ID B7FFD6_MEDTR Unreviewed; 221 AA.
AC B7FFD6;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=phosphoethanolamine N-methyltransferase {ECO:0000256|ARBA:ARBA00035674};
DE EC=2.1.1.103 {ECO:0000256|ARBA:ARBA00035674};
DE Flags: Fragment;
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:ACJ83326.1};
RN [1] {ECO:0000313|EMBL:ACJ83326.1}
RP NUCLEOTIDE SEQUENCE.
RA Moskal W., Chan A., Cheung F., Xiao Y., Town C.D.;
RT "Medicago truncatula full length cdna cloning project.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine =
CC H(+) + phosphocholine + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:25325, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:58641, ChEBI:CHEBI:59789, ChEBI:CHEBI:295975;
CC EC=2.1.1.103; Evidence={ECO:0000256|ARBA:ARBA00035588};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25326;
CC Evidence={ECO:0000256|ARBA:ARBA00035588};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-methylethanolamine phosphate + S-adenosyl-L-methionine =
CC H(+) + N,N-dimethylethanolamine phosphate + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:25321, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57781, ChEBI:CHEBI:57856, ChEBI:CHEBI:58641,
CC ChEBI:CHEBI:59789; EC=2.1.1.103;
CC Evidence={ECO:0000256|ARBA:ARBA00035580};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25322;
CC Evidence={ECO:0000256|ARBA:ARBA00035580};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphoethanolamine + S-adenosyl-L-methionine = H(+) + N-
CC methylethanolamine phosphate + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:20365, ChEBI:CHEBI:15378, ChEBI:CHEBI:57781,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58190, ChEBI:CHEBI:59789;
CC EC=2.1.1.103; Evidence={ECO:0000256|ARBA:ARBA00035571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20366;
CC Evidence={ECO:0000256|ARBA:ARBA00035571};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004969}.
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DR EMBL; BT050657; ACJ83326.1; -; mRNA.
DR AlphaFoldDB; B7FFD6; -.
DR ProMEX; B7FFD6; -.
DR ExpressionAtlas; B7FFD6; differential.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR44307; PHOSPHOETHANOLAMINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR44307:SF2; PHOSPHOETHANOLAMINE METHYLTRANSFERASE ISOFORM X1; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 63..158
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT NON_TER 221
FT /evidence="ECO:0000313|EMBL:ACJ83326.1"
SQ SEQUENCE 221 AA; 25178 MW; 68BEB3A47C477D4F CRC64;
MAHLEAMKQG GEDEREVQRS YWKEHCVNLS VESMMLDSNA SHLDKEERPE VLSLLPSYEG
KSVLELGAGI GRFTAELAQK AGQLLAVDFI ESAIKKNENT NGHHKNVKFM CADVTSPNLH
ISEGSVDLIF SNWLLMYLSD EEVKNLAERM VKWLNVNGCI FFRESCFHQS GDSKRKYNPT
HYREPRFYTN VFKECHMSDD NGNSFELSLV GCKCIGAYVR N
//
