ID A0A8H3G5R4_9LECA Unreviewed; 201 AA. AC A0A8H3G5R4; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 13-SEP-2023, entry version 7. DE RecName: Full=Phosphatidyl-N-methylethanolamine N-methyltransferase {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=OPI3 {ECO:0000313|EMBL:CAF9937054.1}; GN ORFNames=ALECFALPRED_007087 {ECO:0000313|EMBL:CAF9937054.1}; OS Alectoria fallacina. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes; OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Parmeliaceae; OC Alectoria. OX NCBI_TaxID=1903189 {ECO:0000313|EMBL:CAF9937054.1, ECO:0000313|Proteomes:UP000664203}; RN [1] {ECO:0000313|EMBL:CAF9937054.1} RP NUCLEOTIDE SEQUENCE. RA Tagirdzhanova G.; RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases. 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). {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 -!- 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}. 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:CAF9937054.1}. 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; CAJPDR010000460; CAF9937054.1; -; Genomic_DNA. DR UniPathway; UPA00753; -. DR Proteomes; UP000664203; 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: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:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule. 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 ECO:0000313|EMBL:CAF9937054.1}; 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:UP000664203}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03216}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03216, KW ECO:0000313|EMBL:CAF9937054.1}; 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..13 FT /note="Lumenal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT INTRAMEM 14..34 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT TOPO_DOM 35..46 FT /note="Lumenal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT TRANSMEM 51..69 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 90..110 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 114..156 FT /note="Lumenal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT TRANSMEM 155..175 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 178..201 FT /note="Cytoplasmic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT BINDING 97..99 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT BINDING 179..180 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" SQ SEQUENCE 201 AA; 22575 MW; FECC4191D23E6B26 CRC64; MSQLNGGLVD FSQSSLYFSA LAIAFNPTFW NIIARQEYHN KTLTRLFNGN SLRACYALAL TIFGLGLFRD ALYERALRHQ PFIPAFHHPY IAYVLLTIGN TLVLTSYYAL GLTGTFLGDY FGILMDEPVT GFPFNVTSAP MYWGSTTSFL GTSLLYGRPA GALLTIQVFV VYLAALQFED PFTSKIYAKR DKEEKEEKKA K //