condition: C
FT   ACT_SITE        464
FT                   /note="Charge relay system"
FT   Condition: E
FT   BINDING         26
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT   Condition: [TS]
FT   BINDING         27
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT   Condition: [IV]
FT   BINDING         93
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT   Condition: [DN]
FT   BINDING         180
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT   Condition: I
FT   BINDING         246
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT   Condition: [LVI]
FT   BINDING         457
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT   Condition: K
FT   BINDING         460
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT   Condition: G
FT   BINDING         254
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: G
FT   BINDING         286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /note="covalent"
FT   Condition: C
FT   BINDING         387
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: E
FT   SITE            248
FT                   /note="Seems to be a necessary countercharge to the
FT                   potassium cations"
FT   Condition: [ED]
FT   MOD_RES         286
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT   Condition: C
XX
Size: 481-493;
Related: None;
Template: P17445; Q9HTJ1; Q3JLL8;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: in RHIME
Plasmid: in RHIME
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.
XX
# Revision 1.26 2023/06/01
//