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Database: UniProt
Entry: G0QDU3_NANSJ
LinkDB: G0QDU3_NANSJ
Original site: G0QDU3_NANSJ 
ID   G0QDU3_NANSJ            Unreviewed;       255 AA.
AC   G0QDU3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
DE            EC=4.2.1.136 {ECO:0000256|HAMAP-Rule:MF_01965};
DE   AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
GN   Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
GN   ORFNames=J07AB56_11700 {ECO:0000313|EMBL:EGQ40441.1};
OS   Nanosalinarum sp. (strain J07AB56).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC   Candidatus Nanosalinarum.
OX   NCBI_TaxID=889962 {ECO:0000313|EMBL:EGQ40441.1, ECO:0000313|Proteomes:UP000009382};
RN   [1] {ECO:0000313|EMBL:EGQ40441.1, ECO:0000313|Proteomes:UP000009382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Narasingarao P., Podell S., Ugalde J.A., Brochier-Armanet C., Emerson J.B.,
RA   Brocks J.J., Heidelberg K.B., Banfield J.F., Allen E.E.;
RT   "De novo metagenomic assembly reveals abundant novel major lineage of
RT   Archaea in hypersaline microbial communities.";
RL   ISME J. 0:0-0(2011).
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:0000256|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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01965};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01965};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01965}.
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01965}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01965}.
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DR   EMBL; GL982569; EGQ40441.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0QDU3; -.
DR   HOGENOM; CLU_1080123_0_0_2; -.
DR   OMA; HIPHTNE; -.
DR   Proteomes; UP000009382; Unassembled WGS sequence.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   NCBIfam; TIGR00196; yjeF_cterm; 1.
DR   PANTHER; PTHR12592:SF0; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE; 1.
DR   PANTHER; PTHR12592; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER; 1.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS01050; YJEF_C_2; 1.
DR   PROSITE; PS51383; YJEF_C_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01965}; Kinase {ECO:0000313|EMBL:EGQ40441.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01965};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01965};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01965};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01965}; Reference proteome {ECO:0000313|Proteomes:UP000009382};
KW   Transferase {ECO:0000313|EMBL:EGQ40441.1}.
FT   DOMAIN          1..252
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51383"
FT   BINDING         30
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         98
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         140
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         193
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         194
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
SQ   SEQUENCE   255 AA;  26744 MW;  EC57DEE1C6882C53 CRC64;
     MSFPTRDKDS RKGDNGRVGV IAGSSRFTGA PALCGQAAMR AGADLVKVLT SKSVRDVVAG
     FSKDLIVQSY SGRFLTEEDA DRLGDFAEWG DVLVAGPGLG RPDPETLRDV VDSRRCVLDA
     DAIHETVLEA DLSHAVLTPH RREVERLGDP ERFAAQTGAV ILLKGPTDRV FSPEGLEVEI
     ERGDPTMTAG GTGDVLAGVV GGLIAQGMSR VDAAEAGARA NGMAGEEAAV EYGNGALASD
     IVERLPGSLR NLEEM
//
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