ID   NADK_SALTY              Reviewed;         292 AA.
AC   P65774; Q8XFN1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=NAD kinase {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 {ECO:0000255|HAMAP-Rule:MF_00361};
GN   Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361};
GN   OrderedLocusNames=STM2683;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, AND NOMENCLATURE.
RX   PubMed=16682646; DOI=10.1073/pnas.0602494103;
RA   Grose J.H., Joss L., Velick S.F., Roth J.R.;
RT   "Evidence that feedback inhibition of NAD kinase controls responses to
RT   oxidative stress.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7601-7606(2006).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RG   Midwest center for structural genomics (MCSG);
RT   "The crystal structure of a putative kinase from Salmonella typhimurim
RT   LT2.";
RL   Submitted (AUG-2005) to the PDB data bank.
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. It can use ATP and other
CC       nucleoside triphosphates as a source of phosphorus. NADH cannot replace
CC       NAD as a substrate. {ECO:0000255|HAMAP-Rule:MF_00361,
CC       ECO:0000269|PubMed:16682646}.
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:0000269|PubMed:16682646};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00361,
CC         ECO:0000269|PubMed:16682646};
CC   -!- ACTIVITY REGULATION: Allosterically inhibited by NADPH and NADH. NADPH
CC       is the primary inhibitor during aerobic growth and NADH during
CC       anaerobic growth. {ECO:0000269|PubMed:16682646}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.1 mM for NAD {ECO:0000269|PubMed:16682646};
CC         KM=2.7 mM for ATP {ECO:0000269|PubMed:16682646};
CC   -!- SUBUNIT: Equilibrium mixture of dimer and tetramer. It is converted
CC       entirely to tetramer in the presence of the inhibitor NADPH.
CC       {ECO:0000269|PubMed:16682646, ECO:0000269|Ref.3}.
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; AE006468; AAL21572.1; -; Genomic_DNA.
DR   RefSeq; NP_461613.1; NC_003197.2.
DR   RefSeq; WP_001059155.1; NC_003197.2.
DR   PDB; 2AN1; X-ray; 2.00 A; A/B/C/D=1-292.
DR   PDBsum; 2AN1; -.
DR   AlphaFoldDB; P65774; -.
DR   SMR; P65774; -.
DR   STRING; 99287.STM2683; -.
DR   PaxDb; 99287-STM2683; -.
DR   DNASU; 1254206; -.
DR   GeneID; 1254206; -.
DR   KEGG; stm:STM2683; -.
DR   PATRIC; fig|99287.12.peg.2828; -.
DR   HOGENOM; CLU_008831_0_1_6; -.
DR   OMA; SMCHFEI; -.
DR   PhylomeDB; P65774; -.
DR   BioCyc; SENT99287:STM2683-MONOMER; -.
DR   SABIO-RK; P65774; -.
DR   EvolutionaryTrace; P65774; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR   GO; GO:0003951; F:NAD+ kinase activity; IDA:UniProtKB.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..292
FT                   /note="NAD kinase"
FT                   /id="PRO_0000120655"
FT   ACT_SITE        73
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         73..74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         147..148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         177
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         188..193
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   SITE            175
FT                   /note="Responsible for conferring strict specificity to
FT                   NAD"
FT                   /evidence="ECO:0000250"
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   HELIX           22..32
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   HELIX           41..46
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   HELIX           57..63
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   HELIX           73..83
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   HELIX           109..117
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          121..134
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          142..155
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          169..182
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   HELIX           185..188
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   HELIX           190..193
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          204..212
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          221..224
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          229..233
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   STRAND          257..272
FT                   /evidence="ECO:0007829|PDB:2AN1"
FT   HELIX           277..285
FT                   /evidence="ECO:0007829|PDB:2AN1"
SQ   SEQUENCE   292 AA;  32584 MW;  93585C83A2EEF41C CRC64;
     MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CDQGYEVIVE QQIAHELQLK NVPTGTLAEI
     GQQADLAVVV GGDGNMLGAA RTLARYDINV IGINRGNLGF LTDLDPDNAL QQLSDVLEGR
     YISEKRFLLE AQVCQQDRQK RISTAINEVV LHPGKVAHMI EFEVYIDETF AFSQRSDGLI
     ISTPTGSTAY SLSAGGPILT PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRSDL
     EISCDSQIAL PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF
//