ID A0A1A9GMS7_9ACTN Unreviewed; 244 AA.
AC A0A1A9GMS7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
DE EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_01966};
DE AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
GN Name=nnr_2 {ECO:0000313|EMBL:ANH39598.1};
GN Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
GN ORFNames=I601_3191 {ECO:0000313|EMBL:ANH39598.1};
OS Nocardioides dokdonensis FR1436.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1300347 {ECO:0000313|EMBL:ANH39598.1, ECO:0000313|Proteomes:UP000077868};
RN [1] {ECO:0000313|EMBL:ANH39598.1, ECO:0000313|Proteomes:UP000077868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FR1436 {ECO:0000313|EMBL:ANH39598.1,
RC ECO:0000313|Proteomes:UP000077868};
RA Kwon S.-K., Kim K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Nocardioides
RT dokdonensis FR1436.";
RL Submitted (MAR-2016) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01966};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01966};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01966};
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
CC Rule:MF_01966}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
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DR EMBL; CP015079; ANH39598.1; -; Genomic_DNA.
DR RefSeq; WP_068111771.1; NZ_CP015079.1.
DR AlphaFoldDB; A0A1A9GMS7; -.
DR STRING; 1300347.I601_3191; -.
DR KEGG; ndk:I601_3191; -.
DR PATRIC; fig|1300347.3.peg.3193; -.
DR Proteomes; UP000077868; 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; YjeF N-terminal domain; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR NCBIfam; TIGR00197; yjeF_nterm; 1.
DR PANTHER; PTHR13612:SF0; ENHANCER OF MRNA-DECAPPING PROTEIN 3; 1.
DR PANTHER; PTHR13612; UNCHARACTERIZED; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01966};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01966};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01966};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01966};
KW Potassium {ECO:0000256|HAMAP-Rule:MF_01966};
KW Reference proteome {ECO:0000313|Proteomes:UP000077868}.
FT DOMAIN 20..220
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT BINDING 71..75
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 72
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 134
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 138..144
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 167
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 170
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
SQ SEQUENCE 244 AA; 24717 MW; C9B77013B2AA3F21 CRC64;
MDSFVSEAGL VVPAVTTEQM REVDRVAIEG IGPNLYQMME NAGRNLALSC VEMLGEGWAT
SSVVVLAGTG GNGGGGICAA RHLANHGGQV TLVVSDVERL AGVPAEQLAL FRASGGRLAA
IGDLGTLETS LTVDAVLGYS LAGAPHGAAA DLIGWMSQGP APVVSLDVPS GVDATTGEAP
GVHVRAATTM ALALPKTGLA VDATGEIWLA DIGIPAGVLE RARVRPPPAG LFSKGYRVRL
SWSS
//
