PEAMT_SPIOL
ID PEAMT_SPIOL Reviewed; 494 AA.
AC Q9M571;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Phosphoethanolamine N-methyltransferase;
DE EC=2.1.1.103;
GN Name=PEAMT;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=cv. Savoy hybrid 612; TISSUE=Leaf;
RX PubMed=10799484; DOI=10.1074/jbc.275.19.14095;
RA Nuccio M.L., Ziemak M.J., Henry S.A., Weretilnyk E.A., Hanson A.D.;
RT "cDNA cloning of phosphoethanolamine N-methyltransferase from spinach by
RT complementation in Schizosaccharomyces pombe and characterization of the
RT recombinant enzyme.";
RL J. Biol. Chem. 275:14095-14101(2000).
CC -!- FUNCTION: Catalyzes N-methylation of phosphoethanolamine,
CC phosphomonomethylethanolamine and phosphodimethylethanolamine, the
CC three methylation steps required to convert phosphoethanolamine to
CC phosphocholine. Mediates a key step in the biosynthesis of choline, a
CC precursor of the osmoprotectant glycine betaine. Has no
CC ethanolamine- or phosphatidylethanolamine-N-methyltransferase activity.
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:0000255|PROSITE-ProRule:PRU00915};
CC -!- ACTIVITY REGULATION: Inhibited by phosphocholine but not by choline,
CC glycine betaine, monomethylethanolamine or dimethylethanolamine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.8-8.5.;
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from phosphoethanolamine: step 1/1.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By salt stress.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. PEAMT family. {ECO:0000255|PROSITE-ProRule:PRU00915}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF237633; AAF61950.1; -; mRNA.
DR AlphaFoldDB; Q9M571; -.
DR SMR; Q9M571; -.
DR BRENDA; 2.1.1.103; 5812.
DR SABIO-RK; Q9M571; -.
DR UniPathway; UPA00753; UER00738.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000234; F:phosphoethanolamine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052667; F:phosphomethylethanolamine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR025771; Phosphoethanolamine_N-MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51582; SAM_PEAMT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Repeat;
KW S-adenosyl-L-methionine; Stress response; Transferase.
FT CHAIN 1..494
FT /note="Phosphoethanolamine N-methyltransferase"
FT /id="PRO_0000204429"
FT BINDING 248..249
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 257
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 266..267
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 293
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 315
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 341..342
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 358
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 389
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 403
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 407..409
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 475
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
SQ SEQUENCE 494 AA; 56361 MW; 7F2537C8E4B8413B CRC64;
MAASAMGVLQ EREVFKKYWI EHSVDLTVEA MMLDSQASDL DKVERPEVLS MLPPYEGKSV
LELGAGIGRF TGELAEKASQ VIALDFIESV IKKNESINGH YKNVKFMCAD VTSPSLNISP
NSVDIIFSNW LLMYLSDEEV ERLVERMLKW LKPGGYIFFR ESCFHQSGDH KRKSNPTHYR
EPRFYTKIFK ECHMQDDSGN SYELSLIGCK CIGAYVKSKK NQNQISWLWQ KVDSEDDKGF
QRFLDSSQYK FNSILRYERV FGPGYVSTGG LETTKEFVSK LDLKPGQKVL DVGCGIGGGD
FYMAENYDVE VVGIDLSINM ISFALERSIG LKCAVEFEVA DCTKKDYPEN SFDVIYSRDT
ILHIQDKPAL FRSFHKWLKP GGKVLISDYC KSAGTPSAEF AAYIRQRGYD LHDVKAYGKM
LKDAGFVEVI AENRTDQFIQ VLQKELDALE QEKDDFIDDF SEEDYNDIVD GWKAKLVRTT
EGEQQWGLFI AKKM
