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NNRE_PEDHC
ID   NNRE_PEDHC              Reviewed;         228 AA.
AC   E0V9D8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
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=PHUM009640;
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA;
RX   PubMed=20566863; DOI=10.1073/pnas.1003379107;
RA   Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A., Clark J.M.,
RA   Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E., Gerlach D.,
RA   Kriventseva E.V., Elsik C.G., Graur D., Hill C.A., Veenstra J.A.,
RA   Walenz B., Tubio J.M., Ribeiro J.M., Rozas J., Johnston J.S., Reese J.T.,
RA   Popadic A., Tojo M., Raoult D., Reed D.L., Tomoyasu Y., Krause E.,
RA   Mittapalli O., Margam V.M., Li H.M., Meyer J.M., Johnson R.M.,
RA   Romero-Severson J., Vanzee J.P., Alvarez-Ponce D., Vieira F.G., Aguade M.,
RA   Guirao-Rico S., Anzola J.M., Yoon K.S., Strycharz J.P., Unger M.F.,
RA   Christley S., Lobo N.F., Seufferheld M.J., Wang N., Dasch G.A.,
RA   Struchiner C.J., Madey G., Hannick L.I., Bidwell S., Joardar V., Caler E.,
RA   Shao R., Barker S.C., Cameron S., Bruggner R.V., Regier A., Johnson J.,
RA   Viswanathan L., Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M.,
RA   Venter J.C., Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M.,
RA   Pittendrigh B.R.;
RT   "Genome sequences of the human body louse and its primary endosymbiont
RT   provide insights into the permanent parasitic lifestyle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010).
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; DS234992; EEB09994.1; -; Genomic_DNA.
DR   RefSeq; XP_002422732.1; XM_002422687.1.
DR   AlphaFoldDB; E0V9D8; -.
DR   SMR; E0V9D8; -.
DR   STRING; 121224.E0V9D8; -.
DR   EnsemblMetazoa; PHUM009640-RA; PHUM009640-PA; PHUM009640.
DR   GeneID; 8233693; -.
DR   KEGG; phu:Phum_PHUM009640; -.
DR   CTD; 8233693; -.
DR   VEuPathDB; VectorBase:PHUM009640; -.
DR   eggNOG; KOG2585; Eukaryota.
DR   HOGENOM; CLU_024853_3_0_1; -.
DR   InParanoid; E0V9D8; -.
DR   OMA; SMFRGRY; -.
DR   PhylomeDB; E0V9D8; -.
DR   Proteomes; UP000009046; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
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..228
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416320"
FT   DOMAIN          10..214
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         58..62
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         59
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         123
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         127..133
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         156
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         159
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
SQ   SEQUENCE   228 AA;  25777 MW;  6FDDCC1245C355F7 CRC64;
     MVRYLSQQEA IDIDQELFNV YKYSVDQLME LAGLSCSIAI YKCYSKLKKI LVCCGPGNNG
     GDGLVAARHL KLFGFEPSVY YPKRTEKPLY QNLTHQCLAM KIDFLNDIPD AKEMSNNYEL
     IVDALFGFSF KPPVRPEFEK VMNVLGKSKV PICSIDIPSG WDVENGCPEN GILPDMLISL
     TAPKKCAKFF NGRFHYLGGR FVPPDLERKY DLKINSEYSG TECCVQLK
 
 
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