PMT2_CAEEL
ID PMT2_CAEEL Reviewed; 437 AA.
AC Q22993;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Phosphoethanolamine N-methyltransferase 2 {ECO:0000305|PubMed:16681378};
DE Short=PMT-2 {ECO:0000303|PubMed:16681378};
DE EC=2.1.1.103 {ECO:0000269|PubMed:16681378};
DE AltName: Full=S-adenosyl-L-methionine:phosphomethylethanolamine N-methyltransferase {ECO:0000303|PubMed:16681378};
GN Name=pmt-2 {ECO:0000312|EMBL:CCD71034.1, ECO:0000312|WormBase:F54D11.1};
GN ORFNames=F54D11.1 {ECO:0000312|WormBase:F54D11.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RX PubMed=16681378; DOI=10.1021/bi060199d;
RA Palavalli L.H., Brendza K.M., Haakenson W., Cahoon R.E., McLaird M.,
RA Hicks L.M., McCarter J.P., Williams D.J., Hresko M.C., Jez J.M.;
RT "Defining the role of phosphomethylethanolamine N-methyltransferase from
RT Caenorhabditis elegans in phosphocholine biosynthesis by biochemical and
RT kinetic analysis.";
RL Biochemistry 45:6056-6065(2006).
RN [3] {ECO:0007744|PDB:4INE}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND PHOSPHOETHANOLAMINE.
RA Lukk T., Nair S.K.;
RT "Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis
RT elegant complexed with S-adenosyl homocysteine and phosphoethanolamine.";
RL Submitted (JAN-2013) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the last two methylation reactions in the synthesis
CC of phosphocholine, by converting phospho-monomethylethanolamine (N-
CC methylethanolamine phosphate) into phospho-dimethylethanolamine (N,N-
CC dimethylethanolamine phosphate) and the latter into phosphocholine.
CC Phosphocholine is a precursor for phosphatidylcholine, a major
CC component in membranes and a precursor itself in the production of
CC glycoconjugates secreted by parasitic nematodes to avoid host immune
CC responses. {ECO:0000269|PubMed:16681378}.
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:0000269|PubMed:16681378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25322;
CC Evidence={ECO:0000269|PubMed:16681378};
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:0000269|PubMed:16681378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25326;
CC Evidence={ECO:0000269|PubMed:16681378};
CC -!- ACTIVITY REGULATION: Feedback inhibition by phosphatidylcholine and
CC also by S-adenosylhomocysteine. {ECO:0000269|PubMed:16681378}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.27 mM for S-adenosyl-L-methionine {ECO:0000269|PubMed:16681378};
CC KM=3.34 mM for N-methylethanolamine phosphate
CC {ECO:0000269|PubMed:16681378};
CC KM=1.19 mM for N,N-dimethylethanolamine phosphate
CC {ECO:0000269|PubMed:16681378};
CC Vmax=555 nmol/min/mg enzyme with N,N-dimethylethanolamine phosphate
CC as substrate {ECO:0000269|PubMed:16681378};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from phosphoethanolamine. {ECO:0000269|PubMed:16681378}.
CC -!- DISRUPTION PHENOTYPE: Essential in multiple developmental steps, its
CC disruption causes developmentally impaired worms.
CC {ECO:0000269|PubMed:16681378}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; BX284605; CCD71034.1; -; Genomic_DNA.
DR PIR; T29330; T29330.
DR RefSeq; NP_504248.1; NM_071847.6.
DR PDB; 4INE; X-ray; 1.45 A; A/B=1-437.
DR PDBsum; 4INE; -.
DR AlphaFoldDB; Q22993; -.
DR SMR; Q22993; -.
DR STRING; 6239.F54D11.1.1; -.
DR BindingDB; Q22993; -.
DR SwissLipids; SLP:000000514; -.
DR World-2DPAGE; 0020:Q22993; -.
DR EPD; Q22993; -.
DR PaxDb; Q22993; -.
DR PeptideAtlas; Q22993; -.
DR EnsemblMetazoa; F54D11.1.1; F54D11.1.1; WBGene00018811.
DR GeneID; 178854; -.
DR KEGG; cel:CELE_F54D11.1; -.
DR UCSC; F54D11.1.1; c. elegans.
DR CTD; 178854; -.
DR WormBase; F54D11.1; CE11068; WBGene00018811; pmt-2.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_029163_0_0_1; -.
DR InParanoid; Q22993; -.
DR OMA; TGIDAYE; -.
DR OrthoDB; 425421at2759; -.
DR PhylomeDB; Q22993; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SABIO-RK; Q22993; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00018811; Expressed in larva and 4 other tissues.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity; IDA:WormBase.
DR GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IDA:WormBase.
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; IDA:WormBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR040516; PMT2_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF17987; PMT2_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..437
FT /note="Phosphoethanolamine N-methyltransferase 2"
FT /id="PRO_0000452992"
FT BINDING 186..187
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 195
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 204..205
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 232
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 254
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 281..282
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 298
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 329
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 343
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 347..349
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4INE"
FT BINDING 415
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:4INE"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:4INE"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4INE"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:4INE"
FT TURN 75..79
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:4INE"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:4INE"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 318..331
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 354..364
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 375..391
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:4INE"
FT HELIX 402..420
FT /evidence="ECO:0007829|PDB:4INE"
FT STRAND 424..432
FT /evidence="ECO:0007829|PDB:4INE"
SQ SEQUENCE 437 AA; 49769 MW; 6675E262F627D08B CRC64;
MSSLSIPRQS LYYVNKVTEG RSVSNVQVVS PCQKQGQTYV TAFTPLTSNV QVHTSLEQLS
TIRNADVLIF NNALSQIITN ADLLTDFLKN ATNATAIGGT VIIREDLKDC SDKRQVARLT
DYFDVFRTTD SDGNNTGLDL YTVDQVEHSN YVEQNFLDFI FVFRKKVFAP TTDATITFRD
FLDKTQYTNT GIDAYEWMFG VNFISPGGYD ENLKIIKRFG DFKPGQTMLD IGVGIGGGAR
QVADEFGVHV HGIDLSSNML AIALERLHEE KDSRVKYSIT DALVYQFEDN SFDYVFSRDC
IQHIPDTEKL FSRIYKALKP GGKVLITMYG KGYGEQSDKF KTYVAQRAYF LKNLKEIADI
ANKTGFVNVQ TENMTPRFKE ILLEERGHLE QNEAEFMSKF TQRERDSLIS GWTDKLGYIE
KDNHNWNFFL AQKPFPK
