ID H2IS53_RAHAC Unreviewed; 504 AA. AC H2IS53; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 12-AUG-2020, entry version 58. 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 OrderedLocusNames=Rahaq2_0450 {ECO:0000313|EMBL:AEX50384.1}; OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / OS NCIMB 13365 / CIP 78.65). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Rahnella. OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX50384.1, ECO:0000313|Proteomes:UP000009010}; RN [1] {ECO:0000313|EMBL:AEX50384.1, ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; RX PubMed=22582378; DOI=10.1128/JB.00380-12; RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S., RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S., RA Tapia R., Woyke T., Sobecky P.A.; RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65."; RL J. Bacteriol. 194:3020-3021(2012). RN [2] {ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., RA Martinez R., Woyke T.; RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65."; RL Submitted (JAN-2012) 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|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 --------------------------------------------------------------------------- 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; CP003244; AEX50384.1; -; Genomic_DNA. DR RefSeq; WP_014333655.1; NZ_JMPO01000135.1. DR STRING; 745277.GRAQ_03735; -. DR EnsemblBacteria; AEX50384; AEX50384; Rahaq2_0450. DR KEGG; raq:Rahaq2_0450; -. DR PATRIC; fig|745277.3.peg.426; -. DR eggNOG; COG0062; Bacteria. DR eggNOG; COG0063; Bacteria. DR HOGENOM; CLU_024853_4_3_6; -. DR KO; K23997; -. DR OMA; HNGGDAL; -. DR Proteomes; UP000009010; Chromosome. 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; 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; PS01050; YJEF_C_2; 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, ECO:0000256|PIRNR:PIRNR017184}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01966, KW ECO:0000256|PIRNR:PIRNR017184}; Kinase {ECO:0000313|EMBL:AEX50384.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, 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|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01965, KW ECO:0000256|PIRNR:PIRNR017184}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01965, KW ECO:0000256|PIRNR:PIRNR017184}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184}; KW Reference proteome {ECO:0000313|Proteomes:UP000009010}; KW Transferase {ECO:0000313|EMBL:AEX50384.1}. FT DOMAIN 23..225 FT /note="YjeF N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51385" FT NP_BIND 412..416 FT /note="ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT NP_BIND 432..441 FT /note="ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT REGION 71..75 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT REGION 139..145 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT REGION 375..381 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT METAL 72 FT /note="Potassium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT METAL 135 FT /note="Potassium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT METAL 171 FT /note="Potassium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 150 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 168 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 329 FT /note="NAD(P)HX; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 442 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" SQ SEQUENCE 504 AA; 53247 MW; 45E3B22A5B00173A CRC64; MTNQREKRNE ASLPHSVFSA DWLRQAERQA AQETGISLFT LMQRAAKAAF SLAQREFPQM RHWLILCGHG NNGGDGFEVA RLAKNAGIRV TLLAVAGSKP LPEEAEAARE GWLKSGGTVN PADSAWPQDA DLIIDGLLGT GLSSAPRAPY DGLIDAINSA SLPVISLDIP SGLDAQTGQT AGKAVHATHT LSFIALKPGL LTGQARDYTG KLHCDALGLE SWLGGHLAPL QRLDATQLGQ WLHPRRPCSH KGEHGRLLVI GGDTGFAGAI RMASEAALRS GAGLVRVLTH KEHAGPLLTA RPELMVQELT AESLDESLEW ADVLVIGPGL GQKEWGKQAI ERVAKWDKPA LWDADALNLL AINPRKRQNR VLTPHPGEAA RLLGCSVKDI ESDRLLSARN LTQRYGGVVV LKGAGTLIAS ERGEMAVADV GNAGMASGGM GDVLSGIIGG LLAQKLNIYD AACAGSVVHG AAADEIAHRQ GTRGMLATDL LAVIAPLVNP DLKK //