AC MF_03159; DC Protein; auto c? TR HAMAP; MF_01966; -; 1; level=0 XX Names: NADHX_epimerase_euk XX ID NNRE case DE RecName: Full=NAD(P)H-hydrate epimerase; DE EC=5.1.99.6; DE AltName: Full=Apolipoprotein A-I-binding protein; DE Short=AI-BP; DE AltName: Full=NAD(P)HX epimerase; GN Name=APOA1BP; Synonyms=AIBP; else DE RecName: Full=NAD(P)H-hydrate epimerase; DE EC=5.1.99.6; DE AltName: Full=NAD(P)HX epimerase; end case XX case CC -!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of CC NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or CC heat-dependent hydration. This is a prerequisite for the S-specific CC NAD(P)H-hydrate dehydratase to allow the repair of both epimers of CC NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to CC high-density lipoprotein (HDL) and thereby regulates angiogenesis. else CC -!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of CC NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or CC heat-dependent hydration. This is a prerequisite for the S-specific CC NAD(P)H-hydrate dehydratase to allow the repair of both epimers of CC NAD(P)HX. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215, CC ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227, CC ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Note=Binds 1 potassium ion per subunit.; case CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. else case CC -!- SUBUNIT: Homodimer. Interacts with @gn(APOA1) and @gn(APOA2). CC -!- SUBCELLULAR LOCATION: Mitochondrion. Secreted. Note=In sperm, secretion CC gradually increases during capacitation. CC -!- PTM: Undergoes physiological phosphorylation during sperm capacitation, CC downstream to PKA activation. else case and not CC -!- SUBCELLULAR LOCATION: Mitochondrion. Secreted. end case case and not CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal CC transit peptide but none has been predicted. end case CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. XX DR PROSITE; PS51385; YJEF_N; 1; trigger=yes DR Pfam; PF03853; YjeF_N; 1; trigger=no DR NCBIfam; TIGR00197; YjeF_nterm; 1; trigger=no case DR General; TransitM; -; 0-1; trigger=yes end case XX KW Isomerase KW Metal-binding KW NAD KW Nucleotide-binding KW Potassium case KW Cytoplasm KW Mitochondrion else case KW Mitochondrion KW Secreted end case XX GO GO:0052856; F:NADHX epimerase activity case GO GO:0005737; C:cytoplasm else case GO GO:0005739; C:mitochondrion end case XX FT From: NNR_THEMA (Q9X024) FT BINDING 52 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Condition: [NQ] FT BINDING 114 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Condition: D FT BINDING 150 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Condition: [ST] FT BINDING 51..55 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT Condition: x-[NQ]-G-x(2) FT BINDING 118..124 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT BINDING 129 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT Optional; Condition: Y FT BINDING 147 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT Condition: [DE] XX Size: 204-292; Related: None; Template: Q9X024; Q8NCW5; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.15 2023/06/01 //