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 11-JUN-2014, entry version 33. DE RecName: Full=NAD(P)H-hydrate epimerase; DE EC=5.1.99.6; DE AltName: Full=NAD(P)HX epimerase; GN ORFNames=BRAFLDRAFT_104103; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC 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., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA 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 CC or heat-dependent hydration. This is a prerequisite for the S- CC specific NAD(P)H-hydrate dehydratase to allow the repair of both CC epimers of NAD(P)HX (By similarity). CC -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy- CC 1,4,5,6-tetrahydronicotinamide-adenine dinucleotide. CC -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6- CC beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide CC phosphate. CC -!- COFACTOR: Binds 1 potassium ion per subunit (By similarity). CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. CC -!- SIMILARITY: Contains 1 YjeF N-terminal domain. 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 UniGene; Bfl.7308; -. DR ProteinModelPortal; C3YDS7; -. DR STRING; 7739.JGI104103; -. DR GeneID; 7211736; -. DR KEGG; bfo:BRAFLDRAFT_104103; -. DR eggNOG; NOG261179; -. DR KO; K17759; -. DR OMA; ELMSTGA; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.10260; -; 1. DR HAMAP; MF_01966; NADHX_epimerase; 1. DR InterPro; IPR004443; YjeF_N_dom. DR Pfam; PF03853; YjeF_N; 1. DR SUPFAM; SSF64153; SSF64153; 1. DR TIGRFAMs; TIGR00197; yjeF_nterm; 1. DR PROSITE; PS51385; YJEF_N; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Metal-binding; NAD; NADP; KW Nucleotide-binding; Potassium; Reference proteome. FT CHAIN 1 273 NAD(P)H-hydrate epimerase. FT /FTId=PRO_0000416314. FT DOMAIN 52 260 YjeF N-terminal. FT REGION 105 109 NAD(P)HX (By similarity). FT REGION 174 180 NAD(P)HX (By similarity). FT METAL 106 106 Potassium (By similarity). FT METAL 170 170 Potassium (By similarity). FT METAL 206 206 Potassium (By similarity). FT BINDING 203 203 NAD(P)HX (By similarity). 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 //