ID   NADK1_ARATH             Reviewed;         524 AA.
AC   Q56YN3; Q6TXT3; Q8RX27; Q9LJC5;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=NAD(H) kinase 1;
DE            Short=AtNADK-1;
DE            EC=2.7.1.23;
DE            EC=2.7.1.86;
GN   Name=NADK1; OrderedLocusNames=At3g21070; ORFNames=MSA6.11;
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 [MRNA], FUNCTION, INDUCTION, AND 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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15247403; DOI=10.1104/pp.104.040428;
RA   Turner W.L., Waller J.C., Vanderbeld B., Snedden W.A.;
RT   "Cloning and characterization of two NAD kinases from Arabidopsis.
RT   Identification of a calmodulin binding isoform.";
RL   Plant Physiol. 135:1243-1255(2004).
CC   -!- FUNCTION: Phosphorylates both NAD(+) and NADH, with a twofold
CC       preference for NADH. Source of the cellular reductant NADPH which is an
CC       important antioxidant factor. {ECO:0000269|PubMed:15711971}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=520 uM for NAD {ECO:0000269|PubMed:15247403};
CC         KM=730 uM for ATP {ECO:0000269|PubMed:15247403};
CC         Vmax=11.1 umol/h/mg enzyme with ATP as substrate
CC         {ECO:0000269|PubMed:15247403};
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:15247403};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q56YN3-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15247403,
CC       ECO:0000269|PubMed:15711971}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during development from young seedlings
CC       to flowering plants. {ECO:0000269|PubMed:15247403}.
CC   -!- INDUCTION: By gamma radiation, hydrogen peroxide and infection by
CC       P.syringae. {ECO:0000269|PubMed:15711971}.
CC   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM13987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB01450.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY383545; AAR32133.1; -; mRNA.
DR   EMBL; AP000604; BAB01450.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76456.1; -; Genomic_DNA.
DR   EMBL; AY090937; AAM13987.1; ALT_INIT; mRNA.
DR   EMBL; AK176132; BAD43895.1; -; mRNA.
DR   EMBL; AK221288; BAD94003.1; -; mRNA.
DR   RefSeq; NP_974347.1; NM_202618.3. [Q56YN3-1]
DR   AlphaFoldDB; Q56YN3; -.
DR   SMR; Q56YN3; -.
DR   STRING; 3702.Q56YN3; -.
DR   iPTMnet; Q56YN3; -.
DR   PaxDb; 3702-AT3G21070-1; -.
DR   ProteomicsDB; 250994; -. [Q56YN3-1]
DR   EnsemblPlants; AT3G21070.2; AT3G21070.2; AT3G21070. [Q56YN3-1]
DR   GeneID; 821659; -.
DR   Gramene; AT3G21070.2; AT3G21070.2; AT3G21070. [Q56YN3-1]
DR   KEGG; ath:AT3G21070; -.
DR   Araport; AT3G21070; -.
DR   TAIR; AT3G21070; NADK1.
DR   eggNOG; KOG2178; Eukaryota.
DR   InParanoid; Q56YN3; -.
DR   PhylomeDB; Q56YN3; -.
DR   BRENDA; 2.7.1.23; 399.
DR   BRENDA; 2.7.1.86; 399.
DR   PRO; PR:Q56YN3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q56YN3; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IBA:GO_Central.
DR   GO; GO:0042736; F:NADH kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00361; NAD_kinase; 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   PANTHER; PTHR20275; NAD KINASE; 1.
DR   PANTHER; PTHR20275:SF44; NAD(H) KINASE 1; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   Pfam; PF20143; NAD_kinase_C; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   Genevisible; Q56YN3; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; NAD; NADP; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..524
FT                   /note="NAD(H) kinase 1"
FT                   /id="PRO_0000233702"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        178
FT                   /note="M -> I (in Ref. 4; AAM13987)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   524 AA;  58245 MW;  529A4D659C1F9298 CRC64;
     MSSTYKLNHT DSFANGDAKS LLPNPENGFT HLTSLAQSEK AVQELLLQQT PMQATDDHLV
     EFSEALRTVA KALRGAAEGK ALAQAEAAEW KRRYELERSK NVELQHKELS NGVCADESNG
     QRMEHLAKSP RLYAQEISSN GMETICSHEV LQDGGFNSFN NKLKRKASFK LSWGCKGMAN
     DQHKKEIVSF ERGNISTAER SSKQISLTWE SDPQTVLIIT KPNSTSVRVL SVDMVRWLRT
     QKGLNIYVEP RVKEELLSES SSFNFVQTWE DDKEISLLHT KVDLLITLGG DGTVLWAASM
     FKGPVPPIVP FSMGSLGFMT PFHSEQYRDC LEAILKGPIS ITLRHRLQCH IIRDKATHEY
     EPEETMLVLN EVTIDRGISS YLTNLECYCD NSFVTCVQGD GLILSTTSGS TAYSLAAGGS
     MVHPQVPGIL FTPICPHSLS FRPLILPEHV TVRVQVPFNS RSSAWVSFDG KDRKQLEAGD
     ALVCSMAPWP VSTACQVEST NDFLRSIHDG LHWNLRKTQS ADGP
//