ID W5M182_LEPOC Unreviewed; 237 AA.
AC W5M182;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ECO:0000313|Ensembl:ENSLOCP00000002139.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002139.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002139.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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-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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03216};
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:0000256|HAMAP-Rule:MF_03216};
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: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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. 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}.
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DR EMBL; AHAT01031987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01031988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M182; -.
DR STRING; 7918.ENSLOCP00000002139; -.
DR Ensembl; ENSLOCT00000002144.1; ENSLOCP00000002139.1; ENSLOCG00000001840.1.
DR eggNOG; KOG4142; Eukaryota.
DR GeneTree; ENSGT00390000007041; -.
DR HOGENOM; CLU_086119_1_0_1; -.
DR InParanoid; W5M182; -.
DR OMA; PTFWNIA; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000018468; Linkage group LG13.
DR Bgee; ENSLOCG00000001840; Expressed in intestine and 10 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
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 PIRSF; PIRSF005444; PEMT; 1.
DR PROSITE; PS51599; SAM_PEMT_PEM2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_03216};
KW Mitochondrion {ECO:0000256|HAMAP-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:UP000018468};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03216};
KW Transferase {ECO:0000256|HAMAP-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..51
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 43..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT INTRAMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TOPO_DOM 73..84
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 88..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 106..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 154..196
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 187..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 218..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT BINDING 137..139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT BINDING 219..220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
SQ SEQUENCE 237 AA; 26465 MW; 10AD0986999F37E0 CRC64;
LSGGDSPIYL EQNKKKKTSL LDCCGGLNNL DYNKIDMSVM AEVLHYVDVT DAQFSVAVLA
IIFNPFFWNV VARWEHRTKG LTRVFGCPYA ACYCLALLII LLNVYRSHSF TMAMNSQPKA
ELMERSEMFY AGAILVFIGS VFVLSSFYAL GFTGTFLGDY FGILQEEKVN GFPFNVMENP
MYWGSTAIYL GLALMNASPA GVVLTSVVAA AYKIAIMFEG PFTEEIYRQR ISSEKNK
//
