ID A0A0M3RIU9_9FLAO Unreviewed; 487 AA. AC A0A0M3RIU9; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 13-SEP-2023, entry version 45. 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=AM608_08180 {ECO:0000313|EMBL:ALC97622.1}; OS Capnocytophaga sp. oral taxon 323. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=1705617 {ECO:0000313|EMBL:ALC97622.1, ECO:0000313|Proteomes:UP000068952}; RN [1] {ECO:0000313|EMBL:ALC97622.1, ECO:0000313|Proteomes:UP000068952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0383 {ECO:0000313|EMBL:ALC97622.1, RC ECO:0000313|Proteomes:UP000068952}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A., RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D., RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C., RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V., RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A., RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L., RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H., RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.; RL Submitted (AUG-2015) 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; CP012589; ALC97622.1; -; Genomic_DNA. DR RefSeq; WP_053581390.1; NZ_CP012589.1. DR AlphaFoldDB; A0A0M3RIU9; -. DR EnsemblBacteria; ALC97622; ALC97622; AM608_08180. DR KEGG; col:AM608_08180; -. DR PATRIC; fig|1705617.3.peg.1726; -. DR OrthoDB; 9806925at2; -. DR Proteomes; UP000068952; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd01171; YXKO-related; 1. DR Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 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 NCBIfam; TIGR00196; yjeF_cterm; 1. DR NCBIfam; TIGR00197; yjeF_nterm; 1. DR PANTHER; PTHR12592:SF0; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE; 1. DR PANTHER; PTHR12592; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER; 1. DR Pfam; PF01256; Carb_kinase; 1. DR Pfam; PF03853; YjeF_N; 1. DR PIRSF; PIRSF017184; Nnr; 1. DR SUPFAM; SSF53613; Ribokinase-like; 1. DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 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|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:ALC97622.1}; 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|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:ALC97622.1}. FT DOMAIN 9..215 FT /note="YjeF N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51385" FT DOMAIN 224..487 FT /note="YjeF C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51383" FT BINDING 57..61 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966" FT BINDING 58 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 128..134 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" 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 322 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 374 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 409..413 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 437 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 438 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" SQ SEQUENCE 487 AA; 53566 MW; FF1828F166302050 CRC64; MKILNTQQMR EADAHTISAE GITSWQLMER AATKLFEWIK EHLPKERTVT VLAGTGNNGG DGLALARMLI ADGWQVNTYL LCFSEHLSPD CQQNKELLEA QGIAIAEIRA EQVNNITFGK IVIDAAFGIG LNRPAPKWIQ QIFGNLNNSN SYILSVDMPS GLPTERIPSP EEIWVHPHQV LTFQTPKLPF FLPSTGCYIR KWEVLNIGLD EHFLKTLHPD FYYLESDIQQ LQRRRAKFSH KGTYGHALLV GGSYGKIGAV VLSGTAVLRA GAGLLTVAIP QCGYNILQTA LPEAMVLTCE EEKHYKTVEI SFTPSAIGVG IGWGTHPETA SALFGLFQQY PDTPFVIDAD ALNILAQHPE QLKTLPKNAI LTPHPKELER LIGKWDDDLH KLTKAKAFAK EHKVILLIKG AYTMMTDGEK YWINSSGNAG MATAGSGDVL TGMLTGLRAQ GYSAVEAACL GVFLHGLQGD RAAKKMGMER LIARDLL //