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HAMAP rule MF_01965
General rule information
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| Accession | MF_01965 |
| Dates | 14-FEB-2012 (Created)
1-JUN-2023 (Last updated, Version 14) |
| Name | NADHX_dehydratase |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P94368 (NNRD_BACSU); P31806 (NNR_ECOLI); Q9X024 (NNR_THEMA); [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_01965 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| Identifier | NNRD |
| Protein name | RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase; EC=4.2.1.136; AltName: Full=ADP-dependent NAD(P)HX dehydratase; |
| Gene name | Name=nnrD; |
Comments
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| FUNCTION | Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. |
| CATALYTIC ACTIVITY | Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate; Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=4.2.1.136; |
| CATALYTIC ACTIVITY | Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate; Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=4.2.1.136; |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; |
| SUBUNIT | Homotetramer. |
| SIMILARITY | Belongs to the NnrD/CARKD family. |
Keywords
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Gene Ontology
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| GO:0052855; Molecular function:ADP-dependent NAD(P)H-hydrate dehydratase activity |
| GO:0046496; Biological process:nicotinamide nucleotide metabolic process |
Cross-references
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| PROSITE | PS01049; YJEF_C_1; 1; |
| PROSITE | PS01050; YJEF_C_2; 1; |
| PROSITE | PS51383; YJEF_C_3; 1; |
| Pfam | PF01256; Carb_kinase; 1; |
| NCBIfam | TIGR00196; YjeF_C; 1; |
Features
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| From: NNRD_BACSU (P94368) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 186 | 190 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
K-x(3)-[ST] | ||||||||
| BINDING | 42 | 42 | /ligand="(6S)-NADPHX" /ligand_id="ChEBI:CHEBI:64076" |
A | ||||||||
| BINDING | 104 | 104 | /ligand="(6S)-NADPHX" /ligand_id="ChEBI:CHEBI:64076" |
G | ||||||||
| BINDING | 149 | 149 | /ligand="(6S)-NADPHX" /ligand_id="ChEBI:CHEBI:64076" |
H | ||||||||
| BINDING | 215 | 215 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
G | ||||||||
| BINDING | 216 | 216 | /ligand="(6S)-NADPHX" /ligand_id="ChEBI:CHEBI:64076" |
D | ||||||||
Additional information
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| Size range | 257-304 amino acids |
| Related rules |
None |
| Fusion | Nter: MF_01966 (nrrE) Cter: None |