PEMT2_DICDI
ID PEMT2_DICDI Reviewed; 200 AA.
AC Q54H80;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase B {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03216};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03216};
DE EC=2.1.1.71 {ECO:0000255|HAMAP-Rule:MF_03216};
DE AltName: Full=Phospholipid methyltransferase B {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PLMT {ECO:0000255|HAMAP-Rule:MF_03216};
GN Name=pemtB; ORFNames=DDB_G0289645;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the three sequential steps of the methylation
CC pathway of phosphatidylcholine biosynthesis, the SAM-dependent
CC methylation of phosphatidylethanolamine (PE) to
CC phosphatidylmonomethylethanolamine (PMME), PMME to
CC phosphatidyldimethylethanolamine (PDME), and PDME to
CC phosphatidylcholine (PC). {ECO:0000255|HAMAP-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:0000255|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; EC=2.1.1.71;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03216};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03216};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03216}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane
CC {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; AAFI02000147; EAL62640.1; -; Genomic_DNA.
DR RefSeq; XP_636144.1; XM_631052.1.
DR AlphaFoldDB; Q54H80; -.
DR STRING; 44689.DDB0267052; -.
DR PaxDb; Q54H80; -.
DR EnsemblProtists; EAL62640; EAL62640; DDB_G0289645.
DR GeneID; 8627247; -.
DR KEGG; ddi:DDB_G0289645; -.
DR dictyBase; DDB_G0289645; pemtB.
DR eggNOG; KOG4142; Eukaryota.
DR HOGENOM; CLU_086119_0_0_1; -.
DR InParanoid; Q54H80; -.
DR OMA; NGDSFGH; -.
DR PhylomeDB; Q54H80; -.
DR UniPathway; UPA00753; -.
DR PRO; PR:Q54H80; -.
DR Proteomes; UP000002195; Chromosome 5.
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:0004608; F:phosphatidylethanolamine 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 3: Inferred from homology;
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..200
FT /note="Phosphatidylethanolamine N-methyltransferase B"
FT /id="PRO_0000328072"
FT TOPO_DOM 1..8
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT INTRAMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 30..39
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 59..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 108..150
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 172..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 91..93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 174..175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
SQ SEQUENCE 200 AA; 22416 MW; D632C30CA132797E CRC64;
MEKGLSSDLI IAFVAIVLHV VNYNVTAQFE YKTRYFTKLI GRNAIYYYAV FLIISALIRD
HFINVAVLSD KDSIILFPTE IANMIGDSCF IFGILLNIWT LKALGIKGMY NGDSFGHIMD
SPVTGGPYQF FSDPQYVGTT IAALGVAIRN QSIYGFLCTI LVGVVFYISA TFVETPHLKN
IYSNRSYSKI NFKNLKSLKN
