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Phosphatidyl-N-methylethanolamine N-methyltransferase (EC 2.1.1.71) (Phospholipid methyltransferase) (PLMT)

 A0A084FYV7_9PEZI        Unreviewed;       208 AA.
A0A084FYV7;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
27-SEP-2017, entry version 15.
RecName: Full=Phosphatidyl-N-methylethanolamine N-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03216};
EC=2.1.1.71 {ECO:0000256|HAMAP-Rule:MF_03216};
AltName: Full=Phospholipid methyltransferase {ECO:0000256|HAMAP-Rule:MF_03216};
Short=PLMT {ECO:0000256|HAMAP-Rule:MF_03216};
ORFNames=SAPIO_CDS8094 {ECO:0000313|EMBL:KEZ40269.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ40269.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ40269.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ40269.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the second two steps of the methylation
pathway of phosphatidylcholine biosynthesis, the SAM-dependent
methylation of phosphatidylmonomethylethanolamine (PMME) to
phosphatidyldimethylethanolamine (PDME) and of PDME to
phosphatidylcholine (PC). {ECO:0000256|HAMAP-Rule:MF_03216}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + phosphatidyl-N-
dimethylethanolamine = S-adenosyl-L-homocysteine +
phosphatidylcholine. {ECO:0000256|HAMAP-Rule:MF_03216}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + phosphatidyl-N-
methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-
dimethylethanolamine. {ECO:0000256|HAMAP-Rule:MF_03216}.
-!- PATHWAY: Phospholipid metabolism; phosphatidylcholine
biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03216}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
{ECO:0000256|HAMAP-Rule:MF_03216}. Mitochondrion membrane
{ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
{ECO:0000256|HAMAP-Rule:MF_03216}.
-!- SIMILARITY: Belongs to the class VI-like SAM-binding
methyltransferase superfamily. PEMT/PEM2 methyltransferase family.
{ECO:0000256|HAMAP-Rule:MF_03216}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ40269.1}.
-----------------------------------------------------------------------
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EMBL; JOWA01000121; KEZ40269.1; -; Genomic_DNA.
RefSeq; XP_016640068.1; XM_016789805.1.
EnsemblFungi; KEZ40269; KEZ40269; SAPIO_CDS8094.
GeneID; 27727166; -.
UniPathway; UPA00753; -.
Proteomes; UP000028545; Unassembled WGS sequence.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_03216; PLMT; 1.
InterPro; IPR024960; PEMT/MFAP.
InterPro; IPR007318; Phopholipid_MeTrfase.
PANTHER; PTHR15458; PTHR15458; 1.
Pfam; PF04191; PEMT; 1.
PIRSF; PIRSF005444; PEMT; 1.
PROSITE; PS51599; SAM_PEMT_PEM2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03216};
Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03216};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03216};
Membrane {ECO:0000256|HAMAP-Rule:MF_03216, ECO:0000256|SAM:Phobius};
Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03216,
ECO:0000313|EMBL:KEZ40269.1};
Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03216};
Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03216};
Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_03216};
Reference proteome {ECO:0000313|Proteomes:UP000028545};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03216};
Transferase {ECO:0000256|HAMAP-Rule:MF_03216,
ECO:0000313|EMBL:KEZ40269.1};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_03216,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03216,
ECO:0000256|SAM:Phobius}.
TOPO_DOM 1 13 Lumenal. {ECO:0000256|HAMAP-
Rule:MF_03216}.
INTRAMEM 14 34 Helical. {ECO:0000256|HAMAP-
Rule:MF_03216}.
TRANSMEM 16 33 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 35 46 Lumenal. {ECO:0000256|HAMAP-
Rule:MF_03216}.
TRANSMEM 53 73 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 69 95 Cytoplasmic. {ECO:0000256|HAMAP-
Rule:MF_03216}.
TRANSMEM 93 121 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 117 159 Lumenal. {ECO:0000256|HAMAP-
Rule:MF_03216}.
TRANSMEM 142 159 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 165 191 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 181 208 Cytoplasmic. {ECO:0000256|HAMAP-
Rule:MF_03216}.
REGION 100 102 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_03216}.
REGION 182 183 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_03216}.
SEQUENCE 208 AA; 23004 MW; 57CB4F0E0A0BCAFC CRC64;
MSVSITDLVD FDQQSLYISA AAIAFNPLFW NIVARQEYRN KILTKLFLGN SQIACYFLAL
TIFSLGMVRD YLYKEALAPQ PSHPALETDA VKLASYALFA AGNILVITST WALGITGTFL
GDYFGILMDD MVTGFPFNVT DAPMYYGSTM SFLAAALYYG KPAGVLLTVW VFLVYKVALA
FENPFTAGIY AKRDRERAAQ KKGSKKAE


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