ID R7VAP9_CAPTE Unreviewed; 367 AA.
AC R7VAP9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=phosphoethanolamine N-methyltransferase {ECO:0000256|ARBA:ARBA00035674};
DE EC=2.1.1.103 {ECO:0000256|ARBA:ARBA00035674};
GN ORFNames=CAPTEDRAFT_224919 {ECO:0000313|EMBL:ELU15923.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELU15923.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELU15923.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELU15923.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP224919}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; AMQN01017745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMQN01017746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB293476; ELU15923.1; -; Genomic_DNA.
DR AlphaFoldDB; R7VAP9; -.
DR STRING; 283909.R7VAP9; -.
DR EnsemblMetazoa; CapteT224919; CapteP224919; CapteG224919.
DR HOGENOM; CLU_064375_0_0_1; -.
DR OMA; DKHAAME; -.
DR Proteomes; UP000014760; Unassembled WGS sequence.
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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000014760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 158..254
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 367 AA; 41782 MW; 21DF90ED307BA869 CRC64;
MTHSSLPLTS PSIADLLPDF DADIDHASLN GIDPDVNLIT FSQSKYFNRL LTHDPHVGLS
VLSHNIRVLD LFLDSLATIT NTLATEKNTT YIIYSHVERI YKELEQLGIK DNDPLDVHQV
SQFDQYHYHG TESVAEATKK LGIETPPKTI LSSSSHRVLD IGAGLGGPSR YLAELTGCKV
TAIEMQEDLH LVATDLTRRC GLSQKVTHIC GDILKYDIGE AGKYDFIVSW LVFLHIPEKK
RLFEKCFGYL KASGQMYVED FWKKSEFLPE EKEILSERVY MRDPPPSDLD YIAQIKEAGF
DRVEFDDVTD SWSDFCKQRA ESYRKLKERH VRVHGKDVYE EQDAFFDAMD FLFHQGHLGG
CKLIATK
//
