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Database: UniProt
Entry: A0A1U8Q544_NELNU
LinkDB: A0A1U8Q544_NELNU
Original site: A0A1U8Q544_NELNU 
ID   A0A1U8Q544_NELNU        Unreviewed;       329 AA.
AC   A0A1U8Q544;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_03157};
DE            EC=4.2.1.93 {ECO:0000256|HAMAP-Rule:MF_03157};
DE   AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_03157};
GN   Name=LOC104596442 {ECO:0000313|RefSeq:XP_019053175.1};
OS   Nelumbo nucifera (Sacred lotus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX   NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_019053175.1};
RN   [1] {ECO:0000313|RefSeq:XP_019053175.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|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:0000256|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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03157};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03157};
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
CC       Rule:MF_03157}.
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DR   RefSeq; XP_019053175.1; XM_019197630.1.
DR   AlphaFoldDB; A0A1U8Q544; -.
DR   GeneID; 104596442; -.
DR   OrthoDB; 1123001at2759; -.
DR   Proteomes; UP000189703; Unplaced.
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   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; PS51383; YJEF_C_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_03157};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03157};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03157};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03157}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189703}.
FT   DOMAIN          16..325
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51383"
FT   BINDING         129
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   BINDING         182..188
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   BINDING         222..226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   BINDING         241..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   BINDING         251
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
SQ   SEQUENCE   329 AA;  35212 MW;  FD5A738C5555CB6F CRC64;
     MQAIKCVSGS ALEADGQSIL RAIVPTFDPF RYKGQAGKVA VIGGCREYTG APYFAAISAL
     KIGADLSHVF CTKDAAGVIK SYSPELIVHP VLEESYNIRD DEKSIISSKV LADVAKWMER
     FDCLVVGPGL GRDPFLLDCV SEIMKHARQL NIPIVVDGDG LFLVTNNLDL VSGYPLAVLT
     PNVNEYKRLV EKVLDCEIND QDAPEQLLSL ARRVGGITIL RKGKCDIISD GETVHVVSVF
     GSPRRCGGQG DILSGSVAIF SSWARQQNLA TGDNLRGSPS NPMVVGSIAA STLLRKAAST
     AFGKKKRATL TTDIIECLGI SLEEICPAS
//
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