ID A0A2N8NSB6_STREU Unreviewed; 482 AA. AC A0A2N8NSB6; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 02-JUN-2021, entry version 13. 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=AF335_22665 {ECO:0000313|EMBL:PNE31668.1}, FHS36_005042 GN {ECO:0000313|EMBL:MBB5121577.1}; OS Streptomyces eurocidicus (Streptoverticillium eurocidicus). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=66423 {ECO:0000313|EMBL:PNE31668.1, ECO:0000313|Proteomes:UP000235945}; RN [1] {ECO:0000313|EMBL:PNE31668.1, ECO:0000313|Proteomes:UP000235945} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27428 {ECO:0000313|EMBL:PNE31668.1, RC ECO:0000313|Proteomes:UP000235945}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:MBB5121577.1, ECO:0000313|Proteomes:UP000528608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 3259 {ECO:0000313|EMBL:MBB5121577.1, RC ECO:0000313|Proteomes:UP000528608}; RA Whitman W.; RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of RT soil and plant-associated and newly described type strains."; RL Submitted (AUG-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|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|ARBA:ARBA00001958}; 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:PNE31668.1}. 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; JACHJF010000019; MBB5121577.1; -; Genomic_DNA. DR EMBL; LGUI01000008; PNE31668.1; -; Genomic_DNA. DR EnsemblBacteria; PNE31668; PNE31668; AF335_22665. DR Proteomes; UP000235945; Unassembled WGS sequence. DR Proteomes; UP000528608; 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:0016301; F:kinase activity; IEA:UniProtKB-KW. 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 Kinase {ECO:0000313|EMBL:PNE31668.1}; 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}; KW Transferase {ECO:0000313|EMBL:PNE31668.1}. FT DOMAIN 10..208 FT /note="YjeF N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51385" FT NP_BIND 390..394 FT /note="ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT NP_BIND 411..420 FT /note="ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT REGION 58..62 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT REGION 124..130 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT REGION 353..359 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT METAL 59 FT /note="Potassium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT METAL 120 FT /note="Potassium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT METAL 154 FT /note="Potassium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 151 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 305 FT /note="NAD(P)HX; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 421 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" SQ SEQUENCE 482 AA; 47900 MW; DC07F2EF1CEF701F CRC64; MRTAYSVETV RAAERALMAQ LPQGALMQRA AAGLAAACAD LLGRTYGARV ALLVGSGDNG GDALYAGARL ARRGAGVTAV LLAPERTHQG GLAALRAAGG RVASAEEGDR AVRRADLVVD GIVGIGGRGG LRPEAEALVA AAEGALVLAV DLPSGVDADS GEVRGATVRA DATVTFGAYK PGLLIDPARE RAGALRLIDI GLGPHLPRRP EAEALQHADV AALLPRPAAE SDKYRRGVVG VVAGSARYPG AAVLAVAGAL HGGAGAVRYA GPAAEAVVSR FPETLVSEGP PSKAGRVQAW VVGPGVGDDA AARRALDDVL ASDVPVLVDA DGLRLLPEAA VRARGAETVL TPHAGEAAAL LGVSRSRVES ARLSAARELA ARFGATALLK GSTTVVAAPG RTAVRVNPTG TPWLATAGSG DVLSGVTGSL LAAGLRGLDA ASVGAYLHGL AARSLGGAPL TASGVAEALA GAWGEVTGHS YE //