ID A0A3Q9UJF7_9ACTN Unreviewed; 490 AA. AC A0A3Q9UJF7; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 02-JUN-2021, entry version 12. DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_01965}; DE EC=4.2.1.136 {ECO:0000256|HAMAP-Rule:MF_01965}; DE AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_01965}; GN Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965}; GN ORFNames=C0Z10_03360 {ECO:0000313|EMBL:AZZ38947.1}; OS Acidipropionibacterium jensenii. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Acidipropionibacterium. OX NCBI_TaxID=1749 {ECO:0000313|EMBL:AZZ38947.1, ECO:0000313|Proteomes:UP000285875}; RN [1] {ECO:0000313|Proteomes:UP000285875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS280 {ECO:0000313|Proteomes:UP000285875}; RA Deptula P., Laine P., Smolander O.-P., Paulin L., Auvinen P., Varmanen P.; RT "Whole genome sequencing of Acidipropionibacterium jensenii strains JS279 RT and JS280."; RL Submitted (DEC-2017) 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 -!- 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, CC 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, CC 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|PIRNR:PIRNR017184}; CC Note=Binds 1 potassium ion per subunit. CC {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: 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; CP025570; AZZ38947.1; -; Genomic_DNA. DR EnsemblBacteria; AZZ38947; AZZ38947; C0Z10_03360. DR KEGG; aji:C0Z10_03360; -. DR Proteomes; UP000285875; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-EC. 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 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 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|PIRNR:PIRNR017184}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184}; KW Metal-binding {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}; Potassium {ECO:0000256|PIRNR:PIRNR017184}. FT DOMAIN 10..216 FT /note="YjeF N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51385" FT NP_BIND 386..390 FT /note="ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT NP_BIND 406..415 FT /note="ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT REGION 349..355 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 305 FT /note="NAD(P)HX; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 416 FT /note="NAD(P)HX" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" SQ SEQUENCE 490 AA; 50020 MW; A11346860CF51A17 CRC64; MTTVCTAEQM RTAERAFFDA HPGADLMAVA AHAAATTAVT MLLGDEPLEE SAEWIAQQRV LVMAGTGNNG ADGLFAAAEL CRDGWVVDVC PVLGSLHEAG AAAAQEAGCG EVSPVDALDR HYDLAIDAVL GIGGRPSIPD CLARLDEALA GADTPVLAVD LPSGLSADSG EVVRCVHART TVTFASRKWC HLARPAAACC GRVILADIGV TVPDADQVAS VTDLADLWPV PGPASDKYSR GVVGCDTGSS QYPGAGVLGV LGALRSGAGM VRCVGPDAVR QHVMDRTPSV VCADGRVQAW VVGSGWGDDA GNAARLDRRL ADGVPVVVDA DALAVLPRRI PEGCLLTPHA GELARMLGID RAEVEADRRG SCLAGARMFG ATVLLKGSIQ WVATPDQQIS AALPGPAWTA QAGSGDTLAG VCGTLLAAGL SARDAGLAGA GLQALAAICN PGPWSPDQLA DRFPEVIARL VAPGPAGAAE REFVEREFSA //