ID A0A2N7V5N2_XANCJ Unreviewed; 495 AA. AC A0A2N7V5N2; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 03-AUG-2022, entry version 20. 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=nnrD {ECO:0000256|HAMAP-Rule:MF_01965}; GN Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966}; GN ORFNames=XSP_002516 {ECO:0000313|EMBL:CAD1793226.1}, XSP_002539 GN {ECO:0000313|EMBL:CAD0331144.1}; OS Xanthomonas campestris pv. juglandis (Xanthomonas arboricola pv. OS juglandis). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=195709 {ECO:0000313|EMBL:CAD0331144.1}; RN [1] {ECO:0000313|EMBL:CAD0331144.1, ECO:0000313|Proteomes:UP000514411} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3 {ECO:0000313|EMBL:CAD1793226.1}, and Xanthomonas arboricola RC pv. juglandis CPBF 427 {ECO:0000313|EMBL:CAD0331144.1}; RA Teixeira M.; RL Submitted (JUL-2020) 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 --------------------------------------------------------------------------- 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; LR824643; CAD0331144.1; -; Genomic_DNA. DR EMBL; LR861807; CAD1793226.1; -; Genomic_DNA. DR RefSeq; WP_047124331.1; NZ_UNRO01000041.1. DR Proteomes; UP000514411; Chromosome: 1. 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; IPR017953; Carbohydrate_kinase_pred_CS. 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; PS01049; YJEF_C_1; 1. DR PROSITE; PS51383; YJEF_C_3; 1. DR PROSITE; PS51385; YJEF_N; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01965}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01966}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01965}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01965}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01965}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01965}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184}. FT DOMAIN 13..214 FT /note="YjeF N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51385" FT REGION 61..65 FT /note="NADPHX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT REGION 128..134 FT /note="NADPHX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 62 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 124 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 157 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 160 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 259 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 320 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 367 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 404..408 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 433 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 434 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" SQ SEQUENCE 495 AA; 50626 MW; 40E4C410D73D9FEC CRC64; MYAPLDLYDT AAARRLDTQA TTLLGGDGYI LMERAGQAAW QHLLERWPQA RRIVVVCGTG NNGGDGYVLA RLAQRAGRQV QVVHLAEHGP ASSLAQRACT DYLGVGGAIE LFPSPLAQAD VIVDALFGIG LNRAPDAETT ALIDAINAAG VPVLALDVPS GIDADHGVAF GAAVRAQATL QFIVPHLGLH TGDALEHAGT RATASLDVPD AAFDGLAPAA HSWDIDALAA QLRPRRRNTH KGESGRVLCV GGNLGSGGAV MLTAEAALRS GAGLVQVATR VEHVAPLLAR CPEAMVRAVQ ADEDIAALAD AADVVALGPG LGQDHWAQQL WRAVLASDSA VVIDADGLNL LAANPVPARG PRVLTPHPGE AGWLLGISTR QVQQDRLAAA DALAKRFNAV VVLKGAGSVI AAPHAVPRII DAGNPGMAVG GMGDLLTGVI AALLGQGWSP FDAASLGALL HACAGDAAAR AGERGLLPTD LLPELRRLAN AGAIA //