ID   NADK2_SYNY3             Reviewed;         305 AA.
AC   P74430;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=NAD kinase 2 {ECO:0000255|HAMAP-Rule:MF_00361};
DE            EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000305|PubMed:22056937, ECO:0000305|PubMed:27657983, ECO:0000305|PubMed:33560438};
DE   AltName: Full=ATP-dependent NAD kinase 2 {ECO:0000255|HAMAP-Rule:MF_00361};
GN   Name=nadK2 {ECO:0000255|HAMAP-Rule:MF_00361};
GN   OrderedLocusNames=slr0400;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=22056937; DOI=10.1128/jb.05873-11;
RA   Gao H., Xu X.;
RT   "The cyanobacterial NAD kinase gene sll1415 is required for
RT   photoheterotrophic growth and cellular redox homeostasis in Synechocystis
RT   sp. strain PCC 6803.";
RL   J. Bacteriol. 194:218-224(2012).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=27657983; DOI=10.1016/j.jplph.2016.09.002;
RA   Ishikawa Y., Miyagi A., Haishima Y., Ishikawa T., Nagano M., Yamaguchi M.,
RA   Hihara Y., Kawai-Yamada M.;
RT   "Metabolomic analysis of NAD kinase-deficient mutants of the cyanobacterium
RT   Synechocystis sp. PCC 6803.";
RL   J. Plant Physiol. 205:105-112(2016).
RN   [4]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=30693583; DOI=10.1111/tpj.14262;
RA   Ishikawa Y., Miyagi A., Ishikawa T., Nagano M., Yamaguchi M., Hihara Y.,
RA   Kaneko Y., Kawai-Yamada M.;
RT   "One of the NAD kinases, sll1415, is required for the glucose metabolism of
RT   Synechocystis sp. PCC 6803.";
RL   Plant J. 98:654-666(2019).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=33560438; DOI=10.1093/pcp/pcab023;
RA   Ishikawa Y., Cassan C., Kadeer A., Yuasa K., Sato N., Sonoike K.,
RA   Kaneko Y., Miyagi A., Takahashi H., Ishikawa T., Yamaguchi M.,
RA   Nishiyama Y., Hihara Y., Gibon Y., Kawai-Yamada M.;
RT   "The NAD kinase Slr0400 functions as a growth repressor in Synechocystis
RT   sp. PCC 6803.";
RL   Plant Cell Physiol. 62:668-677(2021).
CC   -!- FUNCTION: Involved in the regulation of the intracellular balance of
CC       NAD and NADP, and is a key enzyme in the biosynthesis of NADP.
CC       Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
CC       adenosine moiety of NAD to yield NADP (PubMed:22056937,
CC       PubMed:30693583). Functions as a growth repressor under light-activated
CC       heterotrophic growth conditions and light and dark cycle conditions in
CC       the presence of glucose (PubMed:33560438). NADP(H)/NAD(H) maintenance
CC       by slr0400 probably plays a significant role in modulating glycolysis
CC       and the TCA cycle to repress the growth rate and maintain the
CC       photosynthetic capacity (PubMed:33560438).
CC       {ECO:0000269|PubMed:22056937, ECO:0000269|PubMed:30693583,
CC       ECO:0000269|PubMed:33560438}.
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:0000255|HAMAP-Rule:MF_00361,
CC         ECO:0000305|PubMed:22056937, ECO:0000305|PubMed:27657983,
CC         ECO:0000305|PubMed:33560438};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
CC   -!- INDUCTION: Expression decreases after transfer to photoheterotrophic
CC       conditions. {ECO:0000269|PubMed:30693583}.
CC   -!- DISRUPTION PHENOTYPE: Insertion mutant shows a slight decrease in NADK
CC       activity compared to the wild-type (PubMed:22056937, PubMed:27657983).
CC       Under photoheterotrophic conditions, mutation does not affect growth
CC       rate (PubMed:22056937, PubMed:30693583). Under photoautotrophic
CC       conditions, the growth curves of the wild-type parent and the mutant do
CC       not show any differences, but mutant shows large differences in
CC       NAD(P)(H) levels along with massive changes in metabolite profile
CC       (PubMed:27657983). Mutant exhibits a fast-growth phenotype under light-
CC       activated heterotrophic growth conditions and light and dark cycle
CC       conditions in the presence of glucose (PubMed:33560438).
CC       {ECO:0000269|PubMed:22056937, ECO:0000269|PubMed:27657983,
CC       ECO:0000269|PubMed:30693583, ECO:0000269|PubMed:33560438}.
CC   -!- MISCELLANEOUS: NADK activity derived from sll1415 makes probably a
CC       larger contribution to total cellular NADK activity than activity
CC       derived from slr0400 (PubMed:22056937, PubMed:27657983). Slr0400 cannot
CC       functionally replace sll1415 under photoheterotrophic conditions
CC       (PubMed:30693583). {ECO:0000269|PubMed:22056937,
CC       ECO:0000269|PubMed:27657983, ECO:0000269|PubMed:30693583}.
CC   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
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DR   EMBL; BA000022; BAA18530.1; -; Genomic_DNA.
DR   PIR; S76401; S76401.
DR   AlphaFoldDB; P74430; -.
DR   SMR; P74430; -.
DR   STRING; 1148.gene:10499411; -.
DR   PaxDb; 1148-1653618; -.
DR   EnsemblBacteria; BAA18530; BAA18530; BAA18530.
DR   KEGG; syn:slr0400; -.
DR   eggNOG; COG0061; Bacteria.
DR   InParanoid; P74430; -.
DR   PhylomeDB; P74430; -.
DR   BRENDA; 2.7.1.23; 382.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProt.
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   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:SF13; NAD 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.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..305
FT                   /note="NAD kinase 2"
FT                   /id="PRO_0000120678"
FT   ACT_SITE        78
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         78..79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         152..153
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         193..198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   305 AA;  33398 MW;  695ED7EA16244E2C CRC64;
     MPKVGIIFND DKPTACSVAQ ELQEQLQQSG FTVAMETGSG GLLGYSQPDR PICHTRIEHL
     TPPHFDESMP FAIVLGGDGT VLSAFRQLAP LGIPLLTINT GHMGFLTEIY LNQLPTAIEQ
     LINGDYQIES RSMMTVRLMR EENLLWEALS LNEMVLHREP LTSMCHFEIQ VGYHASVDIA
     ADGIIVSTPT GSTAYSLSAG GPVVTPDVPV FQLAPICPHS LASRALVFSD LEPVTIFPAT
     PNRMVLVVDG NGGCYVLPED RVHLSKSPYP AKFIRLQTPE FFRILREKLG WGLPHIAKPT
     SVELP
//