NNRE_RHOBA
ID NNRE_RHOBA Reviewed; 244 AA.
AC Q7ULX4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=RB9218;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX294149; CAD76143.1; -; Genomic_DNA.
DR RefSeq; NP_868766.1; NC_005027.1.
DR RefSeq; WP_011122200.1; NC_005027.1.
DR AlphaFoldDB; Q7ULX4; -.
DR SMR; Q7ULX4; -.
DR STRING; 243090.RB9218; -.
DR EnsemblBacteria; CAD76143; CAD76143; RB9218.
DR KEGG; rba:RB9218; -.
DR PATRIC; fig|243090.15.peg.4415; -.
DR eggNOG; COG0062; Bacteria.
DR HOGENOM; CLU_024853_0_1_0; -.
DR InParanoid; Q7ULX4; -.
DR OMA; SMFRGRY; -.
DR OrthoDB; 1856227at2; -.
DR Proteomes; UP000001025; 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..244
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_0000416377"
FT DOMAIN 35..240
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 82..86
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 83
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 150
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 154..160
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 165
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 183
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
SQ SEQUENCE 244 AA; 25726 MW; 527CFAFD9EC01063 CRC64;
MSPEVLSARP GFVRNLMDVM MKPVLQLPPM TCQRIREIDS LAMEQFQMPG IILMENAGRG
AAELIEELAP EGNVLILCGK GNNGGDGFTI ARHLQLAGRE VMILAMAATN ELQGDAAIQA
KIAEAAGIKI QVVGEAVEAG RLPATDIVVD GLLGTGAKPP LRGRYAEVVE AANASSAIRI
ALDIPTGMNG DTGETGETTF RADHTLTFAA PKVGFEKLGA ARFTGEVHVI SIGVPLELLR
QFSV
