NADK1_SYNY3
ID NADK1_SYNY3 Reviewed; 307 AA.
AC P73955;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=NAD kinase 1 {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};
DE AltName: Full=ATP-dependent NAD kinase 1 {ECO:0000255|HAMAP-Rule:MF_00361};
GN Name=nadK1 {ECO:0000255|HAMAP-Rule:MF_00361}; OrderedLocusNames=sll1415;
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).
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). Essential for photoheterotrophic growth
CC (PubMed:22056937, PubMed:30693583). Has a significant function in the
CC oxidative pentose phosphate (OPP) pathway for glucose catabolism under
CC photoheterotrophic conditions (PubMed:30693583). Is also involved in
CC cellular redox homeostasis (PubMed:22056937).
CC {ECO:0000269|PubMed:22056937, ECO:0000269|PubMed:30693583}.
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 -!- 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: Induced after transfer to photoheterotrophic conditions.
CC {ECO:0000269|PubMed:30693583}.
CC -!- DISRUPTION PHENOTYPE: Insertion mutant shows a strong decrease in NADK
CC activity compared to the wild-type (PubMed:22056937, PubMed:27657983).
CC Under photoheterotrophic conditions, mutant shows a greatly reduced
CC growth 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, and mutant shows a metabolic pattern similar
CC to that of wild-type (PubMed:27657983). Deficient mutant accumulates
CC glycogen under photoheterotrophic conditions (PubMed:30693583).
CC {ECO:0000269|PubMed:22056937, ECO:0000269|PubMed:27657983,
CC ECO:0000269|PubMed:30693583}.
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; BAA18022.1; -; Genomic_DNA.
DR PIR; S75461; S75461.
DR AlphaFoldDB; P73955; -.
DR SMR; P73955; -.
DR STRING; 1148.1653106; -.
DR PaxDb; P73955; -.
DR EnsemblBacteria; BAA18022; BAA18022; BAA18022.
DR KEGG; syn:sll1415; -.
DR eggNOG; COG0061; Bacteria.
DR InParanoid; P73955; -.
DR OMA; LNEMCIK; -.
DR PhylomeDB; P73955; -.
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..307
FT /note="NAD kinase 1"
FT /id="PRO_0000120679"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 67..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 149..150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 192..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ SEQUENCE 307 AA; 33776 MW; 64EA0964EE45F4EF CRC64;
MELKQVIIAH KAGHNESKTY AERCARELEA RGCKVLMGPS GIKDNPYPVF LASATEKIDL
ALVLGGDGTT LAAARHLSPE GIPILSVNVG GHLGFLTEPF DVFQDTQKVW DRLNQDRYAV
SQRMMLAASL FEGDRRDPQM VGETYYCLNE MCIKPASIDR MPTAIIEVEV DGELIDQYQC
DGLLVATPTG STCYTSSANG PILHPGMDAI VITPICPLSL SSRPIVIPPG SSVNIWPLGD
FELNTKLWTD GSLATGVWPG QRVGVWMAHR AAQFILLRES YSFYKTLRDK LQWAGARFLY
DGNNKVN
