NADHK_ARATH
ID NADHK_ARATH Reviewed; 317 AA.
AC Q500Y9; Q9SYM3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=NADH kinase {ECO:0000303|PubMed:15347288};
DE Short=AtNADK-3 {ECO:0000303|PubMed:15347288};
DE EC=2.7.1.86 {ECO:0000305|PubMed:15347288};
GN Name=NADK3; OrderedLocusNames=At1g78590; ORFNames=T30F21.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15347288; DOI=10.1042/bj20040292;
RA Turner W.L., Waller J.C., Snedden W.A.;
RT "Identification, molecular cloning and functional characterization of a
RT novel NADH kinase from Arabidopsis thaliana (thale cress).";
RL Biochem. J. 385:217-223(2005).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15711971; DOI=10.1007/s00438-005-1113-1;
RA Berrin J.-G., Pierrugues O., Brutesco C., Alonso B., Montillet J.-L.,
RA Roby D., Kazmaier M.;
RT "Stress induces the expression of AtNADK-1, a gene encoding a NAD(H) kinase
RT in Arabidopsis thaliana.";
RL Mol. Genet. Genomics 273:10-19(2005).
CC -!- FUNCTION: Phosphorylates specifically NADH. Can phosphorylate NAD with
CC a 100-fold decrease in efficiency compared to NADH. Prefers ATP as
CC nucleoside triphosphate substrate. Can also utilize UTP, GTP and CTP.
CC Key source of the cellular reductant NADPH which is an important
CC antioxidant factor. {ECO:0000269|PubMed:15347288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NADH = ADP + H(+) + NADPH; Xref=Rhea:RHEA:12260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:456216; EC=2.7.1.86;
CC Evidence={ECO:0000305|PubMed:15347288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12261;
CC Evidence={ECO:0000305|PubMed:15347288};
CC -!- ACTIVITY REGULATION: Two-fold decrease in activity in the presence of
CC PPi, iodoacetate or para-chloromercuribenzoate.
CC {ECO:0000269|PubMed:15347288}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42 uM for NADH {ECO:0000269|PubMed:15347288};
CC KM=63 uM for ATP {ECO:0000269|PubMed:15347288};
CC KM=2390 uM for NAD {ECO:0000269|PubMed:15347288};
CC Vmax=41.2 umol/min/mg enzyme with NADH as substrate
CC {ECO:0000269|PubMed:15347288};
CC Vmax=39.5 umol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:15347288};
CC Vmax=23.2 umol/min/mg enzyme with NAD as substrate
CC {ECO:0000269|PubMed:15347288};
CC Note=Measured at pH 7.9 and 25 degrees Celsius for all experiments.;
CC pH dependence:
CC Optimum pH is 7.9 at 25 degrees Celsius.
CC {ECO:0000269|PubMed:15347288};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15347288}.
CC -!- INTERACTION:
CC Q500Y9; Q500Y9: NADK3; NbExp=3; IntAct=EBI-25512202, EBI-25512202;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15347288}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15711971}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30577.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BT022078; AAY27065.1; -; mRNA.
DR EMBL; AC007260; AAD30577.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36124.1; -; Genomic_DNA.
DR PIR; E96814; E96814.
DR RefSeq; NP_177980.2; NM_106506.3.
DR AlphaFoldDB; Q500Y9; -.
DR SMR; Q500Y9; -.
DR BioGRID; 29414; 1.
DR STRING; 3702.AT1G78590.1; -.
DR iPTMnet; Q500Y9; -.
DR PaxDb; Q500Y9; -.
DR PRIDE; Q500Y9; -.
DR ProteomicsDB; 251035; -.
DR DNASU; 844195; -.
DR EnsemblPlants; AT1G78590.1; AT1G78590.1; AT1G78590.
DR GeneID; 844195; -.
DR Gramene; AT1G78590.1; AT1G78590.1; AT1G78590.
DR KEGG; ath:AT1G78590; -.
DR Araport; AT1G78590; -.
DR TAIR; locus:2202975; AT1G78590.
DR eggNOG; KOG4180; Eukaryota.
DR HOGENOM; CLU_067437_0_0_1; -.
DR InParanoid; Q500Y9; -.
DR OMA; MIYIDGS; -.
DR PhylomeDB; Q500Y9; -.
DR BRENDA; 2.7.1.23; 399.
DR PRO; PR:Q500Y9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q500Y9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003951; F:NAD+ kinase activity; IDA:TAIR.
DR GO; GO:0042736; F:NADH kinase activity; IDA:TAIR.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002504; NADK.
DR Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="NADH kinase"
FT /id="PRO_0000233700"
SQ SEQUENCE 317 AA; 34831 MW; 5256487599C8F90E CRC64;
MAIRKLLLLL KPIDPYPFLQ TEGASLIKNP QVLQYLESRC KVHKNAIKFC QEILSKKPVE
WKPISRNDLS HPIRDVDMVI TVGGDGTLLH ASHFIDDSVP VLGVNSDPTQ AHEVEELSDQ
FDASRSTGHL CAATVENFEQ VLDDILFGRV VPAKVSRISL KLNSETLLSH ALNDILIAQP
CPAAVSRFSF KIKNKDGASS PKTVNCRSSG LRICTAAGST AAMQSAGGFV MPMLSRDLQF
MVREPISPGS TASLMHSTFK PDQFMDVNWY SDHGTIYIDG CQVQHSVQLG DTIEISSDAP
VLNVFLSHGI SQIRSRY
