ID UTR1_YEAST Reviewed; 530 AA.
AC P21373; D6VWM0; E9P8Y8; Q54AD8;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=NAD(+) kinase;
DE EC=2.7.1.23 {ECO:0000269|PubMed:11425472};
DE AltName: Full=Unknown transcript 1 protein;
GN Name=UTR1; OrderedLocusNames=YJR049C; ORFNames=J1655;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=11425472; DOI=10.1111/j.1574-6968.2001.tb10712.x;
RA Kawai S., Mori S., Suzuki S., Murata K.;
RT "Molecular cloning and identification of UTR1 of a yeast Saccharomyces
RT cerevisiae as a gene encoding an NAD kinase.";
RL FEMS Microbiol. Lett. 200:181-184(2001).
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE.
RX PubMed=2158927; DOI=10.1016/0378-1119(90)90297-5;
RA Melnick L., Sherman F.;
RT "Nucleotide sequence of the COR region: a cluster of six genes in the yeast
RT Saccharomyces cerevisiae.";
RL Gene 87:157-166(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7975898; DOI=10.1002/yea.320100611;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Revised nucleotide sequence of the COR region of yeast Saccharomyces
RT cerevisiae chromosome X.";
RL Yeast 10:811-818(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
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 [6]
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 [7]
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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Specifically phosphorylates NAD in the presence of ATP, dATP,
CC or CTP as phosphoryl donors. {ECO:0000269|PubMed:11425472}.
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:0000269|PubMed:11425472};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18630;
CC Evidence={ECO:0000269|PubMed:11425472};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.50 mM for NAD {ECO:0000269|PubMed:11425472};
CC KM=0.60 mM for ATP {ECO:0000269|PubMed:11425472};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:11425472};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:11425472}.
CC -!- INTERACTION:
CC P21373; P32622: YEF1; NbExp=4; IntAct=EBI-20174, EBI-22350;
CC -!- MISCELLANEOUS: Present with 5040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
CC -!- CAUTION: Was briefly thought to be FRE2. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB044344; BAB83863.1; -; Genomic_DNA.
DR EMBL; L26347; AAA62857.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88752.1; -; Genomic_DNA.
DR EMBL; M37696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z49549; CAA89577.1; -; Genomic_DNA.
DR EMBL; AY692899; AAT92918.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08836.1; -; Genomic_DNA.
DR PIR; S46589; S46589.
DR RefSeq; NP_012583.1; NM_001181707.1.
DR AlphaFoldDB; P21373; -.
DR SMR; P21373; -.
DR BioGRID; 33802; 96.
DR DIP; DIP-4479N; -.
DR IntAct; P21373; 5.
DR MINT; P21373; -.
DR STRING; 4932.YJR049C; -.
DR iPTMnet; P21373; -.
DR MaxQB; P21373; -.
DR PaxDb; 4932-YJR049C; -.
DR PeptideAtlas; P21373; -.
DR EnsemblFungi; YJR049C_mRNA; YJR049C; YJR049C.
DR GeneID; 853508; -.
DR KEGG; sce:YJR049C; -.
DR AGR; SGD:S000003810; -.
DR SGD; S000003810; UTR1.
DR VEuPathDB; FungiDB:YJR049C; -.
DR eggNOG; KOG2178; Eukaryota.
DR GeneTree; ENSGT00940000169386; -.
DR HOGENOM; CLU_008831_1_5_1; -.
DR InParanoid; P21373; -.
DR OMA; MRMRLCC; -.
DR OrthoDB; 455155at2759; -.
DR BioCyc; MetaCyc:G3O-31684-MONOMER; -.
DR BioCyc; YEAST:G3O-31684-MONOMER; -.
DR BRENDA; 2.7.1.23; 984.
DR BRENDA; 2.7.1.86; 984.
DR Reactome; R-SCE-196807; Nicotinate metabolism.
DR BioGRID-ORCS; 853508; 2 hits in 10 CRISPR screens.
DR PRO; PR:P21373; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P21373; Protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IDA:SGD.
DR GO; GO:0042736; F:NADH kinase activity; IDA:SGD.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 PANTHER; PTHR20275; NAD KINASE; 1.
DR PANTHER; PTHR20275:SF0; NAD KINASE; 1.
DR Pfam; PF01513; NAD_kinase; 1.
DR Pfam; PF20143; NAD_kinase_C; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; NAD; NADP; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..530
FT /note="NAD(+) kinase"
FT /id="PRO_0000120716"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 337
FT /note="A -> V (in Ref. 6; AAT92918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 59469 MW; 1BF4F01D7213B94B CRC64;
MKENDMNNGV DKWVNEEDGR NDHHNNNNNL MKKAMMNNEQ IDRTQDIDNA KEMLRKISSE
SSSRRSSLLN KDSSLVNGNA NSGGGTSING TRGSSKSSNT HFQYASTAYG VRMLSKDISN
TKVELDVENL MIVTKLNDVS LYFLTRELVE WVLVHFPRVT VYVDSELKNS KKFAAGELCE
DSKCRESRIK YWTKDFIREH DVFFDLVVTL GGDGTVLFVS SIFQRHVPPV MSFSLGSLGF
LTNFKFEHFR EDLPRIMNHK IKTNLRLRLE CTIYRRHRPE VDPNTGKKIC VVEKLSTHHI
LNEVTIDRGP SPFLSMLELY GDGSLMTVAQ ADGLIAATPT GSTAYSLSAG GSLVCPTVNA
IALTPICPHA LSFRPIILPE SINLKVKVSM KSRAPAWAAF DGKDRIELQK GDFITICASP
YAFPTVEASP DEFINSISRQ LNWNVREQQK SFTHILSQKN QEKYAHEANK VRNQAEPLEV
IRDKYSLEAD ATKENNNGSD DESDDESVNC EACKLKPSSV PKPSQARFSV
//
