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NNRE_FINM2
ID   NNRE_FINM2              Reviewed;         214 AA.
AC   B0RZQ3;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=FMG_0094;
OS   Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS   (Peptostreptococcus magnus).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT   pathogen.";
RL   DNA Res. 15:39-47(2008).
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; AP008971; BAG07512.1; -; Genomic_DNA.
DR   RefSeq; WP_012290171.1; NC_010376.1.
DR   AlphaFoldDB; B0RZQ3; -.
DR   SMR; B0RZQ3; -.
DR   STRING; 334413.FMG_0094; -.
DR   EnsemblBacteria; BAG07512; BAG07512; FMG_0094.
DR   KEGG; fma:FMG_0094; -.
DR   eggNOG; COG0062; Bacteria.
DR   HOGENOM; CLU_024853_0_1_9; -.
DR   OMA; IKAANHI; -.
DR   OrthoDB; 1748633at2; -.
DR   Proteomes; UP000001319; 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;
KW   Reference proteome.
FT   CHAIN           1..214
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416353"
FT   DOMAIN          9..207
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         55..59
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         56
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         122
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         126..132
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         137
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         155
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         158
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
SQ   SEQUENCE   214 AA;  23914 MW;  A2A9123B68F4F0F5 CRC64;
     MIYVTAEQMR QIDHYTIHEI GIPSIVLMEN AKAQISKHIL DKNFSKAYVF ASVGNNGGDG
     LAVARDIYNA KKYVKVYVIG KLEKASTDFK INYDILKKLD VEIEFVDENT KFDITENDLI
     VDSIFGTGLK RDIEGIYKGV IDMINDSQAF VVSVDMPSGL DSDENKIHNV AVKADLLVTL
     QLPKKSLQDY EGEYVVEPIG IPEKSIKHVL NNAS
 
 
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