NRK1_YEAST
ID NRK1_YEAST Reviewed; 240 AA.
AC P53915; D6W154;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Nicotinamide riboside kinase;
DE Short=NRK;
DE Short=NmR-K;
DE EC=2.7.1.22 {ECO:0000250|UniProtKB:Q9NWW6};
DE AltName: Full=Nicotinic acid riboside kinase;
DE EC=2.7.1.173 {ECO:0000250|UniProtKB:Q9NWW6};
DE AltName: Full=Ribosylnicotinamide kinase;
DE Short=RNK;
DE AltName: Full=Ribosylnicotinic acid kinase;
GN Name=NRK1; OrderedLocusNames=YNL129W; ORFNames=N1219, N1870;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=15137942; DOI=10.1016/s0092-8674(04)00416-7;
RA Bieganowski P., Brenner C.;
RT "Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes
RT establish a Preiss-Handler independent route to NAD+ in fungi and humans.";
RL Cell 117:495-502(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside (NR)
CC and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide
CC (NMN) and nicotinic acid mononucleotide (NaMN). {ECO:0000250,
CC ECO:0000269|PubMed:15137942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-riboside = ADP + beta-nicotinamide
CC D-ribonucleotide + H(+); Xref=Rhea:RHEA:14017, ChEBI:CHEBI:14649,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.1.22;
CC Evidence={ECO:0000250|UniProtKB:Q9NWW6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-ribosylnicotinate = ADP + H(+) + nicotinate beta-
CC D-ribonucleotide; Xref=Rhea:RHEA:25568, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57502, ChEBI:CHEBI:58527,
CC ChEBI:CHEBI:456216; EC=2.7.1.173;
CC Evidence={ECO:0000250|UniProtKB:Q9NWW6};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
CC {ECO:0000250|UniProtKB:Q9NWW6}.
CC -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.
CC {ECO:0000305}.
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DR EMBL; AY611479; AAT11927.1; -; Genomic_DNA.
DR EMBL; Z46843; CAA86896.1; -; Genomic_DNA.
DR EMBL; Z71405; CAA96011.1; -; Genomic_DNA.
DR EMBL; AY558011; AAS56337.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10420.1; -; Genomic_DNA.
DR PIR; S55154; S55154.
DR RefSeq; NP_014270.1; NM_001182967.1.
DR AlphaFoldDB; P53915; -.
DR SMR; P53915; -.
DR BioGRID; 35698; 88.
DR DIP; DIP-8168N; -.
DR STRING; 4932.YNL129W; -.
DR MaxQB; P53915; -.
DR PaxDb; P53915; -.
DR PRIDE; P53915; -.
DR EnsemblFungi; YNL129W_mRNA; YNL129W; YNL129W.
DR GeneID; 855594; -.
DR KEGG; sce:YNL129W; -.
DR SGD; S000005073; NRK1.
DR VEuPathDB; FungiDB:YNL129W; -.
DR eggNOG; KOG3308; Eukaryota.
DR GeneTree; ENSGT00940000175439; -.
DR HOGENOM; CLU_058668_1_1_1; -.
DR InParanoid; P53915; -.
DR OMA; NCSRIEY; -.
DR BioCyc; MetaCyc:MON3O-4139; -.
DR BioCyc; YEAST:MON3O-4139; -.
DR BRENDA; 2.7.1.22; 984.
DR Reactome; R-SCE-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; -.
DR PRO; PR:P53915; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53915; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050262; F:ribosylnicotinamide kinase activity; IDA:SGD.
DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; IGI:SGD.
DR GO; GO:0009435; P:NAD biosynthetic process; IGI:SGD.
DR GO; GO:0046495; P:nicotinamide riboside metabolic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR026681; NRK.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR PANTHER; PTHR10285:SF158; PTHR10285:SF158; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..240
FT /note="Nicotinamide riboside kinase"
FT /id="PRO_0000215898"
FT ACT_SITE 39
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 13..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 39..42
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 59..60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 162..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 164..165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 208..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
SQ SEQUENCE 240 AA; 27690 MW; F04E99885774CF53 CRC64;
MTSKKVILVA LSGCSSSGKT TIAKLTASLF TKATLIHEDD FYKHDNEVPV DAKYNIQNWD
SPEALDFKLF GKELDVIKQT GKIATKLIHN NNVDDPFTKF HIDRQVWDEL KAKYDSINDD
KYEVVIVDGF MIFNNTGISK KFDLKILVRA PYEVLKKRRA SRKGYQTLDS FWVDPPYYFD
EFVYESYRAN HAQLFVNGDV EGLLDPRKSK NIKEFINDDD TPIAKPLSWV CQEILKLCKD
