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NNRE_TRURR
ID   NNRE_TRURR              Reviewed;         220 AA.
AC   D7CWZ0;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_01966};
DE            EC=5.1.99.6 {ECO:0000255|HAMAP-Rule:MF_01966};
DE   AltName: Full=NAD(P)HX epimerase {ECO:0000255|HAMAP-Rule:MF_01966};
GN   Name=nnrE {ECO:0000255|HAMAP-Rule:MF_01966}; OrderedLocusNames=Trad_1376;
OS   Truepera radiovictrix (strain DSM 17093 / CIP 108686 / LMG 22925 / RQ-24).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Trueperales; Trueperaceae;
OC   Truepera.
OX   NCBI_TaxID=649638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Truepera radiovictris DSM 17093.";
RL   Submitted (MAY-2010) 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_01966}.
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:0000255|HAMAP-Rule:MF_01966};
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:0000255|HAMAP-Rule:MF_01966};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01966};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01966};
CC   -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01966}.
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DR   EMBL; CP002049; ADI14498.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7CWZ0; -.
DR   SMR; D7CWZ0; -.
DR   STRING; 649638.Trad_1376; -.
DR   EnsemblBacteria; ADI14498; ADI14498; Trad_1376.
DR   KEGG; tra:Trad_1376; -.
DR   eggNOG; COG0062; Bacteria.
DR   HOGENOM; CLU_024853_0_1_0; -.
DR   Proteomes; UP000000379; Chromosome.
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   Pfam; PF03853; YjeF_N; 1.
DR   SUPFAM; SSF64153; SSF64153; 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..220
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416379"
FT   DOMAIN          6..203
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         53..57
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         54
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         116
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         120..126
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         149
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         152
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
SQ   SEQUENCE   220 AA;  22930 MW;  52B35B052F63D97A CRC64;
     MSAAQARHLT TLATGRYGFE LQTLMERAGE SLAGLAAHLA PDGPVLVVAG RGHNGGVGLA
     AAHCLARARR AVWVVPTHEA ENYSGVPKEL LERLAELPNV RLRSSLPKMK FSCALDAAVG
     MRLEGPPRGR TLDVITVLNN LGCKVLSLDV PTGLAADSGE VPGDVVRASA TLALALPKPG
     TPPGGVVGDL YLASFDLPEA LFHDVGLEPF VAPSPWARIV
 
 
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