NNRD_HUMAN
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 03-AUG-2022, entry version 146.
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;
CC Evidence={ECO:0000255|HAMAP-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}.
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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; 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; 75.
DR IntAct; Q8IW45; 27.
DR MINT; Q8IW45; -.
DR STRING; 9606.ENSP00000311984; -.
DR GlyGen; Q8IW45; 2 sites.
DR iPTMnet; Q8IW45; -.
DR MetOSite; Q8IW45; -.
DR PhosphoSitePlus; Q8IW45; -.
DR BioMuta; NAXD; -.
DR DMDM; 74728128; -.
DR EPD; Q8IW45; -.
DR jPOST; Q8IW45; -.
DR MassIVE; Q8IW45; -.
DR MaxQB; Q8IW45; -.
DR PaxDb; Q8IW45; -.
DR PeptideAtlas; Q8IW45; -.
DR PRIDE; Q8IW45; -.
DR ProteomicsDB; 70807; -. [Q8IW45-1]
DR ProteomicsDB; 70808; -. [Q8IW45-2]
DR ProteomicsDB; 70809; -. [Q8IW45-3]
DR ProteomicsDB; 70810; -. [Q8IW45-4]
DR Antibodypedia; 2137; 64 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 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; HIPHTNE; -.
DR PhylomeDB; Q8IW45; -.
DR TreeFam; TF300116; -.
DR BioCyc; MetaCyc:ENSG00000153481-MON; -.
DR BRENDA; 4.2.1.93; 2681.
DR PathwayCommons; Q8IW45; -.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR SignaLink; Q8IW45; -.
DR BioGRID-ORCS; 55739; 11 hits in 1076 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 205 other tissues.
DR ExpressionAtlas; Q8IW45; baseline and differential.
DR Genevisible; Q8IW45; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro.
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 Pfam; PF01256; Carb_kinase; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
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
