ID NNRD_COPC7 Reviewed; 336 AA. AC A8N8Z0; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 2. DT 27-MAR-2024, entry version 69. DE RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157}; DE EC=4.2.1.93 {ECO:0000255|HAMAP-Rule:MF_03157}; DE AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157}; GN ORFNames=CC1G_00865; OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) OS (Inky cap fungus) (Hormographiella aspergillata). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis. OX NCBI_TaxID=240176; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003; RX PubMed=20547848; DOI=10.1073/pnas.1003391107; RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M., RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S., RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J., RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C., RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J., RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O., RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M., RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q., RA Zolan M.E., Pukkila P.J.; RT "Insights into evolution of multicellular fungi from the assembled RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus)."; RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010). CC -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the CC expense of ATP, which is converted to ADP. 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:0000255|HAMAP-Rule:MF_03157}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate; CC Xref=Rhea:RHEA:19017, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, CC ChEBI:CHEBI:456216; EC=4.2.1.93; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03157}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-NADPHX + ATP = ADP + H(+) + NADPH + phosphate; CC Xref=Rhea:RHEA:32231, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, CC ChEBI:CHEBI:456216; EC=4.2.1.93; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03157}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03157}. CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP- CC Rule:MF_03157}. 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; AACS02000007; EAU90481.2; -; Genomic_DNA. DR RefSeq; XP_001831318.2; XM_001831266.2. DR AlphaFoldDB; A8N8Z0; -. DR SMR; A8N8Z0; -. DR STRING; 240176.A8N8Z0; -. DR GeneID; 6007789; -. DR KEGG; cci:CC1G_00865; -. DR VEuPathDB; FungiDB:CC1G_00865; -. DR eggNOG; KOG3974; Eukaryota. DR HOGENOM; CLU_030651_0_0_1; -. DR InParanoid; A8N8Z0; -. DR OMA; WRAAYHN; -. DR OrthoDB; 1123001at2759; -. DR Proteomes; UP000001861; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule. 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; 2. 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; Cytoplasm; Lyase; NAD; NADP; Nucleotide-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1..336 FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase" FT /id="PRO_0000416182" FT DOMAIN 7..328 FT /note="YjeF C-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 111 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 164..170 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 202..206 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 244..253 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 254 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" SQ SEQUENCE 336 AA; 35595 MW; 44F2F2B46A6B8EDC CRC64; MPIPRTIIEQ IKRIIPPLDG SLHKGQSGRV GVLGGALDYT GAPFFAAFSA LRFGVDLSHV ICAPTAAGAI KSYSPDLIVH PILNESSSVD KVKSELQSLL SRLHVLVVGP GLGREPYMQS YARLAISLVR ERGMYLVLDA DALFLVGHDL SIIKGYRRAV LTPNVVEFKR LSEQVGVDPD APPDERAGVV SRMLGGVTVL QKGAKDIISV DTTGEEADLS ASHIEGADAE KEKIKETIAV DVEGGLKRCG GQGDVLSGCV GTFMAWGKCY ESGVYGDGTV PTSRVPLLAA VAGSMVTRTT SRRAYAKSGR SLITQDLLSE AGPAFEECFG GDKGRL //