YEF1_YEAST
ID YEF1_YEAST Reviewed; 495 AA.
AC P32622; D3DLK8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=ATP-NADH kinase YEF1;
DE EC=2.7.1.86;
GN Name=YEF1; OrderedLocusNames=YEL041W; ORFNames=SYGP-ORF17;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15978040; DOI=10.1111/j.1742-4658.2005.04749.x;
RA Shi F., Kawai S., Mori S., Kono E., Murata K.;
RT "Identification of ATP-NADH kinase isozymes and their contribution to
RT supply of NADP(H) in Saccharomyces cerevisiae.";
RL FEBS J. 272:3337-3349(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16760478; DOI=10.1074/jbc.m513919200;
RA Bieganowski P., Seidle H.F., Wojcik M., Brenner C.;
RT "Synthetic lethal and biochemical analyses of NAD and NADH kinases in
RT Saccharomyces cerevisiae establish separation of cellular functions.";
RL J. Biol. Chem. 281:22439-22445(2006).
RN [6]
RP FUNCTION.
RX PubMed=19158096; DOI=10.1074/jbc.m804100200;
RA Miyagi H., Kawai S., Murata K.;
RT "Two sources of mitochondrial NADPH in the yeast Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 284:7553-7560(2009).
RN [7]
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).
CC -!- FUNCTION: ATP-NADH kinase with a low phosphorylation activity of both
CC NADH and NAD(+) to produce NADP and NADPH by using ATP. UTR1 is
CC responsible for essentially all of the NAD/NADH kinase activity
CC resident in the cytoplasm, whereas POS5 is responsible for all
CC mitochondrial NAD/NADH kinase activity and consequent mitochondrial
CC genome maintenance. YEF1 can substitute for UTR1 when overexpressed.
CC {ECO:0000269|PubMed:15978040, ECO:0000269|PubMed:16760478,
CC ECO:0000269|PubMed:19158096}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NADH = ADP + H(+) + NADPH; Xref=Rhea:RHEA:12260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:456216; EC=2.7.1.86;
CC Evidence={ECO:0000269|PubMed:15978040, ECO:0000269|PubMed:16760478};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15978040};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15978040};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:15978040};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15978040};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 mM for NAD {ECO:0000269|PubMed:15978040,
CC ECO:0000269|PubMed:16760478};
CC KM=2.0 mM for NADH {ECO:0000269|PubMed:15978040,
CC ECO:0000269|PubMed:16760478};
CC KM=0.17 mM for ATP {ECO:0000269|PubMed:15978040,
CC ECO:0000269|PubMed:16760478};
CC Vmax=3.3 umol/min/mg enzyme for NAD phosphorylation
CC {ECO:0000269|PubMed:15978040, ECO:0000269|PubMed:16760478};
CC Vmax=1.2 umol/min/mg enzyme for NADH phosphorylation
CC {ECO:0000269|PubMed:15978040, ECO:0000269|PubMed:16760478};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:15978040,
CC ECO:0000269|PubMed:16760478};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:15978040, ECO:0000269|PubMed:16760478};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:15978040}.
CC -!- INTERACTION:
CC P32622; P21373: UTR1; NbExp=4; IntAct=EBI-22350, EBI-20174;
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
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DR EMBL; U18779; AAB65001.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07612.1; -; Genomic_DNA.
DR PIR; S30838; S30838.
DR RefSeq; NP_010873.1; NM_001178856.1.
DR AlphaFoldDB; P32622; -.
DR SMR; P32622; -.
DR BioGRID; 36688; 87.
DR DIP; DIP-1885N; -.
DR IntAct; P32622; 7.
DR MINT; P32622; -.
DR STRING; 4932.YEL041W; -.
DR iPTMnet; P32622; -.
DR MaxQB; P32622; -.
DR PaxDb; P32622; -.
DR PRIDE; P32622; -.
DR EnsemblFungi; YEL041W_mRNA; YEL041W; YEL041W.
DR GeneID; 856670; -.
DR KEGG; sce:YEL041W; -.
DR SGD; S000000767; YEF1.
DR VEuPathDB; FungiDB:YEL041W; -.
DR eggNOG; KOG2178; Eukaryota.
DR GeneTree; ENSGT00940000169386; -.
DR HOGENOM; CLU_008831_1_2_1; -.
DR InParanoid; P32622; -.
DR OMA; QKAFKEW; -.
DR BioCyc; MetaCyc:G3O-30162-MON; -.
DR BioCyc; YEAST:G3O-30162-MON; -.
DR BRENDA; 2.7.1.23; 984.
DR BRENDA; 2.7.1.86; 984.
DR PRO; PR:P32622; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32622; protein.
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: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 Gene3D; 2.60.200.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
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 Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Cobalt; Kinase; Magnesium; Manganese; NAD; NADP;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..495
FT /note="ATP-NADH kinase YEF1"
FT /id="PRO_0000120717"
FT REGION 442..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 55874 MW; E8301D466249DA27 CRC64;
MKTDRLLINA SPETCTKGDA EMDTMDTIDR MTSVKVLAEG KVLSNFEEPG LMRCGYHDAK
NWVRRLSSET IVGEDTSNLY PFYVDTAYDV RRLRKDLINA KVDLQVENLI IICNINDIST
VFLMREVVEW ILRNFHSITV YVQDIFKKST QFAVGDLCKD SNCSKNRVKY WSKEFVKKHD
SFFDLMITLG GDGTVLFASS IFTKDVPPIV PFALGSLGFL TNFEFQNFKE TLKHILTDEV
RINLRMRLQC KLYRRNKPEI DAATGRKICY IDFISEHHVL NEVTIDRGPA PCLSLLELYG
NDSLMTKVQG DGLIVATPTG STAYSLSAGG SLISPSVNAI AVTPICPHTL SFRPIILPDS
MELKVRVDMN SRGTSWVNFD GKDRVELKQG DYVVITASPY SVPTIESSAS EFFESISKNL
NWNDREEQKP FAHILSPKNQ EKYRLDSSKN GNDTISNPLE SSCISSDAQD EERKSVTETE
TEIVVERTRQ AHFAI
