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Database: UniProt
Entry: A0A1D6MBP7_MAIZE
LinkDB: A0A1D6MBP7_MAIZE
Original site: A0A1D6MBP7_MAIZE 
ID   A0A1D6MBP7_MAIZE        Unreviewed;       463 AA.
AC   A0A1D6MBP7;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=phosphoethanolamine N-methyltransferase {ECO:0000256|ARBA:ARBA00035674};
DE            EC=2.1.1.103 {ECO:0000256|ARBA:ARBA00035674};
GN   ORFNames=ZEAMMB73_Zm00001d038891 {ECO:0000313|EMBL:AQK88176.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK88176.1};
RN   [1] {ECO:0000313|EMBL:AQK88176.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK88176.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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       phosphocholine from phosphoethanolamine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00035631}.
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DR   EMBL; CM000782; AQK88176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6MBP7; -.
DR   ExpressionAtlas; A0A1D6MBP7; baseline and differential.
DR   GO; GO:0000234; F:phosphoethanolamine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR025771; Phosphoethanolamine_N-MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR44307:SF14; OS05G0548900 PROTEIN; 1.
DR   PANTHER; PTHR44307; PHOSPHOETHANOLAMINE METHYLTRANSFERASE; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS51582; SAM_PEAMT; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AQK88176.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AQK88176.1}.
FT   DOMAIN          30..125
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13649"
FT   DOMAIN          254..373
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
SQ   SEQUENCE   463 AA;  52617 MW;  A2554C3A6827668C CRC64;
     MMLDSRAADL DKEERPEILS LLPSYKGKSV LELGAGIGRF TGDLAKEAGH VLALDFIESV
     IKKNQSINGH HKNITFRCAD VTSNDLKIED NSVDLIFSNW LLMYLSDEEV QKLVGKMVKW
     LKVGGHIFFR ESCFHQSGDS KRKVNPTHYR EPRFYTKVFK EGHSFDQDGG SFELSLVTCK
     CIGAYVKNKK NQNQICWLWE KVKSTEDRDF QRFLDNVQYK TSGILRYERV FGEGFVSTGG
     IETTKEFVGM LDLKPGQKVL DVGCGIGGGD FYMAANYDVH VLGIDLSVNM VSFAIERAIG
     RKCSVEFEVA DCTTKDYPEN SFDVIYSRDT ILHIQDKPAL FRSFFKWLKP GGKVLISDYC
     KNPGKPSEEF AAYIKQRGYD LHDVKAYGQM LKDAGFHNVI AEDRTEQFLN VLQREIGEVE
     KNKDAFLADF TQEDYDDIVN GWNAKLKRSS AGEQRWGLFI ATK
//
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