NNRE_HUMAN
ID NNRE_HUMAN Reviewed; 288 AA.
AC Q8NCW5; B4DGY3; Q496C6; Q5T3I2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
DE EC=5.1.99.6;
DE AltName: Full=Apolipoprotein A-I-binding protein {ECO:0000255|HAMAP-Rule:MF_03159};
DE Short=AI-BP {ECO:0000255|HAMAP-Rule:MF_03159};
DE AltName: Full=NAD(P)HX epimerase {ECO:0000312|HGNC:HGNC:18453};
DE AltName: Full=YjeF N-terminal domain-containing protein 1;
DE Short=YjeF_N1;
DE Flags: Precursor;
GN Name=NAXE {ECO:0000312|HGNC:HGNC:18453};
GN Synonyms=AIBP {ECO:0000255|HAMAP-Rule:MF_03159}, APOA1BP, YJEFN1;
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 [MRNA] (ISOFORM 1), VARIANT LEU-19, TISSUE SPECIFICITY,
RP INTERACTION WITH APOA1 AND APOA2, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=11991719; DOI=10.1006/geno.2002.6761;
RA Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A.,
RA Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G., Schmitz G.;
RT "Cloning and characterization of a novel apolipoprotein A-I-binding
RT protein, AI-BP, secreted by cells of the kidney proximal tubules in
RT response to HDL or ApoA-I.";
RL Genomics 79:693-702(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LEU-19.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP FUNCTION, AND INTERACTION WITH APOA1.
RX PubMed=23719382; DOI=10.1038/nature12166;
RA Fang L., Choi S.H., Baek J.S., Liu C., Almazan F., Ulrich F., Wiesner P.,
RA Taleb A., Deer E., Pattison J., Torres-Vazquez J., Li A.C., Miller Y.I.;
RT "Control of angiogenesis by AIBP-mediated cholesterol efflux.";
RL Nature 498:118-122(2013).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
RP INVOLVEMENT IN PEBEL1, VARIANTS PEBEL1 VAL-218 AND LYS-270 DEL, AND
RP FUNCTION.
RX PubMed=27616477; DOI=10.1016/j.ajhg.2016.07.018;
RA Kremer L.S., Danhauser K., Herebian D., Petkovic Ramadza D.,
RA Piekutowska-Abramczuk D., Seibt A., Mueller-Felber W., Haack T.B.,
RA Ploski R., Lohmeier K., Schneider D., Klee D., Rokicki D., Mayatepek E.,
RA Strom T.M., Meitinger T., Klopstock T., Pronicka E., Mayr J.A., Baric I.,
RA Distelmaier F., Prokisch H.;
RT "NAXE mutations disrupt the cellular NAD(P)HX repair system and cause a
RT lethal neurometabolic disorder of early childhood.";
RL Am. J. Hum. Genet. 99:894-902(2016).
RN [9]
RP VARIANT PEBEL1 ASP-94.
RX PubMed=27122014; DOI=10.1007/s10048-016-0483-3;
RA Spiegel R., Shaag A., Shalev S., Elpeleg O.;
RT "Homozygous mutation in the APOA1BP is associated with a lethal infantile
RT leukoencephalopathy.";
RL Neurogenetics 17:187-190(2016).
RN [10]
RP VARIANT 43-SER--GLN-288 DEL.
RX PubMed=33798445; DOI=10.1016/j.ajhg.2021.03.013;
RA Courage C., Oliver K.L., Park E.J., Cameron J.M., Grabinska K.A., Muona M.,
RA Canafoglia L., Gambardella A., Said E., Afawi Z., Baykan B., Brandt C.,
RA di Bonaventura C., Chew H.B., Criscuolo C., Dibbens L.M., Castellotti B.,
RA Riguzzi P., Labate A., Filla A., Giallonardo A.T., Berecki G.,
RA Jackson C.B., Joensuu T., Damiano J.A., Kivity S., Korczyn A., Palotie A.,
RA Striano P., Uccellini D., Giuliano L., Andermann E., Scheffer I.E.,
RA Michelucci R., Bahlo M., Franceschetti S., Sessa W.C., Berkovic S.F.,
RA Lehesjoki A.E.;
RT "Progressive myoclonus epilepsies-Residual unsolved cases have marked
RT genetic heterogeneity including dolichol-dependent protein glycosylation
RT pathway genes.";
RL Am. J. Hum. Genet. 108:722-738(2021).
