ID A0A137NWG6_CONC2 Unreviewed; 200 AA.
AC A0A137NWG6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CONCODRAFT_19809 {ECO:0000313|EMBL:KXN67170.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN67170.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN67170.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN67170.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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}.
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DR EMBL; KQ964655; KXN67170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137NWG6; -.
DR STRING; 796925.A0A137NWG6; -.
DR EnsemblFungi; KXN67170; KXN67170; CONCODRAFT_19809.
DR OMA; PTFWNIA; -.
DR OrthoDB; 1499at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000070444; 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:KXN67170.1};
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:UP000070444};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03216};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03216, ECO:0000313|EMBL:KXN67170.1};
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..9
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT INTRAMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 31..42
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 42..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 64..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 112..154
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT TRANSMEM 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 176..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT BINDING 95..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
FT BINDING 177..178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03216"
SQ SEQUENCE 200 AA; 22368 MW; D6534D1E1C80B748 CRC64;
MLKDLDLSQQ SLYLSAASIC FNPLFWNIVA RNEYRQKTIQ NIVGSPKVGC YLLGATIFSL
GLIRDYLYKL ALEAQPASEA LNLPFIAPLS AGLVLVGNVL VLSSYFRLGF VGTFLGDYFG
ILMDEPVTGF PFNVSDNPMY HGSTLIFLGT ALWYQKLSGV YLTVLVSVVY YLAIQFENPF
TTMIYANRDK VEKKKSKKLN
//
