ID A0AA35RAB0_9METZ Unreviewed; 214 AA. AC A0AA35RAB0; DT 24-JAN-2024, integrated into UniProtKB/TrEMBL. DT 24-JAN-2024, sequence version 1. DT 27-MAR-2024, entry version 2. 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 ORFNames=GBAR_LOCUS5362 {ECO:0000313|EMBL:CAI8007760.1}; OS Geodia barretti. OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha; OC Tetractinellida; Astrophorina; Geodiidae; Geodia. OX NCBI_TaxID=519541 {ECO:0000313|EMBL:CAI8007760.1, ECO:0000313|Proteomes:UP001174909}; RN [1] {ECO:0000313|EMBL:CAI8007760.1} RP NUCLEOTIDE SEQUENCE. RA Steffen K., Cardenas P.; RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases. 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}. 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:CAI8007760.1}. 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; CASHTH010000799; CAI8007760.1; -; Genomic_DNA. DR Proteomes; UP001174909; Unassembled WGS sequence. 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|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}; 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..26 FT /note="Lumenal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT TRANSMEM 27..49 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 51..62 FT /note="Lumenal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT TRANSMEM 70..92 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 104..123 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 130..153 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 133..175 FT /note="Lumenal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT TRANSMEM 165..194 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 197..214 FT /note="Cytoplasmic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT BINDING 116..118 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" FT BINDING 198..199 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216" SQ SEQUENCE 214 AA; 23535 MW; 290ADE69296398AB CRC64; MDGGPQDNTR VRRLEEMASA LELLNELASP SVLLACPLVM LNPLIWNLIV RHEYNTRSVS RLCGGPRAGV VLVACIVMVN NSIRTSFFHY IVGKNSKLQF LEDNVGATIA GYVIIGVGVL LVLSSTWRLG FFCTFLGDYF GILLDARVTG FPFNILNHPM FWGSFLIYVG DSVLCASAVA FLLSLFIGLS YVLAAAFEVP FTAKIYAQKE TKKI //