PLMT_YEAST
ID PLMT_YEAST Reviewed; 206 AA.
AC P05375; D6VWP3;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Phosphatidyl-N-methylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000305};
DE EC=2.1.1.17 {ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666};
DE EC=2.1.1.71 {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666};
DE AltName: Full=Overproducer of inositol protein 3 {ECO:0000305|PubMed:7047296};
DE AltName: Full=Phospholipid methyltransferase {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000303|PubMed:2445736, ECO:0000303|PubMed:2670666};
DE Short=PLMT {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000303|PubMed:1954254, ECO:0000303|PubMed:2670666};
GN Name=OPI3 {ECO:0000303|PubMed:7047296};
GN Synonyms=PEM2 {ECO:0000303|PubMed:2445736};
GN OrderedLocusNames=YJR073C {ECO:0000312|SGD:S000003834}; ORFNames=J1824;
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, AND CATALYTIC ACTIVITY.
RX PubMed=2445736; DOI=10.1016/s0021-9258(18)47744-7;
RA Kodaki T., Yamashita S.;
RT "Yeast phosphatidylethanolamine methylation pathway. Cloning and
RT characterization of two distinct methyltransferase genes.";
RL J. Biol. Chem. 262:15428-15435(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=6759124; DOI=10.1111/j.1432-1033.1982.tb07005.x;
RA Yamashita S., Oshima A., Nikawa J., Hosaka K.;
RT "Regulation of the phosphatidylethanolamine methylation pathway in
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 128:589-595(1982).
RN [7]
RP FUNCTION.
RX PubMed=7047296; DOI=10.1093/genetics/100.1.19;
RA Greenberg M.L., Reiner B., Henry S.A.;
RT "Regulatory mutations of inositol biosynthesis in yeast: isolation of
RT inositol-excreting mutants.";
RL Genetics 100:19-33(1982).
RN [8]
RP FUNCTION, AND PATHWAY.
RX PubMed=6337128; DOI=10.1128/jb.153.2.791-799.1983;
RA Greenberg M.L., Klig L.S., Letts V.A., Loewy B.S., Henry S.A.;
RT "Yeast mutant defective in phosphatidylcholine synthesis.";
RL J. Bacteriol. 153:791-799(1983).
RN [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=2684666; DOI=10.1111/j.1432-1033.1989.tb15109.x;
RA Kodaki T., Yamashita S.;
RT "Characterization of the methyltransferases in the yeast
RT phosphatidylethanolamine methylation pathway by selective gene
RT disruption.";
RL Eur. J. Biochem. 185:243-251(1989).
RN [10]
RP FUNCTION.
RX PubMed=2670666; DOI=10.1093/genetics/122.2.317;
RA McGraw P., Henry S.A.;
RT "Mutations in the Saccharomyces cerevisiae opi3 gene: effects on
RT phospholipid methylation, growth and cross-pathway regulation of inositol
RT synthesis.";
RL Genetics 122:317-330(1989).
RN [11]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=2198947; DOI=10.1016/0005-2760(90)90145-n;
RA Gaynor P.M., Carman G.M.;
RT "Phosphatidylethanolamine methyltransferase and phospholipid
RT methyltransferase activities from Saccharomyces cerevisiae. Enzymological
RT and kinetic properties.";
RL Biochim. Biophys. Acta 1045:156-163(1990).
RN [12]
RP INDUCTION.
RX PubMed=1954254; DOI=10.1016/0167-4781(91)90197-t;
RA Gaynor P.M., Gill T., Toutenhoofd S., Summers E.F., McGraw P., Homann M.J.,
RA Henry S.A., Carman G.M.;
RT "Regulation of phosphatidylethanolamine methyltransferase and phospholipid
RT methyltransferase by phospholipid precursors in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1090:326-332(1991).
RN [13]
RP INDUCTION.
RX PubMed=1650774;
RA Kodaki T., Hosaka K., Nikawa J., Yamashita S.;
RT "Identification of the upstream activation sequences responsible for the
RT expression and regulation of the PEM1 and PEM2 genes encoding the enzymes
RT of the phosphatidylethanolamine methylation pathway in Saccharomyces
RT cerevisiae.";
RL J. Biochem. 109:276-287(1991).
RN [14]
RP INDUCTION.
RX PubMed=8614637; DOI=10.1093/nar/24.7.1322;
RA Jackson J.C., Lopes J.M.;
RT "The yeast UME6 gene is required for both negative and positive
RT transcriptional regulation of phospholipid biosynthetic gene expression.";
RL Nucleic Acids Res. 24:1322-1329(1996).
RN [15]
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 [16]
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 [17]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [18]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22001639; DOI=10.1016/j.bbalip.2011.09.018;
RA Bilgin M., Markgraf D.F., Duchoslav E., Knudsen J., Jensen O.N.,
RA de Kroon A.I., Ejsing C.S.;
RT "Quantitative profiling of PE, MMPE, DMPE, and PC lipid species by multiple
RT precursor ion scanning: a tool for monitoring PE metabolism.";
RL Biochim. Biophys. Acta 1811:1081-1089(2011).
CC -!- FUNCTION: Catalyzes the second two steps of the methylation pathway of
CC phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC phosphatidylmonomethylethanolamine (PMME) to
CC phosphatidyldimethylethanolamine (PDME) and of PDME to
CC phosphatidylcholine (PC). Can also catalyze the first methylation
CC reaction of PE to PMME in the absence of PE methyltransferase CHO2.
