NNRD_ENTFA
ID NNRD_ENTFA Reviewed; 291 AA.
AC Q833Y3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=EF_1790;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RC STRAIN=ATCC 700802 / V583;
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of a putative kinase in the ribokinase-like superfamily
RT from Enterococcus faecalis V583 (NP_815490.1) at 1.95 A resolution.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RC STRAIN=ATCC 700802 / V583;
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of a putative kinase in the ribokinase-like superfamily
RT from Enterococcus faecalis V583 (NP_815490.1) at 1.80 A resolution.";
RL Submitted (AUG-2007) to the PDB data bank.
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; AE016830; AAO81560.1; -; Genomic_DNA.
DR RefSeq; NP_815490.1; NC_004668.1.
DR RefSeq; WP_002365767.1; NZ_KE136528.1.
DR PDB; 2R3B; X-ray; 1.80 A; A/B=1-291.
DR PDB; 2R3E; X-ray; 1.95 A; A=1-291.
DR PDBsum; 2R3B; -.
DR PDBsum; 2R3E; -.
DR AlphaFoldDB; Q833Y3; -.
DR SMR; Q833Y3; -.
DR STRING; 226185.EF_1790; -.
DR DNASU; 1200678; -.
DR EnsemblBacteria; AAO81560; AAO81560; EF_1790.
DR KEGG; efa:EF1790; -.
DR PATRIC; fig|226185.45.peg.1726; -.
DR eggNOG; COG0063; Bacteria.
DR HOGENOM; CLU_024853_2_1_9; -.
DR OMA; HIPHTNE; -.
DR EvolutionaryTrace; Q833Y3; -.
DR Proteomes; UP000001415; 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; 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; PS01049; YJEF_C_1; 1.
DR PROSITE; PS01050; YJEF_C_2; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Lyase; NAD; NADP; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..291
FT /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416141"
FT DOMAIN 5..273
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 153
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 215
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 216
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2R3B"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 233..250
FT /evidence="ECO:0007829|PDB:2R3B"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2R3B"
FT HELIX 259..273
FT /evidence="ECO:0007829|PDB:2R3B"
SQ SEQUENCE 291 AA; 31723 MW; ADF1F5477C13BF27 CRC64;
MRYLSKDILE EVITQRPSDS YKSNFGRVVL IGGNRQYGGA IIMSTEACIN SGAGLTTVIT
DVKNHGPLHA RCPEAMVVGF EETVLLTNVV EQADVILIGP GLGLDATAQQ ILKMVLAQHQ
KQQWLIIDGS AITLFSQGNF SLTYPEKVVF TPHQMEWQRL SHLPIEQQTL ANNQRQQAKL
GSTIVLKSHR TTIFHAGEPF QNTGGNPGMA TGGTGDTLAG IIAGFLAQFK PTIETIAGAV
YLHSLIGDDL AKTDYVVLPT KISQALPTYM KKYAQPHTAP DSELLEQKRS R
