ID   NNRE_ROSLO              Reviewed;         227 AA.
AC   F7ZKE9;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
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};
GN   OrderedLocusNames=RLO149_c019840;
OS   Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS   15278 / OCh 149).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=391595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149;
RX   PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA   Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA   Daniel R., Simon M., Brinkhoff T.;
RT   "Comparative genome analysis and genome-guided physiological analysis of
RT   Roseobacter litoralis.";
RL   BMC Genomics 12:324-324(2011).
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; CP002623; AEI93968.1; -; Genomic_DNA.
DR   RefSeq; WP_013961896.1; NC_015730.1.
DR   AlphaFoldDB; F7ZKE9; -.
DR   SMR; F7ZKE9; -.
DR   STRING; 391595.RLO149_c019840; -.
DR   EnsemblBacteria; AEI93968; AEI93968; RLO149_c019840.
DR   KEGG; rli:RLO149_c019840; -.
DR   eggNOG; COG0062; Bacteria.
DR   HOGENOM; CLU_024853_0_1_5; -.
DR   OMA; WEAVFPE; -.
DR   OrthoDB; 1748633at2; -.
DR   Proteomes; UP000001353; 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   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.
FT   CHAIN           1..227
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416378"
FT   DOMAIN          10..227
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         62..66
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         63
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         142
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         146..152
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         176
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         179
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
SQ   SEQUENCE   227 AA;  24457 MW;  6413976D7D565651 CRC64;
     MPDILTASQM RALETAAFNS GAVTGLELME RAGQSVIDAL FSSKAELATG EHRAVILCGP
     GNNGGDGFVI ARLLFVLGWQ VRVYLYADPE KMPRDAHANH DSWVDLVPEC TQRISFPSVL
     PAEAERFGDE AFGNGEVDVI VDALFGIGLN RPLSGLHPIL ATCHANRHEA YFVAVDVPSG
     LGENGPLEAA DWSVFPADLT VTFHRPKQAH QNGLSFCGKI MVQYIGL