ID C5XHH2_SORBI Unreviewed; 499 AA.
AC C5XHH2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=phosphoethanolamine N-methyltransferase {ECO:0000256|ARBA:ARBA00035674};
DE EC=2.1.1.103 {ECO:0000256|ARBA:ARBA00035674};
GN ORFNames=SORBI_3003G266500 {ECO:0000313|EMBL:EES01313.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EES01313.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EES01313.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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; CM000762; EES01313.1; -; Genomic_DNA.
DR RefSeq; XP_002456193.1; XM_002456148.1.
DR AlphaFoldDB; C5XHH2; -.
DR STRING; 4558.C5XHH2; -.
DR EnsemblPlants; EES01313; EES01313; SORBI_3003G266500.
DR GeneID; 8063104; -.
DR Gramene; EES01313; EES01313; SORBI_3003G266500.
DR KEGG; sbi:8063104; -.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_029163_0_0_1; -.
DR InParanoid; C5XHH2; -.
DR OrthoDB; 2249143at2759; -.
DR Proteomes; UP000000768; Chromosome 3.
DR ExpressionAtlas; C5XHH2; baseline and differential.
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; IPR025714; Methyltranfer_dom.
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:SF8; PHOSPHOETHANOLAMINE N-METHYLTRANSFERASE-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 66..161
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT DOMAIN 290..406
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
SQ SEQUENCE 499 AA; 56625 MW; 9F3340035E33F3F2 CRC64;
MAAAAAAAVN GSLDVHERKA QRSYWEEHSG ELTLEAMMLD SRAAELDKEE RPEVLSLLPS
YEGKSVLELG AGIGRFTGEL AKTSGHVFAV DFIESAIKKN ESTNGHYDNT SFMCADVTSP
NLMIEANSID LIFSNWLLMY LSDEEIDKLV ERMVKWLKVG GYIFFRESCF HQSGDLERKV
NPTHYREPRF YTKVFKECQT FNQDGTSFKL SLVTFKCIGA YVNIKKDQNQ ICWLWQKVNS
LEDGGFQSFL DNVQYKATGI LRYERIFGDG YVSTGGVETT KEFVDKLDLK PGQKVLDVGC
GIGGGDFYMA EKYGTHVVGI DLSINMILFA LERSIGRKCS VEFEVADCTT KTYPDHMFDV
IYSRDTILHI QDKPSLFKSF FKWLKPGGKV LISDYCKSPG KPSEEFAAYI KQRGYDLHDV
EAYGQMLKNA GFSHVIAEDR TDQFLSVLQK ELDKFEKNKD DFLSEFAQGD YDDIVNGWKA
KLQRTSAREQ RWGLFVATK
//
