NNRE_ANAPD
ID NNRE_ANAPD Reviewed; 218 AA.
AC C7RGH4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=Apre_0539;
OS Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806
OS / PC1) (Peptostreptococcus prevotii) (Peptococcus prevotii).
OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806 / PC1;
RX PubMed=21304652; DOI=10.4056/sigs.24194;
RA Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Detter J.C., Han C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Anaerococcus prevotii type strain (PC1).";
RL Stand. Genomic Sci. 1:159-165(2009).
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; CP001708; ACV28585.1; -; Genomic_DNA.
DR RefSeq; WP_015777496.1; NC_013171.1.
DR AlphaFoldDB; C7RGH4; -.
DR SMR; C7RGH4; -.
DR STRING; 525919.Apre_0539; -.
DR EnsemblBacteria; ACV28585; ACV28585; Apre_0539.
DR KEGG; apr:Apre_0539; -.
DR eggNOG; COG0062; Bacteria.
DR HOGENOM; CLU_024853_0_1_9; -.
DR OMA; IKAANHI; -.
DR OrthoDB; 1856227at2; -.
DR Proteomes; UP000002294; 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..218
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_0000416343"
FT DOMAIN 9..215
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 127
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 131..137
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 160
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT BINDING 163
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
SQ SEQUENCE 218 AA; 24133 MW; D663482486F6CB58 CRC64;
MLVVDSKTMK KIDQYAIDVL KVPSICLVER AALAVIKNIN LEKRTSFAIV VGVGNNGADG
LAIARNLLAM GKYVEIYIVG DLTKQSQDFK LNLDSCKRLT DKIFEPKSIE DLAIMERNLE
EVSTIIDAIF GTGLNRTVGG MQSYMISLIN RTMKYTISVD IPSGLDGDSG RNWGEVVDSD
LIISMQIMKR GVYEKSHFKD KCIVEDIGIP QKAIRAIL
