ID NNRD_HUMAN Reviewed; 347 AA. AC Q8IW45; B4DXT4; Q5T9X3; Q9H7W1; Q9NVF5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 154. 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, ECO:0000269|PubMed:30576410}; DE AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157}; DE AltName: Full=Carbohydrate kinase domain-containing protein {ECO:0000255|HAMAP-Rule:MF_03157}; DE AltName: Full=NAD(P)HX dehydratase {ECO:0000312|HGNC:HGNC:25576}; GN Name=NAXD {ECO:0000312|HGNC:HGNC:25576}; GN Synonyms=CARKD {ECO:0000255|HAMAP-Rule:MF_03157}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-240. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INVOLVEMENT IN RP PEBEL2, VARIANTS PEBEL2 SER-81 AND CYS-326, AND CHARACTERIZATION OF RP VARIANTS PEBEL2 SER-81 AND CYS-326. RX PubMed=30576410; DOI=10.1093/brain/awy310; RA Van Bergen N.J., Guo Y., Rankin J., Paczia N., Becker-Kettern J., RA Kremer L.S., Pyle A., Conrotte J.F., Ellaway C., Procopis P., Prelog K., RA Homfray T., Baptista J., Baple E., Wakeling M., Massey S., Kay D.P., RA Shukla A., Girisha K.M., Lewis L.E.S., Santra S., Power R., Daubeney P., RA Montoya J., Ruiz-Pesini E., Kovacs-Nagy R., Pritsch M., Ahting U., RA Thorburn D.R., Prokisch H., Taylor R.W., Christodoulou J., Linster C.L., RA Ellard S., Hakonarson H.; RT "NAD(P)HX dehydratase (NAXD) deficiency: a novel neurodegenerative disorder RT exacerbated by febrile illnesses."; RL Brain 142:50-58(2019). 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, ECO:0000269|PubMed:30576410}. 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, ECO:0000269|PubMed:30576410}; 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 Evidence={ECO:0000269|PubMed:30576410}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03157}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8.62 uM for (6S)-NADHX {ECO:0000269|PubMed:30576410}; CC Vmax=8.77 umol/min/mg enzyme with (6S)-NADHX as substrate CC {ECO:0000269|PubMed:30576410}; CC -!- INTERACTION: CC Q8IW45; Q15323: KRT31; NbExp=3; IntAct=EBI-8650724, EBI-948001; CC Q8IW45; O76011: KRT34; NbExp=3; IntAct=EBI-8650724, EBI-1047093; CC Q8IW45; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-8650724, EBI-11749135; CC Q8IW45; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-8650724, EBI-12012928; CC Q8IW45; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-8650724, EBI-10172290; CC Q8IW45; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-8650724, EBI-10171774; CC Q8IW45; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-8650724, EBI-10172052; CC Q8IW45; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-8650724, EBI-3958099; CC Q8IW45; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-8650724, EBI-945833; CC Q8IW45; O43765: SGTA; NbExp=7; IntAct=EBI-8650724, EBI-347996; CC Q8IW45; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-8650724, EBI-744081; CC Q8IW45; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-8650724, EBI-741480; CC Q8IW45; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-8650724, EBI-10173939; CC Q8IW45; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-8650724, EBI-947187; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03157}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8IW45-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IW45-2; Sequence=VSP_033830; CC Name=3; CC IsoId=Q8IW45-3; Sequence=VSP_033829; CC Name=4; CC IsoId=Q8IW45-4; Sequence=VSP_042012; CC -!