NADK_SALTY
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 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=STM2683;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; 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; P65774; -.
DR DNASU; 1254206; -.
DR EnsemblBacteria; AAL21572; AAL21572; STM2683.
DR GeneID; 1254206; -.
DR KEGG; stm:STM2683; -.
DR PATRIC; fig|99287.12.peg.2828; -.
DR HOGENOM; CLU_008831_0_1_6; -.
DR OMA; VNLGHVG; -.
DR PhylomeDB; P65774; -.
DR BioCyc; SENT99287:STM2683-MON; -.
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 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 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