CC -!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of
CC NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or
CC heat-dependent hydration. This is a prerequisite for the S-specific
CC NAD(P)H-hydrate dehydratase to allow the repair of both epimers of
CC NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to
CC high-density lipoprotein (HDL) and thereby regulates angiogenesis
CC (PubMed:23719382). {ECO:0000255|HAMAP-Rule:MF_03159,
CC ECO:0000269|PubMed:23719382, ECO:0000269|PubMed:27616477}.
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 -!- 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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03159};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03159};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with APOA1 and APOA2.
CC {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000269|PubMed:11991719,
CC ECO:0000269|PubMed:23719382}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}.
CC Secreted {ECO:0000255|HAMAP-Rule:MF_03159,
CC ECO:0000269|PubMed:11991719}. Note=In sperm, secretion gradually
CC increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NCW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NCW5-2; Sequence=VSP_026417;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC kidney, heart and liver. Present in cerebrospinal fluid and urine but
CC not in serum from healthy patients. Present in serum of sepsis patients
CC (at protein level). {ECO:0000269|PubMed:11991719}.
CC -!- PTM: Undergoes physiological phosphorylation during sperm capacitation,
CC downstream to PKA activation. {ECO:0000255|HAMAP-Rule:MF_03159}.
CC -!- DISEASE: Encephalopathy, progressive, early-onset, with brain edema
CC and/or leukoencephalopathy 1 (PEBEL1) [MIM:617186]: 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:27122014, ECO:0000269|PubMed:27616477}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP-
CC Rule:MF_03159}.
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DR EMBL; AJ315849; CAC86580.1; -; mRNA.
DR EMBL; AK294835; BAG57944.1; -; mRNA.
DR EMBL; AL365181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100931; AAI00932.1; -; mRNA.
DR EMBL; BC100932; AAI00933.1; -; mRNA.
DR EMBL; BC100933; AAI00934.1; -; mRNA.
DR EMBL; BC100934; AAI00935.1; -; mRNA.
DR CCDS; CCDS1145.1; -. [Q8NCW5-1]
DR RefSeq; NP_658985.2; NM_144772.2. [Q8NCW5-1]
DR AlphaFoldDB; Q8NCW5; -.
DR SMR; Q8NCW5; -.
DR BioGRID; 126103; 50.
DR IntAct; Q8NCW5; 5.
DR MINT; Q8NCW5; -.
DR STRING; 9606.ENSP00000357218; -.
DR GlyGen; Q8NCW5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NCW5; -.
DR PhosphoSitePlus; Q8NCW5; -.
DR SwissPalm; Q8NCW5; -.
DR BioMuta; NAXE; -.
DR DMDM; 150438841; -.
DR REPRODUCTION-2DPAGE; IPI00168479; -.
DR CPTAC; CPTAC-25; -.
DR CPTAC; CPTAC-26; -.
DR EPD; Q8NCW5; -.
DR jPOST; Q8NCW5; -.
DR MassIVE; Q8NCW5; -.
DR MaxQB; Q8NCW5; -.
DR PaxDb; Q8NCW5; -.
DR PeptideAtlas; Q8NCW5; -.
DR PRIDE; Q8NCW5; -.
DR ProteomicsDB; 72958; -. [Q8NCW5-1]
DR ProteomicsDB; 72959; -. [Q8NCW5-2]
DR TopDownProteomics; Q8NCW5-1; -. [Q8NCW5-1]
DR TopDownProteomics; Q8NCW5-2; -. [Q8NCW5-2]
DR Antibodypedia; 34221; 220 antibodies from 29 providers.
DR DNASU; 128240; -.
DR Ensembl; ENST00000368235.8; ENSP00000357218.3; ENSG00000163382.13. [Q8NCW5-1]
DR Ensembl; ENST00000679702.1; ENSP00000505913.1; ENSG00000163382.13. [Q8NCW5-1]
DR Ensembl; ENST00000680004.1; ENSP00000506275.1; ENSG00000163382.13. [Q8NCW5-1]
DR Ensembl; ENST00000680269.1; ENSP00000505899.1; ENSG00000163382.13. [Q8NCW5-1]
DR Ensembl; ENST00000681054.1; ENSP00000506192.1; ENSG00000163382.13. [Q8NCW5-1]
DR Ensembl; ENST00000681523.1; ENSP00000505349.1; ENSG00000163382.13. [Q8NCW5-1]
DR GeneID; 128240; -.
DR KEGG; hsa:128240; -.
