NRK1_RAT
ID NRK1_RAT Reviewed; 195 AA.
AC Q6AY91;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Nicotinamide riboside kinase 1;
DE Short=NRK 1;
DE Short=NmR-K 1;
DE EC=2.7.1.22 {ECO:0000250|UniProtKB:Q9NWW6};
DE AltName: Full=Nicotinic acid riboside kinase 1;
DE EC=2.7.1.173 {ECO:0000250|UniProtKB:Q9NWW6};
DE AltName: Full=Ribosylnicotinamide kinase 1;
DE Short=RNK 1;
DE AltName: Full=Ribosylnicotinic acid kinase 1;
GN Name=Nmrk1; Synonyms=Nrk1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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).
CC {ECO:0000250|UniProtKB:Q9NWW6}.
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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NWW6}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.
CC {ECO:0000305}.
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DR EMBL; BC079144; AAH79144.1; -; mRNA.
DR RefSeq; NP_001019463.1; NM_001024292.1.
DR AlphaFoldDB; Q6AY91; -.
DR SMR; Q6AY91; -.
DR STRING; 10116.ENSRNOP00000016930; -.
DR PaxDb; Q6AY91; -.
DR Ensembl; ENSRNOT00000016930; ENSRNOP00000016930; ENSRNOG00000012665.
DR GeneID; 499330; -.
DR KEGG; rno:499330; -.
DR UCSC; RGD:1564687; rat.
DR CTD; 54981; -.
DR RGD; 1564687; Nmrk1.
DR eggNOG; KOG3308; Eukaryota.
DR GeneTree; ENSGT00940000159384; -.
DR HOGENOM; CLU_058668_0_0_1; -.
DR InParanoid; Q6AY91; -.
DR OMA; NCSRIEY; -.
DR OrthoDB; 1230625at2759; -.
DR PhylomeDB; Q6AY91; -.
DR TreeFam; TF105395; -.
DR Reactome; R-RNO-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; -.
DR PRO; PR:Q6AY91; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012665; Expressed in kidney and 19 other tissues.
DR Genevisible; Q6AY91; RN.
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; ISO:RGD.
DR GO; GO:0061769; F:ribosylnicotinate kinase activity; ISO:RGD.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..195
FT /note="Nicotinamide riboside kinase 1"
FT /id="PRO_0000215893"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 36..39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 55..56
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 132..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 134..135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 172..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
SQ SEQUENCE 195 AA; 22321 MW; 5D5155621DEB7E54 CRC64;
MKTFVIGIGG VTNGGKTTLA KNLQKRLPNC SVISQDDFFK PESEIDIDEN GFLQYDVLEA
LNMEKMMSAV SCWMENPGSS AGPAALESAQ GVPILIIEGF LLFNYKPLDT IWNRSYFLTV
PYEECKRRRS TRVYEPPDPP GYFDGHVWPM YLKHRQEMNS ITWDIVYLDG TRSEEDLFSQ
VYEDVKQELE KQNGL
