NADK1_LISMO
ID NADK1_LISMO Reviewed; 264 AA.
AC Q8Y8D7;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 {ECO:0000255|HAMAP-Rule:MF_00361};
GN Name=nadK1 {ECO:0000255|HAMAP-Rule:MF_00361}; OrderedLocusNames=lmo0968;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-45 IN
RP COMPLEX WITH NAD AND NAD ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
RP OF ASP-45 AND HIS-223, ACTIVE SITE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=17686780; DOI=10.1074/jbc.m701394200;
RA Poncet-Montange G., Assairi L., Arold S., Pochet S., Labesse G.;
RT "NAD kinases use substrate-assisted catalysis for specific recognition of
RT NAD.";
RL J. Biol. Chem. 282:33925-33934(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF WILD-TYPE AND MUTANT GLU-223 IN
RP COMPLEX WITH NAD ANALOGS, FUNCTION, MUTAGENESIS OF HIS-223, AND ACTIVITY
RP REGULATION.
RX PubMed=22608967; DOI=10.1016/j.str.2012.03.024;
RA Gelin M., Poncet-Montange G., Assairi L., Morellato L., Huteau V.,
RA Dugue L., Dussurget O., Pochet S., Labesse G.;
RT "Screening and in situ synthesis using crystals of a NAD kinase lead to a
RT potent antistaphylococcal compound.";
RL Structure 20:1107-1117(2012).
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, ECO:0000269|PubMed:17686780,
CC ECO:0000269|PubMed:22608967}.
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:17686780};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC -!- ACTIVITY REGULATION: Competitively inhibited by 5'-thioacetyladenosine
CC (TAA) and di-(5'-thioadenosine) (DTA). {ECO:0000269|PubMed:17686780,
CC ECO:0000269|PubMed:22608967}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 mM for ATP (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17686780};
CC Vmax=6.67 umol/min/mg enzyme (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17686780};
CC Note=kcat is 13.78 sec(-1) for kinase activity with ATP (at pH 7.5
CC and 30 degrees Celsius). kcat is 13.12 sec(-1) for kinase activity
CC with NAD (at pH 7.5 and 30 degrees Celsius).;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17686780,
CC ECO:0000269|PubMed:22608967}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL591977; CAC99046.1; -; Genomic_DNA.
DR PIR; AH1195; AH1195.
DR RefSeq; NP_464493.1; NC_003210.1.
DR RefSeq; WP_003729850.1; NZ_CP023861.1.
DR PDB; 2I1W; X-ray; 2.34 A; A/B/C/D=1-264.
DR PDB; 2I29; X-ray; 2.10 A; A=1-264.
DR PDB; 2I2A; X-ray; 2.10 A; A=1-264.
DR PDB; 2I2B; X-ray; 2.10 A; A=1-264.
DR PDB; 2I2C; X-ray; 1.85 A; A=1-264.
DR PDB; 2I2D; X-ray; 2.22 A; A=1-264.
DR PDB; 2I2F; X-ray; 1.90 A; A=1-264.
DR PDB; 2Q5F; X-ray; 1.90 A; A=1-264.
DR PDB; 3V7U; X-ray; 1.97 A; A=1-264.
DR PDB; 3V7W; X-ray; 2.01 A; A=1-264.
DR PDB; 3V7Y; X-ray; 1.97 A; A=1-264.
DR PDB; 3V80; X-ray; 2.03 A; A=1-264.
DR PDB; 3V8M; X-ray; 2.48 A; A=1-264.
DR PDB; 3V8N; X-ray; 2.38 A; A=1-264.
DR PDB; 3V8P; X-ray; 2.29 A; A=1-264.
DR PDB; 3V8Q; X-ray; 2.37 A; A=1-264.
DR PDB; 3V8R; X-ray; 2.39 A; A=1-264.
DR PDB; 4DY6; X-ray; 2.20 A; A=1-264.
DR PDB; 5DHP; X-ray; 2.27 A; A/B/C/D=1-264.
DR PDB; 5DHQ; X-ray; 2.29 A; A/B/C/D=1-264.
DR PDB; 5DHR; X-ray; 2.31 A; A/B/C/D=1-264.
DR PDB; 5DHS; X-ray; 2.62 A; A/B/C/D=1-264.
