PLMT_NEUCR
ID PLMT_NEUCR Reviewed; 214 AA.
AC Q7S5W9;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Phosphatidyl-N-methylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03216};
DE EC=2.1.1.71 {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:6060457};
DE AltName: Full=Cholineless-2 {ECO:0000303|Ref.2};
DE AltName: Full=Phospholipid methyltransferase {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PLMT {ECO:0000255|HAMAP-Rule:MF_03216};
GN Name=chol-2 {ECO:0000303|Ref.2}; ORFNames=NCU04699;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP PATHWAY.
RA Horowitz N.H., Bonner D., Houlahan M.B.;
RT "The utilization of choline analogues by cholineless mutants of
RT Neurospora.";
RL J. Biol. Chem. 159:145-151(1945).
RN [3]
RP FUNCTION.
RX PubMed=21018749;
RA Horowitz N.H.;
RT "The isolation and identification of a natural precursor of choline.";
RL J. Biol. Chem. 162:413-419(1946).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6060457; DOI=10.1016/0005-2744(67)90077-0;
RA Scarborough G.A., Nyc J.F.;
RT "Properties of a phosphatidylmonomethylethanolamine N-methyl-transferase
RT from Neurospora crassa.";
RL Biochim. Biophys. Acta 146:111-119(1967).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=6016609; DOI=10.1016/s0021-9258(19)81455-2;
RA Scarborough G.A., Nyc J.F.;
RT "Methylation of ethanolamine phosphatides by microsomes from normal and
RT mutant strains of Neurospora crassa.";
RL J. Biol. Chem. 242:238-242(1967).
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:0000255|HAMAP-Rule:MF_03216,
CC ECO:0000269|PubMed:21018749, ECO:0000269|PubMed:6016609,
CC ECO:0000269|PubMed:6060457}.
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:0000255|HAMAP-Rule:MF_03216,
CC ECO:0000269|PubMed:6060457};
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; EC=2.1.1.71;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03216,
CC ECO:0000269|PubMed:6060457};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-
CC methylethanolamine (PMME) as substrate) {ECO:0000269|PubMed:6060457};
CC KM=18 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-
CC dimethylethanolamine (PDME) as substrate)
CC {ECO:0000269|PubMed:6060457};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:6060457};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000305|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:6016609}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion
CC membrane {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03216}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. PEMT/PEM2 methyltransferase family. {ECO:0000255|HAMAP-
CC Rule:MF_03216}.
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DR EMBL; CM002241; EAA30926.1; -; Genomic_DNA.
DR RefSeq; XP_960162.1; XM_955069.2.
DR AlphaFoldDB; Q7S5W9; -.
DR STRING; 5141.EFNCRP00000004586; -.
DR EnsemblFungi; EAA30926; EAA30926; NCU04699.
DR GeneID; 3876309; -.
DR KEGG; ncr:NCU04699; -.
DR VEuPathDB; FungiDB:NCU04699; -.
DR HOGENOM; CLU_086119_0_0_1; -.
DR InParanoid; Q7S5W9; -.
DR OMA; VITSTWA; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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: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; IBA:GO_Central.
DR HAMAP; MF_03216; PLMT; 1.
DR InterPro; IPR024960; PEMT/MFAP.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR PANTHER; PTHR15458; PTHR15458; 1.
DR Pfam; PF04191; PEMT; 1.
DR PIRSF; PIRSF005444; PEMT; 1.
DR PROSITE; PS51599; SAM_PEMT_PEM2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Methyltransferase; Mitochondrion; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..214
FT /note="Phosphatidyl-N-methylethanolamine N-
FT methyltransferase"
FT /id="PRO_0000437450"
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT INTRAMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 41..52
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 53..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 75..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 123..165
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 187..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 106..108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 188..189
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
SQ SEQUENCE 214 AA; 23587 MW; 84F376DAA77276CB CRC64;
MPLVALGVAD LFNFVDYSKT SLAISAAAIA FNPTFWNIVA RREYRTKFLT RAFGGNAQVA
CYFLAVTIFG LGLVRDFLYE RALRDQPSHP LLEGTYVKYA AYALLALGNL LVITSTMRLG
ITGTFLGDYF GILMDGIVTG FPFNVTSAPM YYGSTMSFLG TALLYGKPAG LLLTAWVLFV
YIIAIQFENP FTAEIYAKRD RERAKAAGTS KKEL
