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NNRE_CAEEL
ID   NNRE_CAEEL              Reviewed;         235 AA.
AC   Q9XW15;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
DE            EC=5.1.99.6;
DE   AltName: Full=NAD(P)HX epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
GN   ORFNames=Y18D10A.3 {ECO:0000312|WormBase:Y18D10A.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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. {ECO:0000255|HAMAP-Rule:MF_03159}.
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   -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP-
CC       Rule:MF_03159}.
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DR   EMBL; BX284601; CAA22319.2; -; Genomic_DNA.
DR   PIR; T26528; T26528.
DR   RefSeq; NP_493241.1; NM_060840.1.
DR   AlphaFoldDB; Q9XW15; -.
DR   SMR; Q9XW15; -.
DR   STRING; 6239.Y18D10A.3; -.
DR   EPD; Q9XW15; -.
DR   PaxDb; Q9XW15; -.
DR   PeptideAtlas; Q9XW15; -.
DR   EnsemblMetazoa; Y18D10A.3.1; Y18D10A.3.1; WBGene00012476.
DR   UCSC; Y18D10A.3; c. elegans.
DR   WormBase; Y18D10A.3; CE53972; WBGene00012476; -.
DR   eggNOG; KOG2585; Eukaryota.
DR   GeneTree; ENSGT00390000007227; -.
DR   HOGENOM; CLU_024853_3_0_1; -.
DR   InParanoid; Q9XW15; -.
DR   OrthoDB; 1030667at2759; -.
DR   Reactome; R-CEL-197264; Nicotinamide salvaging.
DR   PRO; PR:Q9XW15; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00012476; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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   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   3: Inferred from homology;
KW   Isomerase; Metal-binding; NAD; NADP; Nucleotide-binding; Potassium;
KW   Reference proteome.
FT   CHAIN           1..235
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416313"
FT   DOMAIN          18..221
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         65..69
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         66
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         127
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         131..137
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         160
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         163
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
SQ   SEQUENCE   235 AA;  25759 MW;  F4CB6EE8973B077E CRC64;
     MVHIISKKTV SFIGQKLAAQ IDEQLFTKYG FKVEQLMELA GLAAAQAIAA HYPKSNVAVL
     CGPGNNGGDG FVCARHLQQF GFTPSIVYPK ESRNELMKSL VVQCETSSIP ITATLPTNLQ
     AFPLIVDALF GFSFHPPTRE PFTEMLKTVR ASGIHVFSID VPSGWDVELG APSGNDDDVI
     HPHSVISLTL PKLCMKNWTG PHFLGGRFVP KSLVDEHELL MPQYPGFEQI VKLED
 
 
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