NADK_ECOLI
ID NADK_ECOLI Reviewed; 292 AA.
AC P0A7B3; P37768; P46140; P77490;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; Synonyms=yfjB, yfjE;
GN OrderedLocusNames=b2615, JW2596;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-163.
RC STRAIN=B178;
RX PubMed=3045760; DOI=10.1093/nar/16.15.7545;
RA Lipinska B., King J., Ang D., Georgopoulos C.;
RT "Sequence analysis and transcriptional regulation of the Escherichia coli
RT grpE gene, encoding a heat shock protein.";
RL Nucleic Acids Res. 16:7545-7562(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-292.
RC STRAIN=K12;
RX PubMed=3037486; DOI=10.1093/nar/15.13.5041;
RA Rostas K., Morton S.J., Picksley S.M., Lloyd R.G.;
RT "Nucleotide sequence and LexA regulation of the Escherichia coli recN
RT gene.";
RL Nucleic Acids Res. 15:5041-5049(1987).
RN [6]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR,
RP AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11488932; DOI=10.1046/j.1432-1327.2001.02358.x;
RA Kawai S., Mori S., Mukai T., Hashimoto W., Murata K.;
RT "Molecular characterization of Escherichia coli NAD kinase.";
RL Eur. J. Biochem. 268:4359-4365(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=3025169; DOI=10.1128/jb.169.1.184-188.1987;
RA Zerez C.R., Moul D.E., Gomez E.G., Lopez V.M., Andreoli A.J.;
RT "Negative modulation of Escherichia coli NAD kinase by NADPH and NADH.";
RL J. Bacteriol. 169:184-188(1987).
RN [8]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-175, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND BINDING SPECIFICITY.
RX PubMed=15855156; DOI=10.1074/jbc.m502518200;
RA Mori S., Kawai S., Shi F., Mikami B., Murata K.;
RT "Molecular conversion of NAD kinase to NADH kinase through single amino
RT acid residue substitution.";
RL J. Biol. Chem. 280:24104-24112(2005).
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 (UTP, CTP, GTP, dATP, TTP) as phosphoryl
CC donors, while nucleoside mono- or diphosphates and poly(P) cannot.
CC {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:11488932,
CC ECO:0000269|PubMed:15855156, ECO:0000269|PubMed:3025169}.
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:11488932, ECO:0000269|PubMed:15855156,
CC ECO:0000269|PubMed:3025169};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361,
CC ECO:0000269|PubMed:11488932};
CC -!- ACTIVITY REGULATION: Competitively and allosterically inhibited by NADH
CC and NADPH at physiological concentrations, whereas inhibition by NADP
CC is only slight. Inhibited by p-chloromercuribenzoate and HgCl(2).
CC {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:3025169}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 mM for NAD (at pH 7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156,
CC ECO:0000269|PubMed:3025169};
CC KM=2.5 mM for ATP (at pH 7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156,
CC ECO:0000269|PubMed:3025169};
CC KM=4.1 mM for magnesium (at pH 7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156,
CC ECO:0000269|PubMed:3025169};
CC Vmax=12.86 umol/min/mg enzyme (at pH 7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156,
CC ECO:0000269|PubMed:3025169};
CC Note=kcat is 55 sec(-1) for kinase activity with ATP. kcat is 125
CC sec(-1) for kinase activity with NAD.;
CC pH dependence:
CC Optimum pH is between 7.2 and 7.5. {ECO:0000269|PubMed:11488932,
CC ECO:0000269|PubMed:15855156, ECO:0000269|PubMed:3025169};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius and half of the activity is
CC lost on treatment at 65 degrees Celsius for 10 minutes.
CC {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156,
CC ECO:0000269|PubMed:3025169};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:11488932}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=X07863; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=Y00357; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U36840; AAA79785.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75664.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16500.1; -; Genomic_DNA.
DR EMBL; X07863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Y00357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B65040; B65040.
DR RefSeq; NP_417105.1; NC_000913.3.
DR RefSeq; WP_001059169.1; NZ_STEB01000040.1.
DR AlphaFoldDB; P0A7B3; -.
DR SMR; P0A7B3; -.
DR BioGRID; 4260607; 19.
DR BioGRID; 851428; 4.
DR DIP; DIP-48103N; -.
DR IntAct; P0A7B3; 4.
DR STRING; 511145.b2615; -.
DR jPOST; P0A7B3; -.
DR PaxDb; P0A7B3; -.
DR PRIDE; P0A7B3; -.
DR EnsemblBacteria; AAC75664; AAC75664; b2615.
DR EnsemblBacteria; BAA16500; BAA16500; BAA16500.
DR GeneID; 67414068; -.
DR GeneID; 947092; -.
DR KEGG; ecj:JW2596; -.
DR KEGG; eco:b2615; -.
DR PATRIC; fig|1411691.4.peg.4124; -.
DR EchoBASE; EB2109; -.
DR eggNOG; COG0061; Bacteria.
DR HOGENOM; CLU_008831_0_1_6; -.
DR InParanoid; P0A7B3; -.
DR OMA; VNLGHVG; -.
DR PhylomeDB; P0A7B3; -.
DR BioCyc; EcoCyc:MON0-541; -.
DR BioCyc; MetaCyc:MON0-541; -.
DR BRENDA; 2.7.1.23; 414.
DR SABIO-RK; P0A7B3; -.
DR PRO; PR:P0A7B3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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:EcoCyc.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IDA:EcoCyc.
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 ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; NAD; NADP;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..292
FT /note="NAD kinase"
FT /id="PRO_0000120616"
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 MUTAGEN 175
FT /note="R->E: Does not exhibit NADH kinase activity in
FT addition to NAD kinase activity."
FT /evidence="ECO:0000269|PubMed:15855156"
FT MUTAGEN 175
FT /note="R->G: Exhibits NADH kinase activity in addition to
FT NAD kinase activity. Reduces the Vmax of the NAD kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:15855156"
FT MUTAGEN 175
FT /note="R->H: Exhibits NADH kinase activity in addition to
FT NAD kinase activity."
FT /evidence="ECO:0000269|PubMed:15855156"
FT MUTAGEN 175
FT /note="R->I: Does not exhibit NADH kinase activity in
FT addition to NAD kinase activity."
FT /evidence="ECO:0000269|PubMed:15855156"
FT MUTAGEN 175
FT /note="R->K: Does not exhibit NADH kinase activity in
FT addition to NAD kinase activity."
FT /evidence="ECO:0000269|PubMed:15855156"
FT MUTAGEN 175
FT /note="R->Q: Exhibits NADH kinase activity in addition to
FT NAD kinase activity."
FT /evidence="ECO:0000269|PubMed:15855156"
FT MUTAGEN 175
FT /note="R->T: Exhibits NADH kinase activity in addition to
FT NAD kinase activity."
FT /evidence="ECO:0000269|PubMed:15855156"
SQ SEQUENCE 292 AA; 32566 MW; D1E631658408F2E1 CRC64;
MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CTKGYEVIVE QQIAHELQLK NVKTGTLAEI
GQLADLAVVV GGDGNMLGAA RTLARYDIKV IGINRGNLGF LTDLDPDNAQ QQLADVLEGH
YISEKRFLLE AQVCQQDCQK RISTAINEVV LHPGKVAHMI EFEVYIDEIF AFSQRSDGLI
ISTPTGSTAY SLSAGGPILT PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRNDL
EISCDSQIAL PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF
