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NNRD_NEIG1
ID   NNRD_NEIG1              Reviewed;         296 AA.
AC   Q5F8G9;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=NGO0804;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AE004969; AAW89518.1; -; Genomic_DNA.
DR   RefSeq; WP_003688608.1; NC_002946.2.
DR   RefSeq; YP_207930.1; NC_002946.2.
DR   AlphaFoldDB; Q5F8G9; -.
DR   SMR; Q5F8G9; -.
DR   STRING; 242231.NGO_0804; -.
DR   EnsemblBacteria; AAW89518; AAW89518; NGO_0804.
DR   GeneID; 66753141; -.
DR   KEGG; ngo:NGO_0804; -.
DR   PATRIC; fig|242231.10.peg.951; -.
DR   HOGENOM; CLU_024853_2_5_4; -.
DR   OMA; ATYWRDG; -.
DR   Proteomes; UP000000535; 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..296
FT                   /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT                   /id="PRO_0000416146"
FT   DOMAIN          18..292
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         53
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         113
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         165
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         202..206
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         231
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         232
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
SQ   SEQUENCE   296 AA;  30241 MW;  05E38075637EC2FB CRC64;
     MFPVFHLSGE SRRRMLQTAL RFPHVFKARA EDSHKGTFGT LAVVGGSAGM SGAPVLAASA
     AMYLGCGKVR AGFNQDTLPF AVIAGFPEIM LDTADGLTKR QGINAWTAGC GLGTDAAAVE
     TVAAVLARNR DEAVVLDADA LNILSTDAET RNLARGCKNL ILTPHPAEAA RLLGTTVAQV
     QADRTAAVRK IGAILGATVV LKGHKTLVAA SDTEIYVNES GNAGLATAGS GDVLGGIIGS
     LLAQGVPVFE AACAGAWLHG AAADVIKESA GIAAGLSAGE IAPAARWLRN WITESM
 
 
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