NADK2_SYNY3
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 03-AUG-2022, entry version 127.
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}; OrderedLocusNames=slr0400;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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; 1148.1653618; -.
DR PaxDb; P74430; -.
DR EnsemblBacteria; BAA18530; BAA18530; BAA18530.
DR KEGG; syn:slr0400; -.
DR eggNOG; COG0061; Bacteria.
DR InParanoid; P74430; -.
DR OMA; VNLGHVG; -.
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 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 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
