NADK_PYRHO
ID NADK_PYRHO Reviewed; 277 AA.
AC O58801;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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};
DE AltName: Full=Poly(P)-dependent NAD kinase;
DE Short=PPNK;
GN Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361}; OrderedLocusNames=PH1074;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RA Ohshima T., Sakuraba H.;
RT "Inorganic polyphosphate/ATP-NAD kinase of Pyrococcus horikoshii OT-3.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16085824; DOI=10.1128/aem.71.8.4352-4358.2005;
RA Sakuraba H., Kawakami R., Ohshima T.;
RT "First archaeal inorganic polyphosphate/ATP-dependent NAD kinase, from
RT hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and
RT characterization.";
RL Appl. Environ. Microbiol. 71:4352-4358(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 (GTP,UTP) as well as inorganic polyphosphate
CC (poly(P)) as a source of phosphorus. NAD is the preferred substrate for
CC the kinase, but NADH can also be used as phosphoryl acceptor.
CC {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:16085824}.
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:16085824};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361,
CC ECO:0000269|PubMed:16085824};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.29 mM for ATP (at pH 6 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:16085824};
CC KM=0.3 mM for NAD (with poly(P) as phosphoryl donor at pH 6.8 and 70
CC degrees Celsius) {ECO:0000269|PubMed:16085824};
CC KM=0.4 mM for NAD (with ATP as phosphoryl donor at pH 6.8 and 70
CC degrees Celsius) {ECO:0000269|PubMed:16085824};
CC pH dependence:
CC Optimum pH is 6.8. At 70 degrees Celsius for 60 minutes, the enzyme
CC does not lose activity in a pH range of 4.0 to 10.5.
CC {ECO:0000269|PubMed:16085824};
CC Temperature dependence:
CC Extremely high thermostability. Upon heating at 95 degrees Celsius
CC for 10 minutes the kinase activity is not lost, but about 80% of the
CC activity is lost upon incubation at 100 degrees Celsius for 10
CC minutes. {ECO:0000269|PubMed:16085824};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16085824}.
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; BA000001; BAA30173.1; -; Genomic_DNA.
DR EMBL; AB055976; BAB32784.1; -; Genomic_DNA.
DR PIR; G71101; G71101.
DR RefSeq; WP_010885160.1; NC_000961.1.
DR AlphaFoldDB; O58801; -.
DR SMR; O58801; -.
DR STRING; 70601.3257490; -.
DR EnsemblBacteria; BAA30173; BAA30173; BAA30173.
DR GeneID; 1443395; -.
DR KEGG; pho:PH1074; -.
DR eggNOG; arCOG01348; Archaea.
DR OMA; VNLGHVG; -.
DR OrthoDB; 104144at2157; -.
DR BRENDA; 2.7.1.23; 5244.
DR Proteomes; UP000000752; 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; Transferase.
FT CHAIN 1..277
FT /note="NAD kinase"
FT /id="PRO_0000120707"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 67..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 137..138
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 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 167
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 178..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ SEQUENCE 277 AA; 31414 MW; 707053D67637F13F CRC64;
MKFGIVARRD KEEALKLAYR VYDFLKVHGY EVVVDKETYE HFPHFKEGDV IPLDEFDVDF
IVAIGGDGTI LRIEHMTKKD IPILSINMGT LGFLTEVEPS DTFFALNRLI EGEYYIDERI
KVRTYIDGEN RVPDALNEVA ILTGIPGKII HMKYYVDGGL ADEVRADGLV VSTPTGSTGY
AMSAGGPFID PRLDVILIAP LLPLPKTSVP MVIPGSSRID IRMLTDREII LAIDGQYYEH
LPPNVEITVV KSPRKTKFIR FTREIYPKYT IRIKERH