CC {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:2198947,
CC ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736,
CC ECO:0000269|PubMed:2670666, ECO:0000269|PubMed:2684666,
CC ECO:0000269|PubMed:6337128, ECO:0000269|PubMed:6759124,
CC ECO:0000269|PubMed:7047296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
CC Evidence={ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736,
CC ECO:0000269|PubMed:2684666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-
CC adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03216,
CC ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639,
CC ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-
CC adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32739,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572; EC=2.1.1.71;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03216,
CC ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639,
CC ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for S-adenosyl-L-methionine (in presence of
CC phosphatidylethanolamine (PE) as substrate)
CC {ECO:0000269|PubMed:2684666};
CC KM=190 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-
CC methylethanolamine (PMME) as substrate) {ECO:0000269|PubMed:2684666};
CC KM=240 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-
CC dimethylethanolamine (PDME) as substrate)
CC {ECO:0000269|PubMed:2684666};
CC KM=270 uM for phosphatidyl-N-methylethanolamine (PMME)
CC {ECO:0000269|PubMed:2684666};
CC KM=110 uM for phosphatidyl-N-dimethylethanolamine (PDME)
CC {ECO:0000269|PubMed:2684666};
CC KM=54 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-
CC methylethanolamine (PMME) as substrate) {ECO:0000269|PubMed:2198947};
CC KM=59 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-
CC dimethylethanolamine (PDME) as substrate)
CC {ECO:0000269|PubMed:2198947};
CC KM=380 uM for phosphatidyl-N-methylethanolamine (PMME)
CC {ECO:0000269|PubMed:2198947};
CC KM=180 uM for phosphatidyl-N-dimethylethanolamine (PDME)
CC {ECO:0000269|PubMed:2198947};
CC pH dependence:
CC Optimum pH is 8.1. {ECO:0000269|PubMed:2684666};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000305|PubMed:6337128}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:14562095}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion
CC membrane {ECO:0000255|HAMAP-Rule:MF_03216,
CC ECO:0000269|PubMed:14576278}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03216}.
CC -!- INDUCTION: Expression is repressed by inositol and choline. The 5'
CC flanking region contains two copies of the CATRTGAA motif and a 5'-
CC AAACCCACACATG-3' GRFI site, which are involved in the regulation of
CC expression. OPI1 and SIN3 play the role of repressors for OPI3
CC expression whereas UME6 is an activator of OPI3 expression.
CC {ECO:0000269|PubMed:1650774, ECO:0000269|PubMed:1954254,
CC ECO:0000269|PubMed:6759124, ECO:0000269|PubMed:8614637}.
CC -!- MISCELLANEOUS: Present with 5890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. PEMT/PEM2 methyltransferase family. {ECO:0000255|HAMAP-
CC Rule:MF_03216}.
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DR EMBL; M16988; AAA34851.1; -; Genomic_DNA.
DR EMBL; Z49573; CAA89601.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39298.1; -; Genomic_DNA.
DR EMBL; AY557899; AAS56225.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08859.1; -; Genomic_DNA.
DR PIR; B28443; B28443.
DR RefSeq; NP_012607.1; NM_001181731.1.
DR AlphaFoldDB; P05375; -.
DR BioGRID; 33829; 615.
DR DIP; DIP-2888N; -.
DR IntAct; P05375; 3.
DR MINT; P05375; -.
DR STRING; 4932.YJR073C; -.
DR SwissLipids; SLP:000000084; -.
DR PaxDb; P05375; -.
DR PRIDE; P05375; -.
DR DNASU; 853536; -.
DR EnsemblFungi; YJR073C_mRNA; YJR073C; YJR073C.
DR GeneID; 853536; -.
DR KEGG; sce:YJR073C; -.
DR SGD; S000003834; OPI3.
DR VEuPathDB; FungiDB:YJR073C; -.
DR eggNOG; KOG4142; Eukaryota.
DR GeneTree; ENSGT00390000007041; -.
DR HOGENOM; CLU_086119_0_0_1; -.
DR InParanoid; P05375; -.
DR OMA; VITSTWA; -.
DR BioCyc; MetaCyc:YJR073C-MON; -.
DR BioCyc; YEAST:YJR073C-MON; -.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR UniPathway; UPA00753; -.
DR PRO; PR:P05375; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P05375; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity; IDA:SGD.
DR GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IDA:SGD.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD.
DR HAMAP; MF_03216; PLMT; 1.
DR InterPro; IPR024960; PEMT/MFAP.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR PANTHER; PTHR15458; PTHR15458; 1.
DR Pfam; PF04191; PEMT; 1.
DR PIRSF; PIRSF005444; PEMT; 1.
DR PROSITE; PS51599; SAM_PEMT_PEM2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Methyltransferase; Mitochondrion; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..206
FT /note="Phosphatidyl-N-methylethanolamine N-
FT methyltransferase"
FT /id="PRO_0000193924"
FT TOPO_DOM 1..20
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT INTRAMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 42..53
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 75..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 123..165
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 187..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 106..108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 188..189
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
SQ SEQUENCE 206 AA; 23150 MW; BC0CDCC1C7B2AD36 CRC64;
MKESVQEIIQ QLIHSVDLQS SKFQLAIVCT MFNPIFWNIV ARMEYHKHSL TKMCGGARKG
CYMLAATIFS LGIVRDMVYE SALREQPTCS LITGENWTKL GVALFGLGQV LVLSSMYKLG
ITGTYLGDYF GILMDERVTG FPFNVSNNPM YQGSTLSFLG IALYKGKPAG LVVSAVVYFM
YKIALRWEEP FTAMIYANRD KAKKNM