- DISEASE: Encephalopathy, progressive, early-onset, with brain edema CC and/or leukoencephalopathy, 2 (PEBEL2) [MIM:618321]: An autosomal CC recessive severe neurometabolic disorder characterized by severe CC leukoencephalopathy usually associated with a trivial febrile illness. CC Affected infants tend to show normal early development followed by CC acute psychomotor regression with ataxia, hypotonia, respiratory CC insufficiency, and seizures. Disease course is rapidly progressive, CC leading to coma, global brain atrophy, and death in the first years of CC life. Brain imaging shows multiple abnormalities, including brain edema CC and signal abnormalities in the cortical and subcortical regions. CC {ECO:0000269|PubMed:30576410}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal CC transit peptide but none has been predicted. {ECO:0000255|HAMAP- CC 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; AK001631; BAA91797.1; -; mRNA. DR EMBL; AK024260; BAB14863.1; -; mRNA. DR EMBL; AK302117; BAG63496.1; -; mRNA. DR EMBL; AL139385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471085; EAX09121.1; -; Genomic_DNA. DR EMBL; CH471085; EAX09125.1; -; Genomic_DNA. DR EMBL; BC041028; AAH41028.1; -; mRNA. DR CCDS; CCDS55903.1; -. [Q8IW45-4] DR CCDS; CCDS91836.1; -. [Q8IW45-1] DR CCDS; CCDS9513.1; -. [Q8IW45-2] DR RefSeq; NP_001229810.1; NM_001242881.1. [Q8IW45-1] DR RefSeq; NP_001229811.1; NM_001242882.1. DR RefSeq; NP_001229812.1; NM_001242883.1. [Q8IW45-4] DR RefSeq; NP_060680.2; NM_018210.3. [Q8IW45-2] DR AlphaFoldDB; Q8IW45; -. DR SMR; Q8IW45; -. DR BioGRID; 120857; 76. DR IntAct; Q8IW45; 27. DR MINT; Q8IW45; -. DR STRING; 9606.ENSP00000311984; -. DR GlyCosmos; Q8IW45; 2 sites, No reported glycans. DR GlyGen; Q8IW45; 2 sites. DR iPTMnet; Q8IW45; -. DR MetOSite; Q8IW45; -. DR PhosphoSitePlus; Q8IW45; -. DR SwissPalm; Q8IW45; -. DR BioMuta; NAXD; -. DR DMDM; 74728128; -. DR EPD; Q8IW45; -. DR jPOST; Q8IW45; -. DR MassIVE; Q8IW45; -. DR MaxQB; Q8IW45; -. DR PaxDb; 9606-ENSP00000311984; -. DR PeptideAtlas; Q8IW45; -. DR ProteomicsDB; 70807; -. [Q8IW45-1] DR ProteomicsDB; 70808; -. [Q8IW45-2] DR ProteomicsDB; 70809; -. [Q8IW45-3] DR ProteomicsDB; 70810; -. [Q8IW45-4] DR Pumba; Q8IW45; -. DR Antibodypedia; 2137; 71 antibodies from 16 providers. DR DNASU; 55739; -. DR Ensembl; ENST00000309957.3; ENSP00000311984.2; ENSG00000213995.12. [Q8IW45-2] DR Ensembl; ENST00000424185.7; ENSP00000413191.2; ENSG00000213995.12. [Q8IW45-4] DR Ensembl; ENST00000680505.1; ENSP00000504986.1; ENSG00000213995.12. [Q8IW45-1] DR GeneID; 55739; -. DR KEGG; hsa:55739; -. DR UCSC; uc001vrc.4; human. [Q8IW45-1] DR AGR; HGNC:25576; -. DR CTD; 55739; -. DR DisGeNET; 55739; -. DR GeneCards; NAXD; -. DR HGNC; HGNC:25576; NAXD. DR HPA; ENSG00000213995; Low tissue specificity. DR MalaCards; NAXD; -. DR MIM; 615910; gene. DR MIM; 618321; phenotype. DR neXtProt; NX_Q8IW45; -. DR OpenTargets; ENSG00000213995; -. DR Orphanet; 555402; NAD(P)HX dehydratase deficiency. DR PharmGKB; PA164717652; -. DR VEuPathDB; HostDB:ENSG00000213995; -. DR eggNOG; KOG3974; Eukaryota. DR GeneTree; ENSGT00390000000917; -. DR HOGENOM; CLU_030651_0_1_1; -. DR InParanoid; Q8IW45; -. DR OMA; WRAAYHN; -. DR OrthoDB; 1123001at2759; -. DR PhylomeDB; Q8IW45; -. DR TreeFam; TF300116; -. DR BioCyc; MetaCyc:ENSG00000153481-MONOMER; -. DR BRENDA; 4.2.1.93; 2681. DR PathwayCommons; Q8IW45; -. DR Reactome; R-HSA-197264; Nicotinamide salvaging. DR SABIO-RK; Q8IW45; -. DR SignaLink; Q8IW45; -. DR BioGRID-ORCS; 55739; 16 hits in 1151 CRISPR screens. DR ChiTaRS; NAXD; human. DR GeneWiki; CARKD; -. DR GenomeRNAi; 55739; -. DR Pharos; Q8IW45; Tbio. DR PRO; PR:Q8IW45; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q8IW45; Protein. DR Bgee; ENSG00000213995; Expressed in cardia of stomach and 207 other cell types or tissues. DR ExpressionAtlas; Q8IW45; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; IMP:UniProtKB. DR GO; GO:0110051; P:metabolite repair; IBA:GO_Central. DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome. DR CDD; cd01171; YXKO-related; 1. DR Gene3D; 3.40.1190.20; -; 1. DR HAMAP; MF_01965; NADHX_dehydratase; 1. 