NRK1_SCHPO
ID NRK1_SCHPO Reviewed; 230 AA.
AC Q9C0W1; O13616;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
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; ORFNames=pi025, SPBP22H7.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21404.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB004535; BAA21404.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CU329671; CAC37374.1; -; Genomic_DNA.
DR RefSeq; NP_595603.1; NM_001021498.2.
DR AlphaFoldDB; Q9C0W1; -.
DR SMR; Q9C0W1; -.
DR BioGRID; 277827; 13.
DR STRING; 4896.SPBP22H7.06.1; -.
DR MaxQB; Q9C0W1; -.
DR PaxDb; Q9C0W1; -.
DR EnsemblFungi; SPBP22H7.06.1; SPBP22H7.06.1:pep; SPBP22H7.06.
DR GeneID; 2541315; -.
DR KEGG; spo:SPBP22H7.06; -.
DR PomBase; SPBP22H7.06; nrk1.
DR VEuPathDB; FungiDB:SPBP22H7.06; -.
DR eggNOG; KOG3308; Eukaryota.
DR HOGENOM; CLU_058668_1_0_1; -.
DR InParanoid; Q9C0W1; -.
DR OMA; NCSRIEY; -.
DR PhylomeDB; Q9C0W1; -.
DR Reactome; R-SPO-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; -.
DR PRO; PR:Q9C0W1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050262; F:ribosylnicotinamide kinase activity; ISO:PomBase.
DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; ISO:PomBase.
DR GO; GO:0046495; P:nicotinamide riboside metabolic process; ISO:PomBase.
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..230
FT /note="Nicotinamide riboside kinase"
FT /id="PRO_0000215897"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 38..41
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 56..57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 157..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 159..160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 203..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
SQ SEQUENCE 230 AA; 26264 MW; 4F7D6E727482D5EB CRC64;
MTRKTIIVGV SGASCSGKST LCQLLHAIFE GSSLVHEDDF YKTDAEIPVK NGIADWDCQE
SLNLDAFLEN LHYIRDHGVL PTHLRNRENK NVAPEALIEY ADIIKEFKAP AIPTLEQHLV
FVDGFMMYVN EDLINAFDIR LMLVTDFDTL KRRREARTGY ITLEGFWQDP PHYFENYVWP
GYVHGHSHLF VNGDVTGKLL DKRIQLSPSS KMSVRDNVQW AINSILNALQ
