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HAMAP rule MF_03159
General rule information
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Accession | MF_03159 |
Dates | 14-FEB-2012 (Created)
1-JUN-2023 (Last updated, Version 15) |
Name | NADHX_epimerase_euk |
Scope(s) |
Eukaryota |
Template(s) | Q9X024 (NNR_THEMA); Q8NCW5 (NNRE_HUMAN); [ Recover all ] |
Triggered by |
case c? <OC:Eukaryota>
HAMAP; MF_01966 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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Identifier | NNRE |
case <OC:Vertebrata> | |
Protein name | RecName: Full=NAD(P)H-hydrate epimerase; EC=5.1.99.6; AltName: Full=Apolipoprotein A-I-binding protein; Short=AI-BP; AltName: Full=NAD(P)HX epimerase; |
Gene name | Name=APOA1BP; Synonyms=AIBP; |
else | |
Protein name | RecName: Full=NAD(P)H-hydrate epimerase; EC=5.1.99.6; AltName: Full=NAD(P)HX epimerase; |
end case |
Comments
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case <OC:Mammalia> | |
FUNCTION | Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis. |
else | |
FUNCTION | Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. |
end case | |
CATALYTIC ACTIVITY | Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215, ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6; |
CATALYTIC ACTIVITY | Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227, ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6; |
COFACTOR | Name=K(+); Xref=ChEBI:CHEBI:29103; Note=Binds 1 potassium ion per subunit.; |
case <OC:Fungi> | |
SUBCELLULAR LOCATION | Cytoplasm. Mitochondrion. |
else case <OC:Mammalia> | |
SUBUNIT | Homodimer. Interacts with @gn(APOA1) and @gn(APOA2). |
SUBCELLULAR LOCATION | Mitochondrion. Secreted. Note=In sperm, secretion gradually increases during capacitation. |
PTM | Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation. |
else case <OC:Vertebrata> and not <OC:Mammalia> | |
SUBCELLULAR LOCATION | Mitochondrion. Secreted. |
end case | |
case <OC:Vertebrata> and not <AnyFeature:TransitM> | |
MISCELLANEOUS | This protein may be expected to contain an N-terminal transit peptide but none has been predicted. |
end case | |
SIMILARITY | Belongs to the NnrE/AIBP family. |
Keywords
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Isomerase | |
Metal-binding | |
NAD | |
Nucleotide-binding | |
Potassium | |
case <OC:Fungi> | |
Cytoplasm | |
Mitochondrion | |
else case <OC:Vertebrata> | |
Mitochondrion | |
Secreted | |
end case |
Gene Ontology
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GO:0052856; Molecular function:NADHX epimerase activity | |
case <OCellular component:Fungi> | |
GO:0005737; Cellular component:cytoplasm | |
else case <OCellular component:Vertebrata> | |
GO:0005739; Cellular component:mitochondrion | |
end case |
Cross-references
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PROSITE | PS51385; YJEF_N; 1; |
Pfam | PF03853; YjeF_N; 1; |
NCBIfam | TIGR00197; YjeF_nterm; 1; |
General | TransitM; -; 0-1; |
Features
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From: NNR_THEMA (Q9X024) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 52 | 52 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
[NQ] | ||||||||
BINDING | 114 | 114 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
D | ||||||||
BINDING | 150 | 150 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
[ST] | ||||||||
BINDING | 51 | 55 | /ligand="(6S)-NADPHX" /ligand_id="ChEBI:CHEBI:64076" |
x-[NQ]-G-x(2) | ||||||||
BINDING | 118 | 124 | /ligand="(6S)-NADPHX" /ligand_id="ChEBI:CHEBI:64076" |
|||||||||
BINDING | 129 | 129 | /ligand="(6S)-NADPHX" /ligand_id="ChEBI:CHEBI:64076" |
Y | ||||||||
BINDING | 147 | 147 | /ligand="(6S)-NADPHX" /ligand_id="ChEBI:CHEBI:64076" |
[DE] |
Additional information
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Size range | 204-292 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |