PEAM3_ARATH
ID PEAM3_ARATH Reviewed; 490 AA.
AC Q9C6B9; Q0WUL3; Q9C9V1;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phosphoethanolamine N-methyltransferase 3;
DE EC=2.1.1.103;
GN Name=NMT3; OrderedLocusNames=At1g73600; ORFNames=F25P22.1, F6D5.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes N-methylation of phosphoethanolamine,
CC phosphomonomethylethanolamine and phosphodimethylethanolamine, the
CC three methylation steps required to convert phosphoethanolamine to
CC phosphocholine. {ECO:0000250}.
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 -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from phosphoethanolamine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C6B9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C6B9-2; Sequence=VSP_040637;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. PEAMT family. {ECO:0000255|PROSITE-ProRule:PRU00915}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51806.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AC012679; AAG52075.1; -; Genomic_DNA.
DR EMBL; AC079676; AAG51806.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35480.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35481.1; -; Genomic_DNA.
DR EMBL; AK227139; BAE99185.1; -; mRNA.
DR RefSeq; NP_177501.2; NM_106018.4. [Q9C6B9-1]
DR RefSeq; NP_974139.2; NM_202410.2. [Q9C6B9-2]
DR AlphaFoldDB; Q9C6B9; -.
DR SMR; Q9C6B9; -.
DR STRING; 3702.AT1G73600.2; -.
DR PaxDb; Q9C6B9; -.
DR PRIDE; Q9C6B9; -.
DR ProteomicsDB; 236766; -. [Q9C6B9-1]
DR EnsemblPlants; AT1G73600.1; AT1G73600.1; AT1G73600. [Q9C6B9-1]
DR EnsemblPlants; AT1G73600.2; AT1G73600.2; AT1G73600. [Q9C6B9-2]
DR GeneID; 843694; -.
DR Gramene; AT1G73600.1; AT1G73600.1; AT1G73600. [Q9C6B9-1]
DR Gramene; AT1G73600.2; AT1G73600.2; AT1G73600. [Q9C6B9-2]
DR KEGG; ath:AT1G73600; -.
DR Araport; AT1G73600; -.
DR TAIR; locus:2027779; AT1G73600.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_029163_0_0_1; -.
DR InParanoid; Q9C6B9; -.
DR OMA; ECHSYDK; -.
DR OrthoDB; 425421at2759; -.
DR PhylomeDB; Q9C6B9; -.
DR BioCyc; ARA:AT1G73600-MON; -.
DR BRENDA; 2.1.1.103; 399.
DR UniPathway; UPA00753; UER00738.
DR PRO; PR:Q9C6B9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6B9; baseline and differential.
DR Genevisible; Q9C6B9; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000234; F:phosphoethanolamine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0052667; F:phosphomethylethanolamine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IMP:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:TAIR.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR025771; Phosphoethanolamine_N-MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR44307:SF4; PTHR44307:SF4; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51582; SAM_PEAMT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Methyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..490
FT /note="Phosphoethanolamine N-methyltransferase 3"
FT /id="PRO_0000204428"
FT BINDING 244..245
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 253
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 262..263
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 289
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 311
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 337..338
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 354
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 385
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 399
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 403..405
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 471
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT VAR_SEQ 1..5
FT /note="MASYG -> MAHSHTNGAISPSFSKDLC (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_040637"
FT CONFLICT 56
FT /note="V -> A (in Ref. 3; BAE99185)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="T -> A (in Ref. 3; BAE99185)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="T -> A (in Ref. 3; BAE99185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 56368 MW; 77FDFAFBC89C41CB CRC64;
MASYGEEREI QKNYWKEHSV GLSVEAMMLD SKASDLDKEE RPEILAFLPP IEGTTVLEFG
AGIGRFTTEL AQKAGQVIAV DFIESVIKKN ENINGHYKNV KFLCADVTSP NMNFPNESMD
LIFSNWLLMY LSDQEVEDLA KKMLQWTKVG GYIFFRESCF HQSGDNKRKY NPTHYREPKF
YTKLFKECHM NDEDGNSYEL SLVSCKCIGA YVRNKKNQNQ ICWLWQKVSS DNDRGFQRFL
DNVQYKSSGI LRYERVFGEG FVSTGGLETT KEFVDMLDLK PGQKVLDVGC GIGGGDFYMA
ENFDVDVVGI DLSVNMISFA LEHAIGLKCS VEFEVADCTK KEYPDNTFDV IYSRDTILHI
QDKPALFRRF YKWLKPGGKV LITDYCRSPK TPSPDFAIYI KKRGYDLHDV QAYGQMLRDA
GFEEVIAEDR TDQFMKVLKR ELDAVEKEKE EFISDFSKED YEDIIGGWKS KLLRSSSGEQ
KWGLFIAKRN
