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HAMAP rule MF_00804

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General rule information [?]

Accession MF_00804
Dates 20-JAN-2005 (Created)
1-JUN-2023 (Last updated, Version 26)
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 [?]

FUNCTIONInvolved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.
CATALYTIC ACTIVITY Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH; 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.;
PATHWAYAmine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
SUBUNITDimer of dimers.
SIMILARITYBelongs to the aldehyde dehydrogenase family.

Keywords [?]


Gene Ontology [?]

GO:0008802; Molecular function:betaine-aldehyde dehydrogenase 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.



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