NNRD_BOVIN
ID NNRD_BOVIN Reviewed; 329 AA.
AC E1BNQ4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE EC=4.2.1.93 {ECO:0000250|UniProtKB:Q9CZ42, ECO:0000255|HAMAP-Rule:MF_03157};
DE AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE AltName: Full=Carbohydrate kinase domain-containing protein {ECO:0000255|HAMAP-Rule:MF_03157};
DE AltName: Full=NAD(P)HX dehydratase {ECO:0000250|UniProtKB:Q8IW45};
DE Flags: Precursor;
GN Name=NAXD {ECO:0000250|UniProtKB:Q8IW45};
GN Synonyms=CARKD {ECO:0000255|HAMAP-Rule:MF_03157};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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:0000255|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:0000250|UniProtKB:Q9CZ42, ECO:0000255|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:0000250|UniProtKB:Q9CZ42};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03157};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03157}.
CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC Rule:MF_03157}.
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DR EMBL; DAAA02034911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02034912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002692037.1; XM_002691991.3.
DR AlphaFoldDB; E1BNQ4; -.
DR SMR; E1BNQ4; -.
DR STRING; 9913.ENSBTAP00000015238; -.
DR PaxDb; E1BNQ4; -.
DR PRIDE; E1BNQ4; -.
DR Ensembl; ENSBTAT00000015238; ENSBTAP00000015238; ENSBTAG00000011466.
DR GeneID; 613996; -.
DR KEGG; bta:613996; -.
DR CTD; 55739; -.
DR VEuPathDB; HostDB:ENSBTAG00000011466; -.
DR VGNC; VGNC:53829; NAXD.
DR eggNOG; KOG3974; Eukaryota.
DR GeneTree; ENSGT00390000000917; -.
DR HOGENOM; CLU_030651_3_0_1; -.
DR InParanoid; E1BNQ4; -.
DR OMA; HIPHTNE; -.
DR OrthoDB; 1337331at2759; -.
DR TreeFam; TF300116; -.
DR Reactome; R-BTA-197264; Nicotinamide salvaging.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000011466; Expressed in saliva-secreting gland and 104 other tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; IBA:GO_Central.
DR GO; GO:0110051; P:metabolite repair; IBA:GO_Central.
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 Pfam; PF01256; Carb_kinase; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Lyase; Mitochondrion; NAD; NADP;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT CHAIN 29..329
FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416156"
FT DOMAIN 35..326
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 135
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 188..194
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 228..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 247..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 257
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT MOD_RES 49
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ42"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ42"
SQ SEQUENCE 329 AA; 34809 MW; 7580A8A4A93374AE CRC64;
MALGPGCRAV RGCRPVLKRA FSLHKAHSVK DMESILQLVR SVVPALTTKK HKGQDGRIGV
VGGCREYTGA PYFAAISALK VGADLSHVFC TQEAAPVIKA YSPELIVHPV LDSPEAVRDV
EQWLPRLHAL VVGPGLGRDD ALLENVKGIL EASKARGIPV VIDADGLWLI AQQPALIQGY
RKAVLTPNHV EFGRLSEAVL GVPLDGGDRH GAVLRLSQAL GNVTVVQKGE QDVISDGEQV
LECSQEGSGR RCGGQGDLLS GSLGVLAHWA LRAGPQKTGG PSPLLVAAFG ACALTRQCSQ
QAFQKYGRAT TTSDMVAEVG PAFRRLFEA
