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   27-MAR-2024, entry version 164.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
DE            EC=5.1.99.6 {ECO:0000269|PubMed:27616477};
DE   AltName: Full=Apolipoprotein A-I-binding protein {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000303|PubMed:11991719};
DE            Short=AI-BP {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000303|PubMed:11991719};
DE   AltName: Full=NAD(P)HX epimerase {ECO:0000303|PubMed:27616477};
DE            Short=NAXE {ECO:0000303|PubMed:27616477};
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, FUNCTION,
RP   AND CATALYTIC ACTIVITY.
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 (By similarity) (PubMed:27616477). This is a
CC       prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow
CC       the repair of both epimers of NAD(P)HX (By similarity). Accelerates
CC       cholesterol efflux from endothelial cells to high-density lipoprotein
CC       (HDL) and thereby regulates angiogenesis (PubMed:23719382).
CC       {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000269|PubMed:23719382,
CC       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         Evidence={ECO:0000269|PubMed:27616477};
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         Evidence={ECO:0000305|PubMed:27616477};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-
CC         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; 59.
DR   IntAct; Q8NCW5; 5.
DR   MINT; Q8NCW5; -.
DR   STRING; 9606.ENSP00000357218; -.
DR   GlyGen; Q8NCW5; 2 sites, 2 O-linked glycans (2 sites).
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; 9606-ENSP00000357218; -.
DR   PeptideAtlas; Q8NCW5; -.
DR   ProteomicsDB; 72958; -. [Q8NCW5-1]
DR   ProteomicsDB; 72959; -. [Q8NCW5-2]
DR   Pumba; Q8NCW5; -.
DR   TopDownProteomics; Q8NCW5-1; -. [Q8NCW5-1]
DR   TopDownProteomics; Q8NCW5-2; -. [Q8NCW5-2]
DR   Antibodypedia; 34221; 237 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   AGR; HGNC:18453; -.
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; RHLFHYG; -.
DR   OrthoDB; 1493at2759; -.
DR   PhylomeDB; Q8NCW5; -.
DR   TreeFam; TF300197; -.
DR   BioCyc; MetaCyc:ENSG00000163382-MONOMER; -.
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 1147 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 185 other cell types or tissues.
DR   ExpressionAtlas; Q8NCW5; baseline and differential.
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: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; YjeF N-terminal domain; 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   NCBIfam; TIGR00197; yjeF_nterm; 1.
DR   PANTHER; PTHR13232; NAD(P)H-HYDRATE EPIMERASE; 1.
DR   PANTHER; PTHR13232:SF11; NAD(P)H-HYDRATE EPIMERASE; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
DR   Genevisible; Q8NCW5; HS.
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; uncertain
FT                   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
//