ID A0A2N7PQK1_9BACT Unreviewed; 522 AA. AC A0A2N7PQK1; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 18-JUL-2018, entry version 4. 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=C0190_00020 {ECO:0000313|EMBL:PMP69234.1}; OS Thermodesulfobacterium geofontis. OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales; OC Thermodesulfobacteriaceae; Thermodesulfobacterium. OX NCBI_TaxID=1295609 {ECO:0000313|EMBL:PMP69234.1}; RN [1] {ECO:0000313|EMBL:PMP69234.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZAV-08 {ECO:0000313|EMBL:PMP69234.1}; RA Wilkins L., Ettinger C.; RT "Metagenomic assembled genomes from two thermal pools in the Uzon RT Caldera, Kamchatka, Russia."; RL Submitted (JAN-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 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 -!- 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:PMP69234.1}. 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; PNIK01000001; PMP69234.1; -; 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: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 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}. FT DOMAIN 9 224 YjeF N-terminal. {ECO:0000259|PROSITE: FT PS51385}. FT NP_BIND 428 432 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT NP_BIND 448 457 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT REGION 59 63 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 134 140 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 391 397 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. FT METAL 60 60 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 130 130 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 170 170 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 167 167 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 340 340 NAD(P)HX; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01965}. FT BINDING 458 458 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. SQ SEQUENCE 522 AA; 57115 MW; 3A6DCE6E999573CB CRC64; MKVVTGSEMQ ELDKVVINFL GISAEVLMER AGLGVAEKIL SYYPLERYRK VLIICGPGNN GGDGMVCARH LWDMDYEVKV LLLCKKEKYK GEALINLKIL ENLNLSLEEI KDLSVFKNLL YSYFPDILVD AIFGTGLKRS VEGVFKEVIE EINTYKEKKE AKVVAVDIPS GVCAETGQIL GTAVKADLTV TFELPKVGHF FYPGKEYVGK LEIVPIGFPK KIIEEKGPKR EYLDLNWAKI VFKPRRGYTH KGTFGHVVIL AGSRGKSGAG ALCALGALKG GAGLVTLAST KSLQKIYSSM IPEILTAGFE ENDKGEISYK NLMKILEIVK NKSVLVIGPG LGLSEEVKNL FFDLIPRLEI PLVIDADALT HLSENPEILK NYRAPKIITP HPGEAVRLLK VSKDEIMRDR LESAKRLSQL TDAIVVLKGP HSIVYSPDGR CGISSIDEPG LSQGGQGDIL SGLIGAFIAQ GYDPFIGTSL AVYLHGEAGK YLSKTLGPFG YTATEVAETV PKILKELKND RS //