ID   NNRD_CENSY              Reviewed;         287 AA.
AC   A0RU82;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_01965};
DE            EC=4.2.1.136 {ECO:0000255|HAMAP-Rule:MF_01965};
DE   AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_01965};
GN   Name=nnrD {ECO:0000255|HAMAP-Rule:MF_01965}; OrderedLocusNames=CENSYa_0257;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC   -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC       expense of ADP, which is converted to AMP. Together with NAD(P)HX
CC       epimerase, which catalyzes the epimerization of the S- and R-forms, the
CC       enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of
CC       NAD(P)H that is a result of enzymatic or heat-dependent hydration.
CC       {ECO:0000255|HAMAP-Rule:MF_01965}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate;
CC         Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01965};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate;
CC         Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01965};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01965};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01965}.
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01965}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK76899.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DP000238; ABK76899.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A0RU82; -.
DR   SMR; A0RU82; -.
DR   STRING; 414004.CENSYa_0257; -.
DR   PRIDE; A0RU82; -.
DR   EnsemblBacteria; ABK76899; ABK76899; CENSYa_0257.
DR   KEGG; csy:CENSYa_0257; -.
DR   PATRIC; fig|414004.10.peg.224; -.
DR   HOGENOM; CLU_024853_2_2_2; -.
DR   Proteomes; UP000000758; Chromosome.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01171; YXKO-related; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_01965; NADHX_dehydratase; 1.
DR   InterPro; IPR000631; CARKD.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR   PROSITE; PS51383; YJEF_C_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Lyase; NAD; NADP; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..287
FT                   /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT                   /id="PRO_0000416152"
FT   DOMAIN          7..283
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         42
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         159
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         196..200
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         224
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         225
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
SQ   SEQUENCE   287 AA;  30027 MW;  6643E7BB0AED62E5 CRC64;
     MAARMIGEDD VRKFVPSRRR DSRKGENGKV LVVGGSYIYH GAPIFSSVAA LRSGCDLVYT
     AVPKINAPAT RAASPSMIVI PLADQKLTRG AARKLAGQIP TGLDSATIGM GLAIAERSAL
     KVLVVALVDM DVRISLDAGA LVREILGDIS GKNCLVTPHA GEFKRLFGES PPADIEGRAS
     MVERLAQEHG ITILLKGPTD VISDGNRTLL NDRGAPAMTV GGTGDVLSGI AAGILARNRS
     PLESAAAAAY INGLAGEAAQ EMHGLHITAM DLCELLPSVM KPFDRLE