NNRE_LEUKI
ID NNRE_LEUKI Reviewed; 225 AA.
AC D5T3F2;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=LKI_06305;
OS Leuconostoc kimchii (strain IMSNU 11154 / KCTC 2386 / IH25).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=762051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMSNU 11154 / KCTC 2386 / IH25;
RX PubMed=20494991; DOI=10.1128/jb.00508-10;
RA Oh H.M., Cho Y.J., Kim B.K., Roe J.H., Kang S.O., Nahm B.H., Jeong G.,
RA Han H.U., Chun J.;
RT "Complete genome sequence analysis of Leuconostoc kimchii IMSNU 11154.";
RL J. Bacteriol. 192:3844-3845(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_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; CP001758; ADG40801.1; -; Genomic_DNA.
DR RefSeq; WP_013103396.1; NC_014136.1.
DR AlphaFoldDB; D5T3F2; -.
DR SMR; D5T3F2; -.
DR STRING; 762051.LKI_06305; -.
DR EnsemblBacteria; ADG40801; ADG40801; LKI_06305.
DR KEGG; lki:LKI_06305; -.
DR PATRIC; fig|762051.18.peg.1270; -.
DR eggNOG; COG0062; Bacteria.
DR HOGENOM; CLU_024853_0_1_9; -.
DR OrthoDB; 1856227at2; -.
DR Proteomes; UP000002362; 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..225
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_0000416367"
FT DOMAIN 9..209
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 57..61
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 58
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 119
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 123..129
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 152
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 155
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
SQ SEQUENCE 225 AA; 24015 MW; 273457DA76A74D4A CRC64;
MQLVTAAEMQ TIDNYTVETI GMPQDVLIER AAMSVIDVIG AGHFNLDHIL VLAGLGNNGA
DGVAISRLLY AQGFNVSLQF VGNVTRAKDS VKRQLDIIEK YGLVRAEKSD FNEATLIIDA
IFGTGLNNLL PEGLQKMIKA ANHIEKTVIA VDTPTGIDAT TGEVRGAALK AHTTVTFGYN
KIGLTQRVGG YLSGNVIVKD IGLLTPQDFN FSLPDKENSP SVATS
