CHO2_YEAS8
ID CHO2_YEAS8 Reviewed; 869 AA.
AC C8Z951;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PE methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217};
GN Name=CHO2; ORFNames=EC1118_1G1_4786g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC -!- FUNCTION: Catalyzes the first step of the methylation pathway of
CC phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine
CC (PMME). {ECO:0000255|HAMAP-Rule:MF_03217}.
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:0000255|HAMAP-Rule:MF_03217};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03217}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. CHO2 family. {ECO:0000255|HAMAP-Rule:MF_03217}.
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DR EMBL; FN393070; CAY79917.1; -; Genomic_DNA.
DR AlphaFoldDB; C8Z951; -.
DR EnsemblFungi; CAY79917; CAY79917; EC1118_1G1_4786g.
DR HOGENOM; CLU_005987_0_1_1; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000000286; Chromosome VII, Scaffold EC1118_1G1.
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:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03217; PEMT; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR Pfam; PF04191; PEMT; 2.
DR PIRSF; PIRSF000383; PEAMT; 1.
DR PROSITE; PS51598; SAM_CHO2; 1.
PE 3: Inferred from homology;
KW Acetylation; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Methyltransferase; Phospholipid biosynthesis;
KW Phospholipid metabolism; S-adenosyl-L-methionine; Transferase;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P05374"
FT CHAIN 2..869
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405914"
FT TOPO_DOM 2..55
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 77..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 108..187
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 209..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 234..258
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 280..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 292..310
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 311..362
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 384..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 412..439
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 461..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 485..534
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 556..869
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P05374"
SQ SEQUENCE 869 AA; 101192 MW; 8128D4BC1B46CF9F CRC64;
MSSCKTTLSE MVGSVTKDRG TINVKARTRS SNVTFKPPVT HDMVRSLFDP TLKKSLLEKC
IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN LGIGLVLHYQ SHYETLTNCA
KTHAIFSKIP HNKDANSNFS TNSNSFSEKF WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN
VWLIFRQFVD LILMQDFVTY IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV
VKDYAWYWGD FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH
YSQFLFLKYV ENPHIERTYG DGIDSDSQMN SRIDDLISKE NCDYSRPLIN MGLSFNNFNK
LRFTDYFTIG TVAALMLGTI MNARFINLNH LFITVFVTKL VSWLFISTIL YKQSQSKWFT
RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT LMIIYTGLQI WSNFSNINNS QLIFGLILVA
LQTWCDKETR LAISDFGWFY GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL
MTNFAVTNII LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI
VNRIENIIIK SLIDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR LSPYCELKIE
NEQIETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR ADREKTRVGS GGHWSATSKD
SYMNHGLRHK ESVTEIKATE KYVQGKVTFD TSLLYFENGI YEFRYHSGNS HKVLLISTPF
EISLPVLNTT TPELFEKDLT EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS
SEYMRRVNGD AHVISHRAWD IKQTLDSLA
