ID A0A135SS32_9PEZI Unreviewed; 843 AA.
AC A0A135SS32;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=CSAL01_03068 {ECO:0000313|EMBL:KXH38743.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH38743.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH38743.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH38743.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) 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: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {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:KXH38743.1}.
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DR EMBL; JFFI01002267; KXH38743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135SS32; -.
DR SMR; A0A135SS32; -.
DR STRING; 1209931.A0A135SS32; -.
DR OrthoDB; 1093299at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000070121; 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:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
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; IPR001046; NRAMP_fam.
DR InterPro; IPR024960; PEMT/MFAP.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR NCBIfam; TIGR01197; nramp; 1.
DR NCBIfam; NF037982; Nramp_1; 1.
DR PANTHER; PTHR11706:SF101; MANGANESE TRANSPORTER SMF1; 1.
DR PANTHER; PTHR11706; SOLUTE CARRIER PROTEIN FAMILY 11 MEMBER; 1.
DR Pfam; PF01566; Nramp; 1.
DR Pfam; PF04191; PEMT; 1.
DR PRINTS; PR00447; NATRESASSCMP.
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 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:UP000070121};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TOPO_DOM 1..16
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT INTRAMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TOPO_DOM 85..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 109..129
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 167..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 197..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 366..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 725..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 811..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 214..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 843 AA; 91338 MW; 9FDC09BE54BA067D CRC64;
MAPVQIDNKA LVDFDQKSLL VSAAAIAFNP LFWKFVKSPP SCPSSYRLTR SPEYKNKILT
KLAGGRSQAA CYGLAATIFS LGIFRDLLYE RALRFQPAHP LLASDTVTYV GYALVACGNV
LVLSSTWQLG ITGTFLGDYF GILMDSIVTG FPFNITDAPM YNGSTMSFLG AALIYGKPAG
ILLTVWVFIV YQIALRYENP FTAGIYSKRD RERAAGKDTK KIRGSNAAAH KRSHASRTRS
KSVVATWDTM KPTWLDEPVA QQGGSSRRSS VSPFTADYTI SQTLHGQSHS ESRRLSGDVP
PDFINLNAIV SSQGTSASTE DFPPKTLKKQ TRIDDEGPFS LLEGPTLPLP SHAVHKREKR
WINRRWSDLL TFGKFVGPGF MIAVAYIDPG NYATDIAAGA SYHFDLLFIV LLSNVVAIFL
QGLAIKLGTI TGLDLATACR VFLPKWMNII VYALAEIAIV ATDMAVVIGT ATAIHLLIPK
LPLLACVVLT IVDVVFIVVF YRPDGSMRGL RLFEIGVCFL VLGVVVCFCI QLSLIENTTV
GQVFRGYLPS SSIIQTQGLY QSCGILGATV MPHSLHLGSG VVQSRLKDFD MKEGNLQELP
RSDTMTTVDS YHKVFYFPSM AAIKHCMKFS IAEIVFSLFI FALFVNSAIL IVAGSALYQG
QTSLASDIFG MHGLLANSIS SAAGIIFAFA LLLSGVSAGL VCTIAGQLVS EGALNWRMRP
WLRRLATRLI SVTPTIVVVA VAGQSGLSNA LTGTQVVLST VLPVITAPLI YFTSFNKYMT
VVPGAASYGS DTGVVPARRF SAVGVKMANS WWVTVLAVLL WLMITVMVVA NLVLLVLNAH
NSN
//
