ID A0A2N7V5N2_XANCJ Unreviewed; 495 AA. AC A0A2N7V5N2; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 20-JUN-2018, entry version 3. 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=C1H21_01440 {ECO:0000313|EMBL:PMR87929.1}; 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:PMR87929.1, ECO:0000313|Proteomes:UP000235775}; RN [1] {ECO:0000313|EMBL:PMR87929.1, ECO:0000313|Proteomes:UP000235775} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW3F3 {ECO:0000313|EMBL:PMR87929.1, RC ECO:0000313|Proteomes:UP000235775}; RA Fu B.; RT "Walnut bacterial blight pathogen Xaj-DW3F3 complete genome RT sequence."; 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:PMR87929.1}. 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; PNRC01000001; PMR87929.1; -; Genomic_DNA. DR RefSeq; WP_047124331.1; NZ_PNRC01000001.1. DR Proteomes; UP000235775; 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: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|HAMAP-Rule:MF_01965, KW ECO:0000256|PIRNR:PIRNR017184}; KW Complete proteome {ECO:0000313|Proteomes:UP000235775}; 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_01966, ECO:0000256|PIRNR:PIRNR017184}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}. FT DOMAIN 13 214 YjeF N-terminal. {ECO:0000259|PROSITE: FT PS51385}. FT NP_BIND 404 408 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT NP_BIND 424 433 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}. FT REGION 61 65 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 128 134 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT REGION 367 373 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01965}. FT METAL 62 62 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 124 124 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT METAL 160 160 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 157 157 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT MF_01966}. FT BINDING 320 320 NAD(P)HX; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01965}. FT BINDING 434 434 NAD(P)HX. {ECO:0000256|HAMAP-Rule: FT 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 //