NADK1_BACSU
ID NADK1_BACSU Reviewed; 266 AA.
AC O31612;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
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};
DE AltName: Full=Poly(P)-dependent NAD kinase;
DE Short=PPNK;
GN Name=ppnKA; Synonyms=nadF, yjbN; OrderedLocusNames=BSU11610;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP COFACTOR, SUBUNIT, AND NOMENCLATURE.
RC STRAIN=168;
RX PubMed=12897004; DOI=10.1128/jb.185.16.4844-4850.2003;
RA Garavaglia S., Galizzi A., Rizzi M.;
RT "Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic
RT acid.";
RL J. Bacteriol. 185:4844-4850(2003).
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 (GTP, UTP) as well as inorganic polyphosphate
CC (poly(P)) as a source of phosphorus. {ECO:0000255|HAMAP-Rule:MF_00361,
CC ECO:0000269|PubMed:12897004}.
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:12897004};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361,
CC ECO:0000269|PubMed:12897004};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361,
CC ECO:0000269|PubMed:12897004};
CC Note=Divalent metal ions. Both Ca(2+) and Mn(2+) ions are more
CC effective activators than zinc, cobalt, copper and magnesium ions at
CC low concentrations. {ECO:0000255|HAMAP-Rule:MF_00361,
CC ECO:0000269|PubMed:12897004};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by NADP and activated by
CC quinolinic acid. Strongly inhibited by HgCl(2).
CC {ECO:0000269|PubMed:12897004}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.73 mM for NAD (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12897004};
CC Vmax=3.82 umol/min/mg enzyme (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12897004};
CC Note=kcat is 8 sec(-1) for kinase activity with NAD (at pH 7.8 and 25
CC degrees Celsius).;
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:12897004};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. Half of the activity is
CC lost after treatment at 40 degrees Celsius for 15 minutes.
CC {ECO:0000269|PubMed:12897004};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12897004}.
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; AL009126; CAB13018.1; -; Genomic_DNA.
DR PIR; F69844; F69844.
DR RefSeq; NP_389043.1; NC_000964.3.
DR RefSeq; WP_003232918.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31612; -.
DR SMR; O31612; -.
DR STRING; 224308.BSU11610; -.
DR PaxDb; O31612; -.
DR PRIDE; O31612; -.
DR EnsemblBacteria; CAB13018; CAB13018; BSU_11610.
DR GeneID; 936414; -.
DR KEGG; bsu:BSU11610; -.
DR PATRIC; fig|224308.179.peg.1250; -.
DR eggNOG; COG0061; Bacteria.
DR InParanoid; O31612; -.
DR OMA; NGIERMS; -.
DR PhylomeDB; O31612; -.
DR BioCyc; BSUB:BSU11610-MON; -.
DR BRENDA; 2.7.1.23; 658.
DR SABIO-RK; O31612; -.
DR Proteomes; UP000001570; 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 ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; NAD; NADP;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..266
FT /note="NAD kinase 1"
FT /id="PRO_0000120598"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 45..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 122..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
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="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 161..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ SEQUENCE 266 AA; 30012 MW; 82FA00BC6FE53364 CRC64;
MKFAVSSKGD QVSDTLKSKI QAYLLDFDME LDENEPEIVI SVGGDGTLLY AFHRYSDRLD
KTAFVGVHTG HLGFYADWVP HEIEKLVLAI AKTPYHTVEY PLLEVIVTYH ENEREERYLA
LNECTIKSIE GSLVADVEIK GQLFETFRGD GLCLSTPSGS TAYNKALGGA IIHPSIRAIQ
LAEMASINNR VFRTVGSPLL LPSHHDCMIK PRNEVDFQVT IDHLTLLHKD VKSIRCQVAS
EKVRFARFRP FPFWKRVQDS FIGKGE
