ID A0A3M0PF03_9LACO Unreviewed; 282 AA. AC A0A3M0PF03; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 24-JAN-2024, entry version 17. 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=F5ESL0259_05765 {ECO:0000313|EMBL:RMC60532.1}; OS Lactobacillus sp. ESL0259. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=2069346 {ECO:0000313|EMBL:RMC60532.1, ECO:0000313|Proteomes:UP000281651}; RN [1] {ECO:0000313|EMBL:RMC60532.1, ECO:0000313|Proteomes:UP000281651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ESL0259 {ECO:0000313|EMBL:RMC60532.1, RC ECO:0000313|Proteomes:UP000281651}; RA Ellegaard K.M., Brochet S., Bonilla-Rosso G., Emery O., Glover N., RA Hadadi N., Jaron K.S., Van Der Meer J.R., Sentchilo V., Tagini F., RA Sage Class S., Engel P.; RT "Genomic changes underlying host specialization in the bee gut symbiont RT Lactobacillus Firm5."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. 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=(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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965}; 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01965}; 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 -!- 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:RMC60532.1}. 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; REHP01000008; RMC60532.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3M0PF03; -. DR Proteomes; UP000281651; 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-KW. 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 HAMAP; MF_01965; NADHX_dehydratase; 1. DR InterPro; IPR017953; Carbohydrate_kinase_pred_CS. DR InterPro; IPR000631; CARKD. DR InterPro; IPR029056; Ribokinase-like. DR NCBIfam; TIGR00196; yjeF_cterm; 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 SUPFAM; SSF53613; Ribokinase-like; 1. DR PROSITE; PS01050; YJEF_C_2; 1. DR PROSITE; PS51383; YJEF_C_3; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01965}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01965}; 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|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01965}. FT DOMAIN 5..278 FT /note="YjeF C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51383" FT BINDING 40 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 100 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 153 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 191..195 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 220 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" FT BINDING 221 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965" SQ SEQUENCE 282 AA; 30373 MW; CCAFCA7654B57DF1 CRC64; MSEITAKILT KVIKKRPSNS HKGNYGRILL IGGNENYGGA IIMAAEAALN SGAGLISVAT HPVNLNALHA RNPEVMFIDW RDRNLLNLIT KMDVIVCGPG LGTNFFAHQM MLILCQNVSS NQTLVLDANA LDLIGQDPKL IPTSAGLIVL TPHQMEWQRL SQIRIPYQTD SANLSALKKI FPTQNVILVL KSNRTHVYTS TNEIFVNTSG NPGMATGGMG DTLAGLIGGF IAQFGGTLDP VLAAIYLHSL AGDKIAETDY VVRPTKISAI LPQLMNQYAN KG //