DR PDB; 5DHT; X-ray; 2.59 A; A/B/C/D=1-264.
DR PDB; 5DHU; X-ray; 2.33 A; A/B/C/D=1-264.
DR PDB; 5EJF; X-ray; 2.12 A; A/B/C/D=1-264.
DR PDB; 5EJG; X-ray; 2.88 A; A/B/C/D=1-264.
DR PDB; 5EJH; X-ray; 2.00 A; A=1-264.
DR PDB; 5EJI; X-ray; 2.29 A; A=1-264.
DR PDB; 6RBO; X-ray; 1.94 A; A=1-264.
DR PDB; 6RBP; X-ray; 2.47 A; A=1-264.
DR PDB; 6RBQ; X-ray; 2.24 A; A=1-264.
DR PDB; 6RBR; X-ray; 2.06 A; A=1-264.
DR PDB; 6RBS; X-ray; 2.32 A; A=1-264.
DR PDB; 6RBT; X-ray; 2.55 A; A=1-264.
DR PDB; 6RBU; X-ray; 1.97 A; A=1-264.
DR PDB; 6RBV; X-ray; 2.29 A; A=1-264.
DR PDB; 6RBW; X-ray; 2.50 A; A=1-264.
DR PDB; 6RBX; X-ray; 2.47 A; A=1-264.
DR PDB; 6RBY; X-ray; 2.31 A; A=1-264.
DR PDB; 6RBZ; X-ray; 2.32 A; A=1-264.
DR PDB; 6RC0; X-ray; 2.75 A; A=1-264.
DR PDB; 6RC1; X-ray; 2.54 A; A=1-264.
DR PDB; 6RC2; X-ray; 2.05 A; A=1-264.
DR PDB; 6RC3; X-ray; 2.31 A; A=1-264.
DR PDB; 6RC4; X-ray; 2.28 A; A=1-264.
DR PDB; 6RC5; X-ray; 2.04 A; A=1-264.
DR PDB; 6RC6; X-ray; 2.29 A; A=1-264.
DR PDB; 6RG6; X-ray; 2.52 A; A=1-264.
DR PDB; 6RG7; X-ray; 2.08 A; A=1-264.
DR PDB; 6RG8; X-ray; 2.47 A; A=1-264.
DR PDB; 6RG9; X-ray; 2.08 A; A=1-264.
DR PDB; 6RGA; X-ray; 2.18 A; A=1-264.
DR PDB; 6RGB; X-ray; 2.25 A; A=1-264.
DR PDB; 6RGC; X-ray; 2.19 A; A=1-264.
DR PDB; 6RGD; X-ray; 2.30 A; A=1-264.
DR PDB; 6RGE; X-ray; 1.80 A; A=1-264.
DR PDB; 6RGF; X-ray; 2.30 A; A=1-264.
DR PDB; 6RR2; X-ray; 1.99 A; A=1-264.
DR PDB; 6Z61; X-ray; 2.47 A; A=1-264.
DR PDB; 6Z64; X-ray; 1.89 A; A=1-264.
DR PDB; 6Z65; X-ray; 1.97 A; A=1-264.
DR PDBsum; 2I1W; -.
DR PDBsum; 2I29; -.
DR PDBsum; 2I2A; -.
DR PDBsum; 2I2B; -.
DR PDBsum; 2I2C; -.
DR PDBsum; 2I2D; -.
DR PDBsum; 2I2F; -.
DR PDBsum; 2Q5F; -.
DR PDBsum; 3V7U; -.
DR PDBsum; 3V7W; -.
DR PDBsum; 3V7Y; -.
DR PDBsum; 3V80; -.
DR PDBsum; 3V8M; -.
DR PDBsum; 3V8N; -.
DR PDBsum; 3V8P; -.
DR PDBsum; 3V8Q; -.
DR PDBsum; 3V8R; -.
DR PDBsum; 4DY6; -.
DR PDBsum; 5DHP; -.
DR PDBsum; 5DHQ; -.
DR PDBsum; 5DHR; -.
DR PDBsum; 5DHS; -.
DR PDBsum; 5DHT; -.
DR PDBsum; 5DHU; -.
DR PDBsum; 5EJF; -.
DR PDBsum; 5EJG; -.
DR PDBsum; 5EJH; -.
DR PDBsum; 5EJI; -.
