NRK1_ASHGO
ID NRK1_ASHGO Reviewed; 241 AA.
AC P62511; Q74Z64;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=AGR342C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 -!- 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 -!- SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016820; AAS54832.2; -; Genomic_DNA.
DR RefSeq; NP_987008.2; NM_212070.2.
DR AlphaFoldDB; P62511; -.
DR SMR; P62511; -.
DR STRING; 33169.AAS54832; -.
DR EnsemblFungi; AAS54832; AAS54832; AGOS_AGR342C.
DR GeneID; 4623311; -.
DR KEGG; ago:AGOS_AGR342C; -.
DR eggNOG; KOG3308; Eukaryota.
DR HOGENOM; CLU_058668_1_0_1; -.
DR InParanoid; P62511; -.
DR OMA; NCSRIEY; -.
DR UniPathway; UPA00253; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; IEA:EnsemblFungi.
DR GO; GO:0046495; P:nicotinamide riboside metabolic process; IEA:EnsemblFungi.
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 PANTHER; PTHR10285:SF158; PTHR10285:SF158; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..241
FT /note="Nicotinamide riboside kinase"
FT /id="PRO_0000215896"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 47..50
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 67..68
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 167..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 169..170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 213..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
SQ SEQUENCE 241 AA; 27239 MW; 42D107778344E403 CRC64;
MTSQLAGFKG TRGTLLVGIG GCSSSGKSTI AKLAVQVLED AVLVHQDDFY RHDDEVPFDE
EYQIGNWDVP EALDMAQFER ELDHIRATGR PAAKLVHNGN IDDVGKFGIS EEYLEELRRR
YRGRISQPVV LVDGFMLYHD DKVAARFDCR LLVRAPYATM KARRASRGGY KTLDSFWQDP
PFYFDKFVYK SYAATHARLF RNCDVEDRLV APDVQEIYNG DEAQITCVLE QVLDAIAAAQ
C
