NNRE_LEUGG
ID NNRE_LEUGG Reviewed; 223 AA.
AC D8MHV4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=LEGAS_1774;
OS Leuconostoc gelidum subsp. gasicomitatum (strain DSM 15947 / CCUG 46042 /
OS CECT 5767 / JCM 12535 / LMG 18811 / NBRC 113245 / TB1-10).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=762550;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15947 / CCUG 46042 / CECT 5767 / JCM 12535 / LMG 18811 / NBRC
RC 113245 / TB1-10;
RA Johansson P., Paulin L., Vihavainen E.J., Salovuori N., Alatalo E.R.,
RA Bjoerkroth J.K., Auvinen P.;
RT "Genome sequence and comparative genomics of a food spoilage lactic acid
RT bacterium Leuconostoc gasicomitatum 18811T.";
RL Submitted (APR-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; FN822744; CBL92422.1; -; Genomic_DNA.
DR RefSeq; WP_010385385.1; NC_014319.1.
DR AlphaFoldDB; D8MHV4; -.
DR SMR; D8MHV4; -.
DR KEGG; lgs:LEGAS_1774; -.
DR HOGENOM; CLU_024853_0_1_9; -.
DR OMA; IKAANHI; -.
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..223
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_0000416366"
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 223 AA; 23926 MW; B6DAA0709CD2A503 CRC64;
MQLVTASEMQ KIDTYTVNTI GMPQDVLIER AALSVIDVIG AGHFNLEHIL VLAGLGNNGA
DGVAITRLLY AQGFNVSLQF VGNVSRAKES VQRQLAIIEK YGLVRSEKSD FNEATLIIDA
IFGTGLNNLL PEGLQKMIKA ANHIEKTVIA IDTPTGIDAT TGEVRGAALK AHTTVTFGYN
KIGLTRRVGG YLSGNVIVKD IGLLTPPDFS FSDTEENHST KDV