DR PDBsum; 6RBO; -.
DR PDBsum; 6RBP; -.
DR PDBsum; 6RBQ; -.
DR PDBsum; 6RBR; -.
DR PDBsum; 6RBS; -.
DR PDBsum; 6RBT; -.
DR PDBsum; 6RBU; -.
DR PDBsum; 6RBV; -.
DR PDBsum; 6RBW; -.
DR PDBsum; 6RBX; -.
DR PDBsum; 6RBY; -.
DR PDBsum; 6RBZ; -.
DR PDBsum; 6RC0; -.
DR PDBsum; 6RC1; -.
DR PDBsum; 6RC2; -.
DR PDBsum; 6RC3; -.
DR PDBsum; 6RC4; -.
DR PDBsum; 6RC5; -.
DR PDBsum; 6RC6; -.
DR PDBsum; 6RG6; -.
DR PDBsum; 6RG7; -.
DR PDBsum; 6RG8; -.
DR PDBsum; 6RG9; -.
DR PDBsum; 6RGA; -.
DR PDBsum; 6RGB; -.
DR PDBsum; 6RGC; -.
DR PDBsum; 6RGD; -.
DR PDBsum; 6RGE; -.
DR PDBsum; 6RGF; -.
DR PDBsum; 6RR2; -.
DR PDBsum; 6Z61; -.
DR PDBsum; 6Z64; -.
DR PDBsum; 6Z65; -.
DR AlphaFoldDB; Q8Y8D7; -.
DR SMR; Q8Y8D7; -.
DR STRING; 169963.lmo0968; -.
DR BindingDB; Q8Y8D7; -.
DR ChEMBL; CHEMBL4523411; -.
DR PaxDb; Q8Y8D7; -.
DR EnsemblBacteria; CAC99046; CAC99046; CAC99046.
DR GeneID; 986453; -.
DR KEGG; lmo:lmo0968; -.
DR PATRIC; fig|169963.11.peg.995; -.
DR eggNOG; COG0061; Bacteria.
DR HOGENOM; CLU_008831_0_3_9; -.
DR OMA; NGIERMS; -.
DR PhylomeDB; Q8Y8D7; -.
DR BioCyc; LMON169963:LMO0968-MON; -.
DR BRENDA; 2.7.1.23; 3045.
DR EvolutionaryTrace; Q8Y8D7; -.
DR Proteomes; UP000000817; 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..264
FT /note="NAD kinase 1"
FT /id="PRO_0000120632"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:17686780"
FT BINDING 45..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:17686780"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:17686780"
FT BINDING 122..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:17686780"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:17686780"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:17686780"
FT BINDING 161..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:17686780"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361,
FT ECO:0000269|PubMed:17686780"
FT MUTAGEN 45
FT /note="D->N: Only minor changes in the structure and a 10-
FT fold decrease in the kinase activity."
FT /evidence="ECO:0000269|PubMed:17686780"
FT MUTAGEN 223
FT /note="H->E: Twice less active than the wild-type. Its
FT activity toward DTA is increased 2-fold."
FT /evidence="ECO:0000269|PubMed:17686780,
FT ECO:0000269|PubMed:22608967"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6RGE"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:6RGE"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3V7W"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6RGE"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:6RGE"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:6RGE"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6RGE"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6RGE"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2I1W"
FT STRAND 116..131
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 142..155
FT /evidence="ECO:0007829|PDB:6RGE"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6RGE"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:6RGE"
FT STRAND 233..247
FT /evidence="ECO:0007829|PDB:6RGE"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:6RGE"
SQ SEQUENCE 264 AA; 29933 MW; 00E0BCC4CAD30653 CRC64;
MKYMITSKGD EKSDLLRLNM IAGFGEYDME YDDVEPEIVI SIGGDGTFLS AFHQYEERLD
EIAFIGIHTG HLGFYADWRP AEADKLVKLL AKGEYQKVSY PLLKTTVKYG IGKKEATYLA
LNESTVKSSG GPFVVDVVIN DIHFERFRGD GLCMSTPSGT TAYNKSLGGA LMHPSIEAMQ
LTEMASINNR VYRTIGSPLV FPKHHVVSLQ PVNDKDFQIS VDHLSILHRD VQEIRYEVSA
KKIHFARFRS FPFWRRVHDS FIED
