ID A0A7J8BJT1_MOLMO Unreviewed; 182 AA.
AC A0A7J8BJT1;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03216};
DE Short=PEAMT {ECO:0000256|HAMAP-Rule:MF_03216};
DE Short=PEMT {ECO:0000256|HAMAP-Rule:MF_03216};
DE EC=2.1.1.17 {ECO:0000256|HAMAP-Rule:MF_03216};
DE EC=2.1.1.71 {ECO:0000256|HAMAP-Rule:MF_03216};
DE AltName: Full=Phospholipid methyltransferase {ECO:0000256|HAMAP-Rule:MF_03216};
DE Short=PLMT {ECO:0000256|HAMAP-Rule:MF_03216};
GN Name=PEMT {ECO:0000256|HAMAP-Rule:MF_03216};
GN ORFNames=HJG59_014055 {ECO:0000313|EMBL:KAF6398731.1};
OS Molossus molossus (Pallas' mastiff bat) (Vespertilio molossus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Molossidae;
OC Molossus.
OX NCBI_TaxID=27622 {ECO:0000313|EMBL:KAF6398731.1, ECO:0000313|Proteomes:UP000550707};
RN [1] {ECO:0000313|EMBL:KAF6398731.1, ECO:0000313|Proteomes:UP000550707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMolMol1 {ECO:0000313|EMBL:KAF6398731.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6398731.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- FUNCTION: Catalyzes the three sequential steps of the methylation
CC pathway for the biosynthesis of phosphatidylcholine, a critical and
CC essential component for membrane structure. Uses S-adenosylmethionine
CC (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for
CC the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-
CC phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2-
CC diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to
CC phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2-
CC diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L-
CC homocysteine in each step. {ECO:0000256|HAMAP-Rule:MF_03216}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phosphocholine + S-adenosyl-L-
CC homocysteine + H(+); Xref=Rhea:RHEA:70759, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:86161,
CC ChEBI:CHEBI:189860; Evidence={ECO:0000256|ARBA:ARBA00051210};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70760;
CC Evidence={ECO:0000256|ARBA:ARBA00051210};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-
CC adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:70755,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:189859, ChEBI:CHEBI:189860;
CC Evidence={ECO:0000256|ARBA:ARBA00051880};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70756;
CC Evidence={ECO:0000256|ARBA:ARBA00051880};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-
CC adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:70751,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:189858, ChEBI:CHEBI:189859;
CC Evidence={ECO:0000256|ARBA:ARBA00052126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70752;
CC Evidence={ECO:0000256|ARBA:ARBA00052126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine + S-adenosyl-L-
CC homocysteine + H(+); Xref=Rhea:RHEA:70747, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:42027, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:189849; Evidence={ECO:0000256|ARBA:ARBA00051451};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70748;
CC Evidence={ECO:0000256|ARBA:ARBA00051451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-
CC adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:70743,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:189848, ChEBI:CHEBI:189849;
CC Evidence={ECO:0000256|ARBA:ARBA00050814};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70744;
CC Evidence={ECO:0000256|ARBA:ARBA00050814};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-
CC adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:70739,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:172403, ChEBI:CHEBI:189848;
CC Evidence={ECO:0000256|ARBA:ARBA00050788};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70740;
CC Evidence={ECO:0000256|ARBA:ARBA00050788};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine
CC + H(+); Xref=Rhea:RHEA:70623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74669, ChEBI:CHEBI:85680;
CC Evidence={ECO:0000256|ARBA:ARBA00052148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70624;
CC Evidence={ECO:0000256|ARBA:ARBA00052148};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-
CC adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:46112,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85679, ChEBI:CHEBI:85680;
CC Evidence={ECO:0000256|ARBA:ARBA00051455};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46113;
CC Evidence={ECO:0000256|ARBA:ARBA00051455};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + S-
CC adenosyl-L-methionine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+);
CC Xref=Rhea:RHEA:70619, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74986, ChEBI:CHEBI:85679;
CC Evidence={ECO:0000256|ARBA:ARBA00051941};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70620;
CC Evidence={ECO:0000256|ARBA:ARBA00051941};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine
CC = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+);
CC Xref=Rhea:RHEA:70771, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74963, ChEBI:CHEBI:189862;
CC Evidence={ECO:0000256|ARBA:ARBA00050433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70772;
CC Evidence={ECO:0000256|ARBA:ARBA00050433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1-
CC hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+);
CC Xref=Rhea:RHEA:70767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:189861, ChEBI:CHEBI:189862;
CC Evidence={ECO:0000256|ARBA:ARBA00050899};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70768;
CC Evidence={ECO:0000256|ARBA:ARBA00050899};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1-
CC hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+);
CC Xref=Rhea:RHEA:70763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:78261, ChEBI:CHEBI:189861;
CC Evidence={ECO:0000256|ARBA:ARBA00050744};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70764;
CC Evidence={ECO:0000256|ARBA:ARBA00050744};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine +
CC S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine +
CC S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:32739,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03216};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-
CC adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-homocysteine + H(+);
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:0000256|HAMAP-Rule:MF_03216};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC methionine = a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC S-adenosyl-L-homocysteine + H(+); 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:0000256|HAMAP-Rule:MF_03216};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004969, ECO:0000256|HAMAP-Rule:MF_03216}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03216}. Mitochondrion membrane
CC {ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03216}. Note=Found in endoplasmic reticulum
CC where most PEMT activity is generated and in mitochondria.
CC {ECO:0000256|HAMAP-Rule:MF_03216}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. PEMT/PEM2 methyltransferase family. {ECO:0000256|HAMAP-
CC Rule:MF_03216}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03216}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6398731.1}.
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; JACASF010000028; KAF6398731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8BJT1; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000550707; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
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 FunFam; 1.20.120.1630:FF:000005; Phosphatidylethanolamine N-methyltransferase; 1.
DR Gene3D; 1.20.120.1630; -; 1.
DR HAMAP; MF_03216; PLMT; 1.
DR InterPro; IPR024960; PEMT/MFAP.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR PANTHER; PTHR15458; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR15458:SF5; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR Pfam; PF04191; PEMT; 1.
DR PROSITE; PS51599; SAM_PEMT_PEM2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03216};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_03216};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_03216};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03216};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03216};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03216};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_03216};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_03216}; Reference proteome {ECO:0000313|Proteomes:UP000550707};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03216};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03216};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03216};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03216}.
FT TOPO_DOM 1..38
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT INTRAMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 41..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 60..71
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 71..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 93..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 117..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 124..126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
SQ SEQUENCE 182 AA; 19827 MW; 4499C05D865BA337 CRC64;
MSSAAAGPDC CGGLGSIDWR QADFCIMTRL LGSVDPAEPC FVAAVLTIIF NPLFWNVVAR
WEHKTRKLSR ALGSPYLGCY ALGGVILLLN VLRSHCFTQA MLNQPTTDSL QDPSARWLGL
ALLGVGCLLV LSSFFALGFT GTFLGDYFGI LKEARVTSFP FNILDNPMYW GSTANYLGWA
IM
//
