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NNRD_LISMO
ID   NNRD_LISMO              Reviewed;         276 AA.
AC   Q8Y6R2;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=lmo1622;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591980; CAC99700.1; -; Genomic_DNA.
DR   PIR; AF1277; AF1277.
DR   RefSeq; NP_465147.1; NC_003210.1.
DR   RefSeq; WP_003732536.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y6R2; -.
DR   SMR; Q8Y6R2; -.
DR   STRING; 169963.lmo1622; -.
DR   PaxDb; Q8Y6R2; -.
DR   EnsemblBacteria; CAC99700; CAC99700; CAC99700.
DR   GeneID; 985726; -.
DR   KEGG; lmo:lmo1622; -.
DR   PATRIC; fig|169963.11.peg.1665; -.
DR   eggNOG; COG0063; Bacteria.
DR   HOGENOM; CLU_024853_2_1_9; -.
DR   OMA; HIPHTNE; -.
DR   PhylomeDB; Q8Y6R2; -.
DR   BioCyc; LMON169963:LMO1622-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0052856; F:NADHX epimerase activity; IBA:GO_Central.
DR   GO; GO:0052857; F:NADPHX epimerase activity; IBA:GO_Central.
DR   GO; GO:0110051; P:metabolite repair; IBA:GO_Central.
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; IPR017953; Carbohydrate_kinase_pred_CS.
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; PS01050; YJEF_C_2; 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..276
FT                   /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT                   /id="PRO_0000416145"
FT   DOMAIN          5..269
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         40
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         103
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         152
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         211
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT   BINDING         212
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
SQ   SEQUENCE   276 AA;  29796 MW;  0EAFFD71DEC7157F CRC64;
     MKKITPKAMC AWIPKREDET HKGDYGRVLI VAGNKQFGGA AIMAAEACVK SGAGLTTVAS
     DSVNRPALQT RIPECMFIDY ENITSLSEQI SQFDTILIGP GLGLDAYAEE IFRLVLQKST
     EHQQVIIDGD GITIYAKGEN PHPAAKLTFT PHAGEWERLK VLAPDAVTPT DVALAIDATI
     VLKGHRTKVY SGESAWQNMY GTPAMATGGM GDTLAGTICG LMAQTEKPIT GTLAAVFLHS
     YIGEILAKKR YVVLPTEIAE ELPTYLKIFS ETDEHA
 
 
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