DR MANE-Select; ENST00000368235.8; ENSP00000357218.3; NM_144772.3; NP_658985.2.
DR UCSC; uc001fph.4; human. [Q8NCW5-1]
DR CTD; 128240; -.
DR DisGeNET; 128240; -.
DR GeneCards; NAXE; -.
DR HGNC; HGNC:18453; NAXE.
DR HPA; ENSG00000163382; Low tissue specificity.
DR MalaCards; NAXE; -.
DR MIM; 608862; gene.
DR MIM; 617186; phenotype.
DR neXtProt; NX_Q8NCW5; -.
DR OpenTargets; ENSG00000163382; -.
DR Orphanet; 555407; NAD(P)HX epimerase deficiency.
DR PharmGKB; PA38538; -.
DR VEuPathDB; HostDB:ENSG00000163382; -.
DR eggNOG; KOG2585; Eukaryota.
DR GeneTree; ENSGT00390000007227; -.
DR HOGENOM; CLU_024853_3_0_1; -.
DR InParanoid; Q8NCW5; -.
DR OMA; TIYYPKP; -.
DR OrthoDB; 1030667at2759; -.
DR PhylomeDB; Q8NCW5; -.
DR TreeFam; TF300197; -.
DR BioCyc; MetaCyc:ENSG00000163382-MON; -.
DR BRENDA; 5.1.99.6; 2681.
DR PathwayCommons; Q8NCW5; -.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR SignaLink; Q8NCW5; -.
DR BioGRID-ORCS; 128240; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; NAXE; human.
DR GenomeRNAi; 128240; -.
DR Pharos; Q8NCW5; Tbio.
DR PRO; PR:Q8NCW5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NCW5; protein.
DR Bgee; ENSG00000163382; Expressed in apex of heart and 183 other tissues.
DR ExpressionAtlas; Q8NCW5; baseline and differential.
DR Genevisible; Q8NCW5; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IBA:GO_Central.
DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0031580; P:membrane raft distribution; IMP:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IMP:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR Gene3D; 3.40.50.10260; -; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR PANTHER; PTHR13232; PTHR13232; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; SSF64153; 1.
DR TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Isomerase; Lipid transport;
KW Metal-binding; Mitochondrion; NAD; NADP; Neurodegeneration;
KW Nucleotide-binding; Phosphoprotein; Potassium; Reference proteome;
KW Secreted; Transit peptide; Transport.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT CHAIN 48..288
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_5000067606"
FT DOMAIN 65..275
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 119..123
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 120
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 189..195
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 218
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4Z3"
FT MOD_RES 144
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4Z3"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026417"
FT VARIANT 19
FT /note="V -> L (in dbSNP:rs7516274)"
FT /evidence="ECO:0000269|PubMed:11991719,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_032992"
FT VARIANT 43..288
FT /note="Missing (found in a patient with progressive
FT myoclonus epilepsy and developmental delay; unknown
FT pathological significance; dbSNP:rs765587923)"
FT /evidence="ECO:0000269|PubMed:33798445"
FT /id="VAR_085045"
FT VARIANT 94
FT /note="A -> D (in PEBEL1; dbSNP:rs879255647)"
FT /evidence="ECO:0000269|PubMed:27122014"
FT /id="VAR_077991"
FT VARIANT 218
FT /note="D -> V (in PEBEL1; dbSNP:rs886041064)"
FT /evidence="ECO:0000269|PubMed:27616477"
FT /id="VAR_077992"
FT VARIANT 270
FT /note="Missing (in PEBEL1; dbSNP:rs897694449)"
FT /evidence="ECO:0000269|PubMed:27616477"
FT /id="VAR_077993"
SQ SEQUENCE 288 AA; 31675 MW; 1D8B04FEC595EA01 CRC64;
MSRLRALLGL GLLVAGSRVP RIKSQTIACR SGPTWWGPQR LNSGGRWDSE VMASTVVKYL
SQEEAQAVDQ ELFNEYQFSV DQLMELAGLS CATAIAKAYP PTSMSRSPPT VLVICGPGNN
GGDGLVCARH LKLFGYEPTI YYPKRPNKPL FTALVTQCQK MDIPFLGEMP AEPMTIDELY
ELVVDAIFGF SFKGDVREPF HSILSVLKGL TVPIASIDIP SGWDVEKGNA GGIQPDLLIS
LTAPKKSATQ FTGRYHYLGG RFVPPALEKK YQLNLPPYPD TECVYRLQ
