NNRD_SORBI
ID NNRD_SORBI Reviewed; 381 AA.
AC C5Y210;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE EC=4.2.1.93 {ECO:0000255|HAMAP-Rule:MF_03157};
DE AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
GN OrderedLocusNames=Sb05g010020;
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623;
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M.,
RA Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(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; Evidence={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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={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; CM000764; EES09669.1; -; Genomic_DNA.
DR RefSeq; XP_002450681.1; XM_002450636.1.
DR AlphaFoldDB; C5Y210; -.
DR SMR; C5Y210; -.
DR STRING; 4558.Sb05g010020.1; -.
DR eggNOG; KOG3974; Eukaryota.
DR HOGENOM; CLU_030651_1_0_1; -.
DR InParanoid; C5Y210; -.
DR Proteomes; UP000000768; Chromosome 5.
DR ExpressionAtlas; C5Y210; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
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:0006734; P:NADH metabolic process; IEA:EnsemblPlants.
DR GO; GO:0006739; P:NADP metabolic process; IEA:EnsemblPlants.
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 ATP-binding; Lyase; NAD; NADP; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..381
FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416175"
FT DOMAIN 84..376
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 197
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 250..256
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 290..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 309..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 319
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
SQ SEQUENCE 381 AA; 41415 MW; 4E359EB21F8BEE23 CRC64;
MSRPTGACPH AWRHQQQPLR GRMWAASPAF RRQLVLLRSL LPSPPAPSSV AGFPPSCPSC
SSFLRVRTNH AMAASAGTVY EADAEAVVRR ITPPLDRARH KGQAGKIAVI GGCREYTGAP
YFAAISALKV GADLSHVFCT KDAATVIKSY SPELIVHPIL EESYSVRDDE RASVSSKILT
EVGKWMERFD CIVVGPGLGR DSFLLDCVSN IMRHARQANI PTVVDGDGLF LVTNNLSLVE
GNPLAILTPN VYEYKRLVQK VLNCDVDEET ASEQLITLCQ KIGDVTIMQK GKADVISDGK
TVTQVSTFGS PRRCGGQGDI LSGSVAVFAS WARHFVLTNE QPTEKRKAAS HAFEKNKRST
VTSDIIEFLG KSLEDICPAE H
