NADK2_ARATH
ID NADK2_ARATH Reviewed; 985 AA.
AC Q9C5W3; Q9XI15;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=NAD kinase 2, chloroplastic;
DE Short=AtNADK-2;
DE EC=2.7.1.23;
DE Flags: Precursor;
GN Name=NADK2; OrderedLocusNames=At1g21640; ORFNames=F8K7.5;
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 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 [2]
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 [3]
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 [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, AND CALMODULIN-BINDING
RP DOMAIN.
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).
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).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16244906; DOI=10.1007/s11103-005-6802-y;
RA Chai M.-F., Chen Q.-J., An R., Chen Y.-M., Chen J., Wang X.-C.;
RT "NADK2, an Arabidopsis chloroplastic NAD kinase, plays a vital role in both
RT chlorophyll synthesis and chloroplast protection.";
RL Plant Mol. Biol. 59:553-564(2005).
CC -!- FUNCTION: Involved in chlorophyll synthesis and chloroplast protection
CC against oxidative damage. {ECO:0000269|PubMed:16244906}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=430 uM for NAD {ECO:0000269|PubMed:15247403};
CC KM=740 uM for ATP {ECO:0000269|PubMed:15247403};
CC Vmax=14.3 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16244906}.
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=Q9C5W3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:15711971}.
CC -!- DEVELOPMENTAL STAGE: Expressed during development from young seedlings
CC to flowering plants. {ECO:0000269|PubMed:15247403}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD41416.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007727; AAD41416.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30130.1; -; Genomic_DNA.
DR EMBL; AF337912; AAG60064.1; -; mRNA.
DR EMBL; AY099794; AAM20645.1; -; mRNA.
DR PIR; D86349; D86349.
DR RefSeq; NP_564145.1; NM_102013.5. [Q9C5W3-1]
DR AlphaFoldDB; Q9C5W3; -.
DR SMR; Q9C5W3; -.
DR STRING; 3702.AT1G21640.2; -.
DR PaxDb; Q9C5W3; -.
DR ProteomicsDB; 251080; -. [Q9C5W3-1]
DR EnsemblPlants; AT1G21640.1; AT1G21640.1; AT1G21640. [Q9C5W3-1]
DR GeneID; 838766; -.
DR Gramene; AT1G21640.1; AT1G21640.1; AT1G21640. [Q9C5W3-1]
DR KEGG; ath:AT1G21640; -.
DR Araport; AT1G21640; -.
DR eggNOG; KOG2178; Eukaryota.
DR InParanoid; Q9C5W3; -.
DR OMA; YCRIFRT; -.
DR PhylomeDB; Q9C5W3; -.
DR BRENDA; 2.7.1.23; 399.
DR PRO; PR:Q9C5W3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5W3; baseline and differential.
DR Genevisible; Q9C5W3; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IBA:GO_Central.
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 Gene3D; 3.90.190.10; -; 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 InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calmodulin-binding; Chloroplast; Kinase;
KW NAD; NADP; Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 63..985
FT /note="NAD kinase 2, chloroplastic"
FT /id="PRO_0000233705"
FT REGION 335..380
FT /note="Calmodulin-binding"
FT REGION 389..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 109188 MW; CF9BDFD804AF5C0E CRC64;
MFLCFCPCHV PIMSRLSPAT GISSRLRFSI GLSSDGRLIP FGFRFRRNDV PFKRRLRFVI
RAQLSEAFSP DLGLDSQAVK SRDTSNLPWI GPVPGDIAEV EAYCRIFRSA ERLHGALMET
LCNPVTGECR VPYDFSPEEK PLLEDKIVSV LGCILSLLNK GRKEILSGRS SSMNSFNLDD
VGVAEESLPP LAVFRGEMKR CCESLHIALE NYLTPDDERS GIVWRKLQKL KNVCYDAGFP
RSDNYPCQTL FANWDPIYSS NTKEDIDSYE SEIAFWRGGQ VTQEGLKWLI ENGFKTIVDL
RAEIVKDTFY QTALDDAISL GKITVVQIPI DVRMAPKAEQ VELFASIVSD SSKRPIYVHS
KEGVWRTSAM VSRWKQYMTR PITKEIPVSE ESKRREVSET KLGSNAVVSG KGVPDEQTDK
VSEINEVDSR SASSQSKESG RFEGDTSASE FNMVSDPLKS QVPPGNIFSR KEMSKFLKSK
SIAPAGYLTN PSKILGTVPT PQFSYTGVTN GNQIVDKDSI RRLAETGNSN GTLLPTSSQS
LDFGNGKFSN GNVHASDNTN KSISDNRGNG FSAAPIAVPP SDNLSRAVGS HSVRESQTQR
NNSGSSSDSS DDEAGAIEGN MCASATGVVR VQSRKKAEMF LVRTDGVSCT REKVTESSLA
FTHPSTQQQM LLWKTTPKTV LLLKKLGQEL MEEAKEAASF LYHQENMNVL VEPEVHDVFA
RIPGFGFVQT FYIQDTSDLH ERVDFVACLG GDGVILHASN LFKGAVPPVV SFNLGSLGFL
TSHPFEDFRQ DLKRVIHGNN TLDGVYITLR MRLRCEIYRK GKAMPGKVFD VLNEIVVDRG
SNPYLSKIEC YEHDRLITKV QGDGVIVATP TGSTAYSTAA GGSMVHPNVP CMLFTPICPH
SLSFRPVILP DSAKLELKIP DDARSNAWVS FDGKRRQQLS RGDSVRIYMS QHPLPTVNKS
DQTGDWFRSL IRCLNWNERL DQKAL
