ID A0A2N7PQK1_9BACT Unreviewed; 522 AA. AC A0A2N7PQK1; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 03-AUG-2022, 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=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, ECO:0000313|Proteomes:UP000235460}; RN [1] {ECO:0000313|EMBL:PMP69234.1, ECO:0000313|Proteomes:UP000235460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 Caldera, RT Kamchatka, Russia."; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of the CC S- and R-forms of NAD(P)HX and the dehydration of the S-form of CC NAD(P)HX at the expense of ADP, which is converted to AMP. This allows CC the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that CC is a result of enzymatic or heat-dependent hydration. CC {ECO:0000256|ARBA:ARBA00025153, ECO:0000256|PIRNR:PIRNR017184}. CC -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the CC expense of ADP, which is converted to AMP. Together with NAD(P)HX CC epimerase, which catalyzes the epimerization of the S- and R-forms, the CC enzyme 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|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 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:0000256|HAMAP-Rule:MF_01966}. 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|ARBA:ARBA00000013, ECO:0000256|HAMAP- CC Rule:MF_01966, 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|ARBA:ARBA00000909, ECO:0000256|HAMAP- CC Rule:MF_01966, 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; CC Evidence={ECO:0000256|ARBA:ARBA00001026, 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; CC Evidence={ECO:0000256|ARBA:ARBA00001241, ECO:0000256|HAMAP- CC Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01966, CC 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; CC Evidence={ECO:0000256|HAMAP-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|ARBA:ARBA00009524, ECO:0000256|PIRNR:PIRNR017184}. CC -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family. CC {ECO:0000256|ARBA:ARBA00006001, ECO:0000256|PIRNR:PIRNR017184}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 EnsemblBacteria; PMP69234; PMP69234; C0190_00020. DR Proteomes; UP000235460; Unassembled WGS sequence. 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:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC. 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|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01966}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01965, 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, ECO:0000256|PIRNR:PIRNR017184}. FT DOMAIN 9..224 FT /note="YjeF N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51385" FT REGION 59..63 FT /note="NADPHX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT REGION 134..140 FT /note="NADPHX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 60 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 130 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 167 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 170 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 269 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 340 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 391 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 428..432 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 457 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 458 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule: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 //