ID J6ILF1_9ACTN Unreviewed; 556 AA.
AC J6ILF1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 13-SEP-2023, entry version 47.
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=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
GN ORFNames=HMPREF1155_0409 {ECO:0000313|EMBL:EJU34800.1};
OS Slackia sp. CM382.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=1111137 {ECO:0000313|EMBL:EJU34800.1, ECO:0000313|Proteomes:UP000004399};
RN [1] {ECO:0000313|EMBL:EJU34800.1, ECO:0000313|Proteomes:UP000004399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM382 {ECO:0000313|EMBL:EJU34800.1,
RC ECO:0000313|Proteomes:UP000004399};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJU34800.1}.
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DR EMBL; ALNO01000005; EJU34800.1; -; Genomic_DNA.
DR RefSeq; WP_009076861.1; NZ_ALNO01000005.1.
DR AlphaFoldDB; J6ILF1; -.
DR PATRIC; fig|1111137.3.peg.575; -.
DR Proteomes; UP000004399; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
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 GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd10032; UDG-F6_HDG; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR026353; Hypoxan-DNA_Glyclase.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR NCBIfam; TIGR04274; hypoxanDNAglyco; 1.
DR NCBIfam; TIGR00197; yjeF_nterm; 1.
DR Pfam; PF03167; UDG; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:EJU34800.1};
KW Hydrolase {ECO:0000313|EMBL:EJU34800.1};
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}.
FT DOMAIN 178..435
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT REGION 214..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..271
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 268
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 341
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 378
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 381
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
SQ SEQUENCE 556 AA; 59355 MW; 5239D49863C2003E CRC64;
MPAAQDVTHP FEPVFDERSQ VLVLGTMPSP RSREEGFYYA HPRNRFWRVI AQLFDEPLAR
TNEERIDQLL RHHIALWDVL ASCRIEGAKD ASIRDAVPND LARIMDAAPV TAVFCTGTAA
AQAYRRFSEP KTGIACMQLP STSPANAAMG LDVLVDAYQP LAAAAAASEA PLLDVPDVVR
LEQAIAEAGT PLSTLMDRAG TWIAHRAIAR IEALRGDTGK PTETNKTSET NDRSCPHPSD
EPRAGHDGAR RRACDASQVV VLCGNGNNGG DGWVAARILA DAGLPVSVIC AKEPHDLRAQ
PARNAAIEAL TALEEHGARV LVSPDPAALE SKLQSAAVII DAILGTGFSG GSVAAPFDAW
IEAAVRARNA GAFIIAADVP SGLSAQTGRA VRPCIKADET VTMLAMKPGL STPFAFAWAG
TVRIGAIAYV EPLLERMACE DNAPATGKDG KPDPAGSRGK KTPGKLLHAK AGDEDRAGAA
DDQADRAKES RRRDIGAEEP RRSRTRTEQT ANPSAVCSAL RQDPFARAEQ EDDDGYDPYS
DRPPMPEPVF QRDPWA
//
