ID NNRE_BRAFL Reviewed; 273 AA. AC C3YDS7; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 29-MAY-2024, entry version 67. DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_03159}; DE EC=5.1.99.6; DE AltName: Full=NAD(P)HX epimerase {ECO:0000255|HAMAP-Rule:MF_03159}; GN ORFNames=BRAFLDRAFT_104103; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes; OC Branchiostomatidae; Branchiostoma. OX NCBI_TaxID=7739; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82; TISSUE=Testis; RX PubMed=18563158; DOI=10.1038/nature06967; RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J., RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V., RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A., RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T., RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). 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. {ECO:0000255|HAMAP-Rule:MF_03159}. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_03159}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_03159}; CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP- CC Rule:MF_03159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG666504; EEN61546.1; -; Genomic_DNA. DR RefSeq; XP_002605536.1; XM_002605490.1. DR AlphaFoldDB; C3YDS7; -. DR SMR; C3YDS7; -. DR STRING; 7739.C3YDS7; -. DR eggNOG; KOG2585; Eukaryota. DR InParanoid; C3YDS7; -. DR Proteomes; UP000001554; Genome assembly. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0052856; F:NADHX epimerase activity; IBA:GO_Central. DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1. DR HAMAP; MF_01966; NADHX_epimerase; 1. DR InterPro; IPR004443; YjeF_N_dom. DR InterPro; IPR036652; YjeF_N_dom_sf. DR InterPro; IPR032976; YJEFN_prot_NAXE-like. DR NCBIfam; TIGR00197; yjeF_nterm; 1. DR PANTHER; PTHR13232; NAD(P)H-HYDRATE EPIMERASE; 1. DR PANTHER; PTHR13232:SF10; NAD(P)H-HYDRATE EPIMERASE; 1. DR Pfam; PF03853; YjeF_N; 1. DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1. DR PROSITE; PS51385; YJEF_N; 1. PE 3: Inferred from homology; KW Isomerase; Metal-binding; NAD; NADP; Nucleotide-binding; Potassium; KW Reference proteome. FT CHAIN 1..273 FT /note="NAD(P)H-hydrate epimerase" FT /id="PRO_0000416314" FT DOMAIN 52..260 FT /note="YjeF N-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159" FT BINDING 105..109 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159" FT BINDING 106 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159" FT BINDING 170 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159" FT BINDING 174..180 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159" FT BINDING 203 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159" FT BINDING 206 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159" SQ SEQUENCE 273 AA; 30292 MW; 12B4A1EBF1173EFF CRC64; MESWKGKYAS GLRFSFRKRY STEKGGTVDE DCEVISIGHK IGDISYVSQE EAQQIDQELF NEYAYSVDQL MELAGHSCAV ALAKSYPLTS LKKDATVLVC CGPGNNGGDG LVCARHLKMF GYNPSVFYPK RTDKPLYKNL TIQCEQLDIP FLSHLPKPQL LSDGFSYIVD ALFGFSFKGE VRPPFGDVLK TLKEVTVPIC SIDVPSGWDV EGGNPDGLQP EFLISLTAPK KCAEKFAGRY HYLGGRFVPP GIIQKYELNL PTYPGTEPCI RLH //