ID D8RIF9_SELML Unreviewed; 495 AA.
AC D8RIF9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=phosphoethanolamine N-methyltransferase {ECO:0000256|ARBA:ARBA00035674};
DE EC=2.1.1.103 {ECO:0000256|ARBA:ARBA00035674};
GN ORFNames=SELMODRAFT_270875 {ECO:0000313|EMBL:EFJ28238.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ28238.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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; GL377580; EFJ28238.1; -; Genomic_DNA.
DR RefSeq; XP_002970912.1; XM_002970866.1.
DR AlphaFoldDB; D8RIF9; -.
DR STRING; 88036.D8RIF9; -.
DR EnsemblPlants; EFJ28238; EFJ28238; SELMODRAFT_270875.
DR GeneID; 9633186; -.
DR Gramene; EFJ28238; EFJ28238; SELMODRAFT_270875.
DR KEGG; smo:SELMODRAFT_270875; -.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_029163_0_0_1; -.
DR InParanoid; D8RIF9; -.
DR OMA; CHSYDKD; -.
DR OrthoDB; 2249143at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0000234; F:phosphoethanolamine N-methyltransferase activity; IEA:InterPro.
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; IPR041698; Methyltransf_25.
DR InterPro; IPR025771; Phosphoethanolamine_N-MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR44307; PHOSPHOETHANOLAMINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR44307:SF2; PHOSPHOETHANOLAMINE METHYLTRANSFERASE ISOFORM X1; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF13649; Methyltransf_25; 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 Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 58..153
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 495 AA; 56751 MW; 3F25294B16396265 CRC64;
MAAPILSTER DAQLSYWKEH STALTVEEML LDSQAAKLDQ EERPEILSML PPLEGISVVE
LGAGIGRFTG DLAKSAKHVV AMDFVQSVID KNKEVNGCHR NVEFLCADVT SPSLTFPRSS
KDLIFSNWLL MYLSDDEVTA LTKKMIFWLK RGGSIFFRES CFHQSGDHKR KNNPTHYREP
RFYNKIFEEC YIAEEDGSYS KLQLVLFKCV SAYVKNKRNQ NQICWMWKKI KCTGPDGLKF
QQFLDNVQYT QRGILRYERI FGEGFVSTGG LETTKEFVES LKLEAGQKVL DVGCGIGGGD
FYMAEDFDVQ VVGIDLSVNM VSIALERSIG RKCFVEFEVA DCTEKNFPAE SFDVIYSRDT
ILHIQDKPAL FARLLSWLKP GGKLLITDYC RSRDEVSAEF LEYIKKRGYD LHDVDHYGQM
LRDAGFVDVV AEDRTDQFVR ILTKELDTVE RNKKSFLQDF SEEDYEDIVQ GWKSKLVRCG
QGHQKWGLFR ATKKM
//
