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Database: UniProt
Entry: A0A498HM94_MALDO
LinkDB: A0A498HM94_MALDO
Original site: A0A498HM94_MALDO 
ID   A0A498HM94_MALDO        Unreviewed;       412 AA.
AC   A0A498HM94;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
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   ORFNames=DVH24_013253 {ECO:0000313|EMBL:RXH70507.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH70507.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH70507.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH70507.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03157}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXH70507.1}.
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DR   EMBL; RDQH01000342; RXH70507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498HM94; -.
DR   STRING; 3750.A0A498HM94; -.
DR   Proteomes; UP000290289; Chromosome 16.
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:UP000290289}.
FT   DOMAIN          69..381
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51383"
FT   BINDING         182
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   BINDING         235..241
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   BINDING         275..279
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
SQ   SEQUENCE   412 AA;  44818 MW;  E9F9B396031D9113 CRC64;
     MLIKHGINSG FVARTCLYML GSSGVLRRQQ FLIRSLGVGG CSDRNTITNQ KAMQGIRKFT
     SRPSLEADAE SVLRAITPTL DPNRHKGQAG KIAVIGGCRE YTGAPYFSAI SALKIGADLS
     HVFCTKDAAS VIKSYSPELI VHPILEESYS VRDGDRSFIS EKVLAEVDKW MERFDCLVVG
     PGLGRDPFLL DCVSNIMKHA RRSNVPIVID GDGLFLVTNC IDLVSGYPLA VLTPNINEYK
     RLVQKVLSCE VNDEDAPEQV LSLAKRIGGV TILRKGRSDL ISDGETAGGD DISCDTLDEC
     ELGSLPYQQL LSISVGVFLS WARQKIKNGD LSTSSRNPAL LGCIAASALM RKAASLAFEN
     KKRSTLTTDI IECLGRRISV QLVDAVDFQS IAFDLPTFRE TSISLAYVMS TI
//
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