EKI1_YEAST
ID EKI1_YEAST Reviewed; 534 AA.
AC Q03764; D6VSD0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ethanolamine kinase {ECO:0000305};
DE Short=EK;
DE EC=2.7.1.82 {ECO:0000269|PubMed:10329685};
GN Name=EKI1; OrderedLocusNames=YDR147W; ORFNames=YD8358.04;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10329685; DOI=10.1074/jbc.274.21.14857;
RA Kim K., Kim K.-H., Storey M.K., Voelker D.R., Carman G.M.;
RT "Isolation and characterization of the Saccharomyces cerevisiae EKI1 gene
RT encoding ethanolamine kinase.";
RL J. Biol. Chem. 274:14857-14866(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP INDUCTION.
RX PubMed=15201274; DOI=10.1074/jbc.m405704200;
RA Kersting M.C., Choi H.S., Carman G.M.;
RT "Regulation of the yeast EKI1-encoded ethanolamine kinase by inositol and
RT choline.";
RL J. Biol. Chem. 279:35353-35359(2004).
RN [7]
RP INDUCTION.
RX PubMed=16551612; DOI=10.1074/jbc.m601612200;
RA Kersting M.C., Carman G.M.;
RT "Regulation of the Saccharomyces cerevisiae EKI1-encoded ethanolamine
RT kinase by zinc depletion.";
RL J. Biol. Chem. 281:13110-13116(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Catalyzes the committed step of phosphatidylethanolamine
CC synthesis via the CDP-ethanolamine branch of the Kennedy pathway. Also
CC exhibits choline kinase activity, thus contributing to
CC phosphatidylcholine synthesis via the CDP-choline pathway, but its
CC preferred substrate is ethanolamine. {ECO:0000269|PubMed:10329685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine;
CC Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216;
CC EC=2.7.1.82; Evidence={ECO:0000269|PubMed:10329685};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC Evidence={ECO:0000305|PubMed:10329685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + choline = ADP + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:12837, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:295975, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10329685};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838;
CC Evidence={ECO:0000305|PubMed:10329685};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.171 mM for ethanolamine {ECO:0000269|PubMed:10329685};
CC KM=0.275 mM for choline {ECO:0000269|PubMed:10329685};
CC Vmax=346 nmol/min/mg enzyme for ethanolamine
CC {ECO:0000269|PubMed:10329685};
CC Vmax=249 nmol/min/mg enzyme for choline
CC {ECO:0000269|PubMed:10329685};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Induced by zinc-depletion via the transcription factor ZAP1.
CC Expression is sensitive to intracellular zinc levels (PubMed:16551612).
CC Repressed by inositol (PubMed:15201274). {ECO:0000269|PubMed:15201274,
CC ECO:0000269|PubMed:16551612}.
CC -!- MISCELLANEOUS: Present with 3420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
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DR EMBL; Z50046; CAA90370.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11990.1; -; Genomic_DNA.
DR PIR; S57974; S57974.
DR RefSeq; NP_010431.3; NM_001180454.3.
DR AlphaFoldDB; Q03764; -.
DR SMR; Q03764; -.
DR BioGRID; 32201; 108.
DR MINT; Q03764; -.
DR STRING; 4932.YDR147W; -.
DR SwissLipids; SLP:000000065; -.
DR iPTMnet; Q03764; -.
DR MaxQB; Q03764; -.
DR PaxDb; Q03764; -.
DR PRIDE; Q03764; -.
DR EnsemblFungi; YDR147W_mRNA; YDR147W; YDR147W.
DR GeneID; 851725; -.
DR KEGG; sce:YDR147W; -.
DR SGD; S000002554; EKI1.
DR VEuPathDB; FungiDB:YDR147W; -.
DR eggNOG; KOG2686; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_4_2_1; -.
DR InParanoid; Q03764; -.
DR BioCyc; YEAST:YDR147W-MON; -.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR Reactome; R-SCE-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00741.
DR PRO; PR:Q03764; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03764; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004103; F:choline kinase activity; IDA:SGD.
DR GO; GO:0004305; F:ethanolamine kinase activity; IDA:SGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:SGD.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR007521; Choline_kin_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF04428; Choline_kin_N; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..534
FT /note="Ethanolamine kinase"
FT /id="PRO_0000206230"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 534 AA; 61657 MW; 47B417841D5005A8 CRC64;
MYTNYSLTSS DAMPRTYLVG TASPEMSKKK RQSANCDKPT RRVIHIIDTN EHSEVDLKNE
LPITCTNEDG EMTSSSWTSQ TANDFLKLAY VNAKLDPSLP SQYFKQDIIN VLQSLEIPGW
SVPGSKESSL NKNLLTLTQI KGALTNVIYK IHYPNLPPLL MRIFGDSIDS VIDREYELKV
IARLSFYDLG PKLEGFFENG RFEKYIEGSR TSTQADFIDR DTSIKIAKKL KELHCTVPLT
HKEITDQPSC WTTFDQWIKL IDSHKEWVSN NVNISENLRC SSWNFFLKSF KNYKRWLYND
SAFTSKLLRE DDKDSMINSG LKMVFCHNDL QHGNLLFKSK GKDDISVGDL TIIDFEYAGP
NPVVFDLSNH LNEWMQDYND VQSFKSHIDK YPKEEDILVF AQSYINHMNE NHVKIASQEV
RILYNLIIEW RPCTQLFWCL WALLQSGRLP QRPLIEGEKL MSEKAGLGDE THLMEHKNKE
NGKYDCSEDD SFNYLGFCKE KMSVFWGDLI TLGVIDKDCP DIGKTDYLDT KLIF
