ID K1WU79_MARBU Unreviewed; 204 AA.
AC K1WU79;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ORFNames=MBM_06023 {ECO:0000313|EMBL:EKD16012.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16012.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16012.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16012.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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}.
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DR EMBL; JH921440; EKD16012.1; -; Genomic_DNA.
DR RefSeq; XP_007293912.1; XM_007293850.1.
DR AlphaFoldDB; K1WU79; -.
DR STRING; 1072389.K1WU79; -.
DR GeneID; 18761958; -.
DR KEGG; mbe:MBM_06023; -.
DR eggNOG; KOG4142; Eukaryota.
DR HOGENOM; CLU_086119_0_0_1; -.
DR InParanoid; K1WU79; -.
DR OMA; CRSEYRT; -.
DR OrthoDB; 1499at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000006753; 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 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|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|HAMAP-Rule:MF_03216,
KW ECO:0000313|EMBL:EKD16012.1};
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:UP000006753};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03216};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03216, ECO:0000313|EMBL:EKD16012.1};
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..3
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TOPO_DOM 31..42
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 TOPO_DOM 65..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 113..155
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 177..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT BINDING 178..179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
SQ SEQUENCE 204 AA; 22262 MW; 0CDFF9DFC69BB5F0 CRC64;
MQNKGLVDFD QKSLATPPTR PSSLQQSPNA PSEYHNKILT KLAGGNARHG CYGLAVTIFL
LGIFRDLLYE RALRAQPSHP LLETPLATYI SYALLATGNL LVLSSMWALG ITGTYLGDYF
GILMDDIVTG FPFSVTQSPM YYGSTMSFLG TAILFGKPAG ILLTVEVLVV YLIALRFEDP
FTATIYAKRE KSRIGGNGDA KKEL
//
