NADK1_ARATH
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 03-AUG-2022, entry version 118.
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.AT3G21070.1; -.
DR iPTMnet; Q56YN3; -.
DR PaxDb; Q56YN3; -.
DR PRIDE; Q56YN3; -.
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 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 Genevisible; Q56YN3; AT.
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 Gene3D; 2.60.200.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
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 Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
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
