ID A0A3A5VGD8_9EURY Unreviewed; 481 AA. AC A0A3A5VGD8; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 13-FEB-2019, entry version 3. DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_01965}; DE EC=4.2.1.136 {ECO:0000256|HAMAP-Rule:MF_01965}; DE AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_01965}; GN Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965}; GN ORFNames=DWC02_01315 {ECO:0000313|EMBL:RJU88550.1}; OS Marine Group II euryarchaeote. OC Archaea; Euryarchaeota; Diaforarchaea group; Marine Group II. OX NCBI_TaxID=2163009 {ECO:0000313|EMBL:RJU88550.1}; RN [1] {ECO:0000313|EMBL:RJU88550.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bin_156 {ECO:0000313|EMBL:RJU88550.1}; RA Rinke C.; RT "A phylogenomic and ecological analysis of the globally abundant RT Marine Group II archaea (Poseidoniales ord. nov.)."; RL Submitted (JUL-2018) 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 S-and CC R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, CC a damaged form of NAD(P)H that is a result of enzymatic or heat- CC dependent hydration. {ECO:0000256|HAMAP-Rule:MF_01965}. 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 Evidence={ECO:0000256|PIRNR:PIRNR017184}; 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 Evidence={ECO:0000256|PIRNR:PIRNR017184}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate; CC Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215, CC ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate; CC Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215, CC ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|PIRNR:PIRNR017184}; CC Note=Binds 1 potassium ion per subunit. CC {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: 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_01965}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RJU88550.1}. 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; QQSA01000019; RJU88550.1; -; Genomic_DNA. 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:0016853; F:isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; 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 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 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 Isomerase {ECO:0000256|PIRNR:PIRNR017184}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01965, KW ECO:0000256|PIRNR:PIRNR017184}; KW Metal-binding {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|PIRNR:PIRNR017184}. FT DOMAIN 12 197 YjeF N-terminal. {ECO:0000259|PROSITE: FT PS51385}. FT NP_BIND 398 407 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT REGION 348 354 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. FT BINDING 301 301 NAD(P)HX; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01965}. FT BINDING 408 408 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. SQ SEQUENCE 481 AA; 50515 MW; 154975BDFDBE82AF CRC64; MRPRWIMSPQ EVAVLDSNAE ALGADMDELM KTAAEHLANA LEGAPKPIWI LCGPGNNGGD GFRLATIFEG CKVVATHDKQ KTPLAQRARD DWDGEVHSVE NLPKEDPAVI VDCLLGAGSF GQPRGEILSL MEKIPGRPMV LACDMPTGCG SGVSFNAFRT VTFEAPKSNM IDSHGKLLPE VGDLFIAPVG WPEETLDPGP GDLLRYPHPK EGQIKGDRGR VLIVGGGPYH GAPILSGMAA ARMGVDLVHV AMPKAAAARA KWPSELIQES MTDQEIITDV SDLVKRCMTG RGVQAMVIGP GMGDAPESIE AVKMLIQATP NVPKVIDADA IRALDGWPEG LVGVVTPHQK ELENWIGNID TVPDLIAGSG ESRVVIRTGA EDIIIGAGGR GGIGMGGNPR MSMGGTGDLL AGSIGGLLGL GLSPWSAARL GVHLMRVAGK LAENEIGPGM VADDIPPYLS RALITGPVLL RQPMQEDPSS S //