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; PS51383; YJEF_C_3; 1. DR Genevisible; Q8IW45; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Disease variant; Glycoprotein; Lyase; KW Mitochondrion; NAD; NADP; Neurodegeneration; Nucleotide-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1..347 FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase" FT /id="PRO_0000337021" FT DOMAIN 53..344 FT /note="YjeF C-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 153 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 206..212 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 246..250 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 265..274 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT BINDING 275 FT /ligand="(6S)-NADPHX" FT /ligand_id="ChEBI:CHEBI:64076" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157" FT MOD_RES 85 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9CZ42" FT CARBOHYD 240 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 297 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..221 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_033829" FT VAR_SEQ 1..129 FT /note="MVTRAGAGTAVAGAVVVALLSAALALYGPPLDAVLERAFSLRKAHSIKDMEN FT TLQLVRNIIPPLSSTKHKGQDGRIGVVGGCQEYTGAPYFAAISALKVGADLSHVFCASA FT AAPVIKAYSPELIVHPVL -> MLPDGPGSSLWGNPGLQTS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042012" FT VAR_SEQ 299..347 FT /note="SSPLLVAAFGACSLTRQCNHQAFQKHGRSTTTSDMIAEVGAAFSKLFET -> FT GISDLKLTIWGPEIETGVKTRAQGSCGPRTTTPTSPHLLLSPSPQVQPSPGGRVWRLLS FT HQAVQPPSLPEARSLHHHLRHDRRGGGRLQQAL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_033830" FT VARIANT 81 FT /note="G -> S (in PEBEL2; decreased reaction kinetics for FT ATP-dependent NAD(P)H-hydrate dehydratase activity; FT decreased affinity for (6S)-NADHX; changed ATP-dependent FT NAD(P)H-hydrate dehydratase activity; thermostability FT assays show that activity is lost at temperatures above 30 FT degrees Celsius; dbSNP:rs1566614549)" FT /evidence="ECO:0000269|PubMed:30576410" FT /id="VAR_082224" FT VARIANT 140 FT /note="K -> E (in dbSNP:rs3742191)" FT /id="VAR_043564" FT VARIANT 149 FT /note="V -> I (in dbSNP:rs3742192)" FT /id="VAR_043565" FT VARIANT 152 FT /note="P -> T (in dbSNP:rs1044112)" FT /id="VAR_043566" FT VARIANT 326 FT /note="R -> C (in PEBEL2; decreased reaction kinetics for FT ATP-dependent NAD(P)H-hydrate dehydratase activity; FT decreased affinity for (6S)-NADHX; changed ATP-dependent FT NAD(P)H-hydrate dehydratase activity; thermostability FT assays show that activity is lost at temperatures above 30 FT degrees Celsius; dbSNP:rs767778853)" FT /evidence="ECO:0000269|PubMed:30576410" FT /id="VAR_082225" FT CONFLICT 206 FT /note="N -> D (in Ref. 1; BAA91797)" FT /evidence="ECO:0000305" FT CONFLICT 253 FT /note="S -> P (in Ref. 1; BAB14863)" FT /evidence="ECO:0000305" SQ SEQUENCE 347 AA; 36576 MW; 70D42B97D6E8A41B CRC64; MVTRAGAGTA VAGAVVVALL SAALALYGPP LDAVLERAFS LRKAHSIKDM ENTLQLVRNI IPPLSSTKHK GQDGRIGVVG GCQEYTGAPY FAAISALKVG ADLSHVFCAS AAAPVIKAYS PELIVHPVLD SPNAVHEVEK WLPRLHALVV GPGLGRDDAL LRNVQGILEV SKARDIPVVI DADGLWLVAQ QPALIHGYRK AVLTPNHVEF SRLYDAVLRG PMDSDDSHGS VLRLSQALGN VTVVQKGERD ILSNGQQVLV CSQEGSSRRC GGQGDLLSGS LGVLVHWALL AGPQKTNGSS PLLVAAFGAC SLTRQCNHQA FQKHGRSTTT SDMIAEVGAA FSKLFET //