ID A0A2H5V352_9ARCH Unreviewed; 405 AA.
AC A0A2H5V352;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|ARBA:ARBA00012228, ECO:0000256|HAMAP-Rule:MF_01966};
DE EC=5.1.99.6 {ECO:0000256|ARBA:ARBA00012228, 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:GBC71128.1};
GN Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
GN ORFNames=HRbin02_00907 {ECO:0000313|EMBL:GBC71128.1};
OS Candidatus Calditenuaceae archaeon HR02.
OC Archaea; Nitrososphaerota; Candidatus Caldarchaeales;
OC Candidatus Calditenuaceae.
OX NCBI_TaxID=2035438 {ECO:0000313|EMBL:GBC71128.1, ECO:0000313|Proteomes:UP000236403};
RN [1] {ECO:0000313|Proteomes:UP000236403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kato S., Suzuki K.;
RT "Metaegenomics of thermophilic ammonia-oxidizing enrichment culture.";
RL Submitted (SEP-2017) 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|ARBA:ARBA00000013, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00000909, ECO:0000256|HAMAP-
CC 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: 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:GBC71128.1}.
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DR EMBL; BEHE01000008; GBC71128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5V352; -.
DR Proteomes; UP000236403; Unassembled WGS sequence.
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 InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR NCBIfam; TIGR00197; yjeF_nterm; 1.
DR PANTHER; PTHR13232; NAD(P)H-HYDRATE EPIMERASE; 1.
DR PANTHER; PTHR13232:SF10; NAD(P)H-HYDRATE EPIMERASE; 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|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01966};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01966};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01966};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01966};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01966}; Potassium {ECO:0000256|HAMAP-Rule:MF_01966};
KW Reference proteome {ECO:0000313|Proteomes:UP000236403}.
FT DOMAIN 7..223
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT BINDING 61..65
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 62
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 136
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 140..146
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 151
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 169
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT BINDING 172
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
SQ SEQUENCE 405 AA; 43341 MW; 99787D14FCBF105A CRC64;
MGERRQYRSY EIGIVDENSA YLGVDRRLLM ENAGAAVARV LAMEVPDLTS AKVLVVAGPG
NNGGDALVAA RHLAGKVARL SVILLARPDQ IRTPEAAANW EAISRMRRSV DYYVSDTLEA
LYRLQQLFRE ADIIIDGIFG TGIRGEIREP YKTAINFINS PPAKVFSIDV PSGMDPDTGK
YTTTVRPSVT ITLHGAKPFM TLQRELAGKT YIEPIGAPPD AEAIAGPGDL AYSLSRLRRP
VSASIRGGAE EARGAAEVLR ILGVEPRVEM LGGGLTVTVD GLLVGYGVAE SFGSLSALVK
PIQEQVGGDA ADLAKTIGKP VYLVGGWDSI SDGVYLKSNW IEPPVSSRYI LGVATSLSAA
FLANGVEPIY AIGAACYAAR RPLRGRGSED REAYLDGLRQ LLLRK
//
