ID A0A1J0VDE7_9GAMM Unreviewed; 511 AA. AC A0A1J0VDE7; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 18-JUL-2018, entry version 16. DE RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme {ECO:0000256|PIRNR:PIRNR017184}; DE AltName: Full=Nicotinamide nucleotide repair protein {ECO:0000256|PIRNR:PIRNR017184}; DE Includes: DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|PIRNR:PIRNR017184}; DE EC=4.2.1.136 {ECO:0000256|PIRNR:PIRNR017184}; DE AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|PIRNR:PIRNR017184}; DE Includes: DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|PIRNR:PIRNR017184}; DE EC=5.1.99.6 {ECO:0000256|PIRNR:PIRNR017184}; GN Name=nnrE {ECO:0000256|HAMAP-Rule:MF_01966}; GN Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965}; GN ORFNames=BOX17_03195 {ECO:0000313|EMBL:APE30047.1}; OS Halomonas aestuarii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE30047.1, ECO:0000313|Proteomes:UP000181985}; RN [1] {ECO:0000313|Proteomes:UP000181985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985}; RA Koh H.-W., Rani S., Park S.-J.; RT "Halolamina sediminis sp. nov., an extremely halophilic archaeon RT isolated from solar salt."; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of CC the S- and R-forms of NAD(P)HX and the dehydration of the S-form CC of NAD(P)HX at the expense of ADP, which is converted to AMP. This CC allows the repair of both epimers of NAD(P)HX, a damaged form of CC NAD(P)H that is a result of enzymatic or heat-dependent hydration. CC {ECO:0000256|PIRNR:PIRNR017184}. CC -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at CC the expense of ADP, which is converted to AMP. Together with CC NAD(P)HX epimerase, which catalyzes the epimerization of the CC S- and R-forms, the enzyme allows the repair of both epimers of CC NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic CC or heat-dependent hydration. {ECO:0000256|HAMAP-Rule:MF_01965}. 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. {ECO:0000256|HAMAP-Rule:MF_01966}. 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 {ECO:0000256|PIRNR:PIRNR017184}. 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. {ECO:0000256|PIRNR:PIRNR017184}. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate + CC NADH. {ECO:0000256|PIRNR:PIRNR017184}. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide phosphate = AMP + CC phosphate + NADPH. {ECO:0000256|PIRNR:PIRNR017184}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01965}. CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP- CC Rule:MF_01965}. CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP- CC Rule:MF_01966}. CC -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD CC family. {ECO:0000256|PIRNR:PIRNR017184}. CC -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP CC family. {ECO:0000256|PIRNR:PIRNR017184}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}. 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; CP018139; APE30047.1; -; Genomic_DNA. DR RefSeq; WP_071942034.1; NZ_CP018139.1. DR GeneID; 30419328; -. DR KEGG; hsi:BOX17_03195; -. DR KO; K17758; -. DR KO; K17759; -. DR Proteomes; UP000181985; Chromosome. DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd01171; YXKO-related; 1. DR Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.40.50.10260; -; 1. DR HAMAP; MF_01965; NADHX_dehydratase; 1. DR HAMAP; MF_01966; NADHX_epimerase; 1. DR InterPro; IPR000631; CARKD. DR InterPro; IPR030677; Nnr. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR004443; YjeF_N_dom. DR InterPro; IPR036652; YjeF_N_dom_sf. DR Pfam; PF01256; Carb_kinase; 1. DR Pfam; PF03853; YjeF_N; 1. DR PIRSF; PIRSF017184; Nnr; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR SUPFAM; SSF64153; SSF64153; 1. DR TIGRFAMs; TIGR00196; yjeF_cterm; 1. DR TIGRFAMs; TIGR00197; yjeF_nterm; 1. DR PROSITE; PS51383; YJEF_C_3; 1. DR PROSITE; PS51385; YJEF_N; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01965, KW ECO:0000256|PIRNR:PIRNR017184}; KW Complete proteome {ECO:0000313|Proteomes:UP000181985}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01965, KW ECO:0000256|PIRNR:PIRNR017184}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01965, KW ECO:0000256|PIRNR:PIRNR017184}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; KW Reference proteome {ECO:0000313|Proteomes:UP000181985}. FT DOMAIN 21 222 YjeF N-terminal. {ECO:0000259|PROSITE: FT PS51385}. FT NP_BIND 413 417 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT NP_BIND 432 441 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT REGION 68 72 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 136 142 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 376 382 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. FT METAL 69 69 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 132 132 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 168 168 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 165 165 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 328 328 NAD(P)HX; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01965}. FT BINDING 442 442 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. SQ SEQUENCE 511 AA; 51550 MW; 1FC6D1F436F923D3 CRC64; MTRPAEPPAL SLRPLYRAEQ VRELDRRTIA AGCEGFALMQ RAAAAAWQDL KARWPHVQSL TVLCGGGNNG GDGHVLAALA AAEGVAVQRI LLKPVEELTG DARRAADMAT AAGVSAMPWR QDVSLEGELV VDALLGTGLG GEVRGPIREA IEAVNASGLP VLAIDIPSGL QADTGAMLGV AIRATLTVTF IGDKLGLYTG AAPAHVGELA FRALEVDAEA EGDLVPAARL LEAGLIAAWL PPRPRDAHKG DAGHSLVLGG APGFGGAALL AAEACARLGA GKVSLATAPE HVTASLVRRP EVMVHGVRGA GDLGSLPEHA DVLVVGPGLG QGSWGQGMLQ AALDASKPLV VDADGLNLLA SRFAGRHRDD WILTPHPGEA ARLLGLSVGE VEADRPAAAL ALQRRYGGVV VLKGAGSLVA GPEGLAVCPH GNPGMASGGM GDALSGILGA LLAQGLPIEP AAWLGVLVHA MAADMAAGQG GERGLLAGDL ASCARILVNP TTGEGDAAAT R //