ID   NNRD_ANODA              Reviewed;         295 AA.
AC   E3XDZ8; W5JB86;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE            EC=4.2.1.93 {ECO:0000255|HAMAP-Rule:MF_03157};
DE   AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
GN   ORFNames=AND_008360 {ECO:0000312|EMBL:ETN60029.1};
OS   Anopheles darlingi (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA   Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT   "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT   the genome of the newly sequenced Anopheles darlingi.";
RL   BMC Genomics 11:529-529(2010).
CC   -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC       expense of ATP, which is converted to ADP. 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_03157}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate;
CC         Xref=Rhea:RHEA:19017, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074,
CC         ChEBI:CHEBI:456216; EC=4.2.1.93; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADPHX + ATP = ADP + H(+) + NADPH + phosphate;
CC         Xref=Rhea:RHEA:32231, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076,
CC         ChEBI:CHEBI:456216; EC=4.2.1.93;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03157};
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC       Rule:MF_03157}.
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DR   EMBL; ADMH02002000; ETN60029.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3XDZ8; -.
DR   SMR; E3XDZ8; -.
DR   STRING; 43151.ADAC008360-PA; -.
DR   VEuPathDB; VectorBase:ADAC008360; -.
DR   eggNOG; KOG3974; Eukaryota.
DR   HOGENOM; CLU_030651_3_0_1; -.
DR   InParanoid; E3XDZ8; -.
DR   OMA; HIPHTNE; -.
DR   OrthoDB; 1337331at2759; -.
DR   Proteomes; UP000000673; Unassembled WGS sequence.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
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; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..295
FT                   /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT                   /id="PRO_0000416164"
FT   DOMAIN          9..289
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         109
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         162..168
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         193..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         214..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         224
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
SQ   SEQUENCE   295 AA;  32397 MW;  479F823A49795C9F CRC64;
     MSSENKSPLL ERARNLVPHL ETERHKGQAG RIGIVGGSLE YTGAPYFAAI SALKVGADLV
     HVFCPQAAAQ VIKGYSPELI VHPLLDSNNA IIQIEPWLER LHVLVIGPGL GRDRLILQTV
     AELIRICRQL QKPLIIDADG LFLITQDIGL VKDYYGVILT PNAIEFCRLF GKDRDQTMAS
     LGRLGAGVTV IEKGLNDRIY DSLTSEKYEC PQGGSGRRCG GQGDLLAGAL ATFYYWALES
     KQEISPAMVA CFAASTLTKT CNKYAFKAKG RSMTCSDMID QIHQVFDDLF EHKKD