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NNRE_ISOPI
ID   NNRE_ISOPI              Reviewed;         272 AA.
AC   E8R1E4;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=Isop_1778;
OS   Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B).
OC   Bacteria; Planctomycetes; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Isosphaera.
OX   NCBI_TaxID=575540;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43644 / DSM 9630 / IS1B;
RX   PubMed=21475588; DOI=10.4056/sigs.1533840;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Isosphaera pallida type strain (IS1B).";
RL   Stand. Genomic Sci. 4:63-71(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; CP002353; ADV62361.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8R1E4; -.
DR   SMR; E8R1E4; -.
DR   STRING; 575540.Isop_1778; -.
DR   PRIDE; E8R1E4; -.
DR   EnsemblBacteria; ADV62361; ADV62361; Isop_1778.
DR   KEGG; ipa:Isop_1778; -.
DR   eggNOG; COG0062; Bacteria.
DR   HOGENOM; CLU_024853_0_1_0; -.
DR   OMA; SMFRGRY; -.
DR   Proteomes; UP000008631; 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..272
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416354"
FT   DOMAIN          47..266
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         102..106
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         103
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         176
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         180..186
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         209
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         212
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
SQ   SEQUENCE   272 AA;  29448 MW;  16B4C70927E310A2 CRC64;
     MIRGRKRDGT VHARPDVCLS SMDDFFLRKP PAMDESPRLR PLSRAEARNL DLRAVRELGL
     PTLVLMENAG RSAARWFLED WLSQGKGNLT DHKVLILCGP GSNGGDGGVM ARWLDLAGVL
     VRVAWVSGPV PRLPAGDAAI QRDALAKAGF DQQDWVLPED NAKLAKSLSW CTWVVDALLG
     TGLTRPIDGA FRTAVEMIND SGKPVYALDL PSGLDADTGE PLGVALRATA TATFVAPKLA
     CQYKEAEEYL GEVAVLPIGL PYALLEDYIE ED
 
 
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