ID G1R906_NOMLE Unreviewed; 391 AA.
AC G1R906;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 3.
DT 27-MAR-2024, entry version 62.
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};
DE AltName: Full=Carbohydrate kinase domain-containing protein {ECO:0000256|HAMAP-Rule:MF_03157};
GN Name=CARKD {ECO:0000256|HAMAP-Rule:MF_03157};
GN Synonyms=NAXD {ECO:0000313|Ensembl:ENSNLEP00000009693.3};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000009693.3, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000009693.3, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000009693.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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;
CC Evidence={ECO:0000256|ARBA:ARBA00000465, 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000836, 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 -!- SUBCELLULAR LOCATION: Mitochondrion {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 EMBL; ADFV01054161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01054162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01054163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01054164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01054165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01054166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01054167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000009693; -.
DR Ensembl; ENSNLET00000010158.3; ENSNLEP00000009693.3; ENSNLEG00000007951.3.
DR eggNOG; KOG3974; Eukaryota.
DR GeneTree; ENSGT00390000000917; -.
DR InParanoid; G1R906; -.
DR OMA; CTHEAVQ; -.
DR TreeFam; TF300116; -.
DR Proteomes; UP000001073; Chromosome 5.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 Mitochondrion {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:UP000001073}.
FT DOMAIN 53..391
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51383"
FT REGION 316..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT BINDING 206..212
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT BINDING 246..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT BINDING 265..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT BINDING 275
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
SQ SEQUENCE 391 AA; 41294 MW; F0AD16F66B7B74B6 CRC64;
MVTGAGAGTA IAGAAVVALL SAALALYGPP LDAVLERAFS LHKAHSIKDM ENTLQLVRNI
IPSLSSTKHK GQDGRIGVVG GCQEYTGAPY FAAISALKVG ADLSHVFCAS AAAPVIKAYS
PELIVHPVLD SPSAVHEVEK WLPRLHALVI GPGLGRDDAL LRNVQGILEA SKARDIPVVI
DADGLWLVAQ QPALIQGYRK AVLTPNHMEF SRLYDAVLRG PVDSSDSHGS VLRLSQALGN
VTVVQKGERD ILSDGQQVLV CSQEGSSRRC GGQGDLLSGS LGVLVHWALL AGPEKMXXGI
SDLKLTVWGP EIETGVKTRA QGSCGPQTTT PTSPHLLSSP SPQVQPSPGG RIWRLLSHQA
VQPPSLPEAR ALHHHLRHDR RGGGRLQQAP R
//
