ID   NNRE_IXOSC              Reviewed;         275 AA.
AC   B7QDG3;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=ISCW022186;
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel;
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; DS913224; EEC16885.1; -; Genomic_DNA.
DR   RefSeq; XP_002413577.1; XM_002413532.1.
DR   AlphaFoldDB; B7QDG3; -.
DR   SMR; B7QDG3; -.
DR   STRING; 6945.B7QDG3; -.
DR   GeneID; 8039603; -.
DR   KEGG; isc:IscW_ISCW022186; -.
DR   VEuPathDB; VectorBase:ISCI022186; -.
DR   VEuPathDB; VectorBase:ISCW022186; -.
DR   HOGENOM; CLU_024853_3_0_1; -.
DR   InParanoid; B7QDG3; -.
DR   OMA; TIYYPKP; -.
DR   OrthoDB; 1030667at2759; -.
DR   PhylomeDB; B7QDG3; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
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..275
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416319"
FT   DOMAIN          49..258
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         102..106
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         103
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         167
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         171..177
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         200
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         203
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
SQ   SEQUENCE   275 AA;  30463 MW;  597FF01E78C49F37 CRC64;
     MEKSEKKPMR FSFRRRPKSV SVDRSEAHAA DVSIGQYLEK LNYVSQEEAI KIDQELFSEY
     AYSVDQLMEL AGLSVATAVA KSYPRGPMPK GGTVLVCCGP GNNGGDGLVC ARHLKLFGYE
     PSVFYPKQSN KPLFQNLTKQ CQEMEVPFLS FLPDSQLVSD SYNLVVDALF GFSFKPPVRP
     EFNDVMDKLK KVKIPVVSID IPSGWDVETG GDADSLQPEC LVSLTAPKRC SRNFKGRFHW
     LGGRFVPPAL AAKYELNLPP YPGTDCCLLL TPPPS