NADKC_ARATH
ID NADKC_ARATH Reviewed; 534 AA.
AC Q0WUY1; Q7DM36; Q7GB61;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Calmodulin calcium-dependent NAD kinase {ECO:0000305};
DE EC=2.7.1.23 {ECO:0000269|PubMed:31554701};
DE AltName: Full=NAD kinase-CaM dependent protein {ECO:0000303|PubMed:31554701};
DE Short=NADKc {ECO:0000303|PubMed:31554701};
GN Name=NADKC {ECO:0000303|PubMed:31554701}; Synonyms=H1FLK;
GN OrderedLocusNames=At1g04280 {ECO:0000312|Araport:AT1G04280};
GN ORFNames=F19P19.28 {ECO:0000312|EMBL:AEE27678.1};
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-534.
RX PubMed=1765064; DOI=10.1111/j.1432-1033.1991.tb16466.x;
RA Gantt J.S., Lenvik T.R.;
RT "Arabidopsis thaliana H1 histones. Analysis of two members of a small gene
RT family.";
RL Eur. J. Biochem. 202:1029-1039(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-534.
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP CALMODULIN-BINDIG, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=31554701; DOI=10.1104/pp.19.00912;
RA Dell'Aglio E., Giustini C., Kraut A., Coute Y., Costa A., Decros G.,
RA Gibon Y., Mazars C., Matringe M., Finazzi G., Curien G.;
RT "Identification of the Arabidopsis calmodulin-dependent NAD+ kinase that
RT sustains the elicitor-induced oxidative burst.";
RL Plant Physiol. 181:1449-1458(2019).
CC -!- FUNCTION: Phosphorylates NAD(+) to produces NADP(+) in a calmodulin
CC calcium-dependent manner (PubMed:31554701). Does not possess activity
CC toward NADH (PubMed:31554701). Has broad specificity for the phosphoryl
CC donor, as ATP, CTP, GTP and UTP can be used interchangeably and produce
CC similar efficiencies (PubMed:31554701). May play a role in producing
CC NADP(H) needed to regulate the elicitor-induced reactive oxygen species
CC (ROS) burst by sustaining the activity of NADPH oxidases
CC (PubMed:31554701). Does not seem to play a role in photosynthesis-
CC driven growth (PubMed:31554701). {ECO:0000269|PubMed:31554701}.
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 Evidence={ECO:0000269|PubMed:31554701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18630;
CC Evidence={ECO:0000269|PubMed:31554701};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:31554701};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=203 uM for ATP {ECO:0000269|PubMed:31554701};
CC KM=283 uM for CTP {ECO:0000269|PubMed:31554701};
CC KM=522 uM for GTP {ECO:0000269|PubMed:31554701};
CC KM=207 uM for UTP {ECO:0000269|PubMed:31554701};
CC KM=147 uM for NAD(+) {ECO:0000269|PubMed:31554701};
CC -!- SUBUNIT: Interacts with calmodulin (CaM) in a calcium Ca(2+)-dependent
CC manner in vitro. {ECO:0000269|PubMed:31554701}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:31554701}; Peripheral membrane protein
CC {ECO:0000269|PubMed:31554701}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:31554701}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70448.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ANM60529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000104; AAB70448.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27678.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60529.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK227002; BAE99067.1; -; mRNA.
DR EMBL; X62461; CAA44318.1; -; Genomic_DNA.
DR EMBL; BT026374; ABH04481.1; -; mRNA.
DR RefSeq; NP_001322810.1; NM_001331471.1.
DR RefSeq; NP_171924.2; NM_100309.4.
DR AlphaFoldDB; Q0WUY1; -.
DR STRING; 3702.AT1G04280.1; -.
DR PaxDb; Q0WUY1; -.
DR PRIDE; Q0WUY1; -.
DR ProteomicsDB; 177679; -.
DR ProteomicsDB; 192050; -.
DR EnsemblPlants; AT1G04280.1; AT1G04280.1; AT1G04280.
DR GeneID; 839555; -.
DR Gramene; AT1G04280.1; AT1G04280.1; AT1G04280.
DR KEGG; ath:AT1G04280; -.
DR Araport; AT1G04280; -.
DR TAIR; locus:2018304; AT1G04280.
DR eggNOG; ENOG502QPRV; Eukaryota.
DR HOGENOM; CLU_021671_0_0_1; -.
DR InParanoid; Q0WUY1; -.
DR OrthoDB; 422273at2759; -.
DR PhylomeDB; Q0WUY1; -.
DR PRO; PR:Q0WUY1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WUY1; baseline and differential.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR GO; GO:0003951; F:NAD+ kinase activity; IDA:TAIR.
DR GO; GO:0006741; P:NADP biosynthetic process; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044802; NADKc-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010488; Zeta_toxin_domain.
DR PANTHER; PTHR31153; PTHR31153; 1.
DR Pfam; PF06414; Zeta_toxin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Kinase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..534
FT /note="Calmodulin calcium-dependent NAD kinase"
FT /id="PRO_0000448694"
FT REGION 167..196
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:31554701"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97QZ1"
SQ SEQUENCE 534 AA; 59977 MW; F39D2EEE70F12766 CRC64;
MVKPLGEGTR DVSNVGCKSV DLLLASLGGL AAAVAAAYAG ELLLRRRKLD QGASMGYKDV
KIAPLIERKD SGRRSNLERF SHYVARQLGF EDPNEYPQLC KLANGYLLKT KGYDENVDEY
LENEAERDSL YVHLLEEFDR CILTYFSFNW TQSSNLISQA LSDESDQKVP KLKDFVMAAT
RKQRFERVTK DLKVKRVIST LVEEMRVIGS GSSEPHCTEV MSPVAHNKRS PVLLLMGGGM
GAGKSTVLKD IFLESFWSEA QADAVVIEAD AFKETDVIYR ALSSRGHHDD MLQTAELVHQ
SSTDAASSLL VTALNDGRDV IMDGTLSWEP FVEQMIEMAR NVHKQKYRMG EGYKVSEEGT
ITEKYWEEEE EETKENGKQQ NLKPYRIELV GVVCDAYLAV ARGIRRALMV KRAVRVKPQL
NSHKRFANAF PKYCELVDNA RLYCTNAVGG PPRLIAWKDG NSKLLVDPED IDCLKRVSSL
NPDAESIYEL YPDPSQLSKP GSVWNDVVLV PSRPKVQKEL SDAIRRIEKA QPKN
