ID   NADK1_PROM9             Reviewed;         303 AA.
AC   Q31D25;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=NAD kinase 1 {ECO:0000255|HAMAP-Rule:MF_00361};
DE            EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361};
DE   AltName: Full=ATP-dependent NAD kinase 1 {ECO:0000255|HAMAP-Rule:MF_00361};
GN   Name=nadK1 {ECO:0000255|HAMAP-Rule:MF_00361};
GN   OrderedLocusNames=PMT9312_0158;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RX   PubMed=16556843; DOI=10.1126/science.1122050;
RA   Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
RA   Delong E.F., Chisholm S.W.;
RT   "Genomic islands and the ecology and evolution of Prochlorococcus.";
RL   Science 311:1768-1770(2006).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
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   -!- 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   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
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DR   EMBL; CP000111; ABB49220.1; -; Genomic_DNA.
DR   RefSeq; WP_011375724.1; NC_007577.1.
DR   AlphaFoldDB; Q31D25; -.
DR   SMR; Q31D25; -.
DR   STRING; 74546.PMT9312_0158; -.
DR   KEGG; pmi:PMT9312_0158; -.
DR   eggNOG; COG0061; Bacteria.
DR   HOGENOM; CLU_008831_0_1_3; -.
DR   OrthoDB; 9774737at2; -.
DR   Proteomes; UP000002715; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule.
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:SF0; NAD KINASE; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   Pfam; PF20143; NAD_kinase_C; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding; Transferase.
FT   CHAIN           1..303
FT                   /note="NAD kinase 1"
FT                   /id="PRO_0000229668"
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         72
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         148..149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   303 AA;  34065 MW;  14B8B84A93AD5792 CRC64;
     MKLSLVLIIY RSDSSIALEA SKFCEEVLKA KNIKSNRIAS DFHRDEIEKN LYNTKFQPDI
     GIVLGGDGTF LKCANALADY DIPLLSINIG GNLGFLTQEK DFLFDKSFIE ILENEEYIID
     SRNRLNCNVC ISERSPEKKI IKSYDALNDF YFKSVEEAIS PTNQIQIEID NEKVNEYKGD
     GLIISTSTGS TAYSMAAGGP IVHPSIDAMI INPICPMSLA SRPIVIPNTS KVIIKPVKKS
     KGEIKLWRDG SKCMTIKETY YCEIKKGKAP CKIIKFKKST NYYNTLIKKL DWKGDLSLKN
     SKN
//