PEAM2_ARATH
ID PEAM2_ARATH Reviewed; 491 AA.
AC Q944H0; F4HYI6; Q9LP63; Q9LP64;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphomethylethanolamine N-methyltransferase;
DE Short=AtPMEAMT;
DE EC=2.1.1.-;
DE AltName: Full=Phosphoethanolamine N-methyltransferase 2;
GN Name=NMT2; Synonyms=PMEAMT; OrderedLocusNames=At1g48600;
GN ORFNames=T1N15.22/T1N15.23, T1N15_20;
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20650897; DOI=10.1074/jbc.m110.112151;
RA Begora M.D., Macleod M.J., McCarry B.E., Summers P.S., Weretilnyk E.A.;
RT "Identification of phosphomethylethanolamine N-methyltransferase from
RT Arabidopsis and its role in choline and phospholipid metabolism.";
RL J. Biol. Chem. 285:29147-29155(2010).
CC -!- FUNCTION: Catalyzes N-methylation of phosphomonomethylethanolamine and
CC phosphodimethylethanolamine, the two methylation steps required to
CC convert phosphomonoethanolamine to phosphocholine. Unlike NMT1, NMT2
CC cannot utilize phosphoethanolamine as substrate in vitro.
CC {ECO:0000269|PubMed:20650897}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q944H0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q944H0-2; Sequence=VSP_053713;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:20650897}.
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=AAF79704.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79705.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC020889; AAF79704.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC020889; AAF79705.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32323.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32324.1; -; Genomic_DNA.
DR EMBL; AF428454; AAL16223.1; -; mRNA.
DR EMBL; AY063866; AAL36222.1; -; mRNA.
DR EMBL; AY133811; AAM91745.1; -; mRNA.
DR PIR; F96525; F96525.
DR RefSeq; NP_175293.1; NM_103756.3. [Q944H0-2]
DR RefSeq; NP_973993.1; NM_202264.2. [Q944H0-1]
DR PDB; 5WP5; X-ray; 1.50 A; A/B=1-491.
DR PDBsum; 5WP5; -.
DR AlphaFoldDB; Q944H0; -.
DR SMR; Q944H0; -.
DR BioGRID; 26506; 3.
DR STRING; 3702.AT1G48600.2; -.
DR iPTMnet; Q944H0; -.
DR PaxDb; Q944H0; -.
DR PRIDE; Q944H0; -.
DR ProteomicsDB; 236148; -. [Q944H0-1]
DR EnsemblPlants; AT1G48600.1; AT1G48600.1; AT1G48600. [Q944H0-2]
DR EnsemblPlants; AT1G48600.2; AT1G48600.2; AT1G48600. [Q944H0-1]
DR GeneID; 841281; -.
DR Gramene; AT1G48600.1; AT1G48600.1; AT1G48600. [Q944H0-2]
DR Gramene; AT1G48600.2; AT1G48600.2; AT1G48600. [Q944H0-1]
DR KEGG; ath:AT1G48600; -.
DR Araport; AT1G48600; -.
DR TAIR; locus:2198035; AT1G48600.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_029163_0_0_1; -.
DR InParanoid; Q944H0; -.
DR BioCyc; ARA:AT1G48600-MON; -.
DR BRENDA; 2.1.1.103; 399.
DR UniPathway; UPA00753; -.
DR PRO; PR:Q944H0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q944H0; baseline and differential.
DR Genevisible; Q944H0; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0000234; F:phosphoethanolamine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0052667; F:phosphomethylethanolamine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA: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 Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51582; SAM_PEAMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Repeat; S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9FR44"
FT CHAIN 2..491
FT /note="Phosphomethylethanolamine N-methyltransferase"
FT /id="PRO_0000204427"
FT BINDING 245..246
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 254
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 263..264
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 290
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 312
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 338..339
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 355
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 386
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 400
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 404..406
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT BINDING 472
FT /ligand="N-methylethanolamine phosphate"
FT /ligand_id="ChEBI:CHEBI:57781"
FT /evidence="ECO:0000250|UniProtKB:Q22993"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9FR44"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053713"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:5WP5"
FT TURN 63..67
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 148..161
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:5WP5"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 375..388
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 432..448
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:5WP5"
FT HELIX 459..477
FT /evidence="ECO:0007829|PDB:5WP5"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:5WP5"
SQ SEQUENCE 491 AA; 56045 MW; 9ECEE303C50200C6 CRC64;
MATPYKEERD IQKSYWMEHS SDLTVEAMML DSKASDLDKE ERPEVLSLIP PYEGKSVLEL
GAGIGRFTGE LAQKAGEVIA LDFIESAIQK NESVNGHYKN IKFMCADVTS PDLKIKDGSI
DLIFSNWLLM YLSDKEVELM AERMIGWVKP GGYIFFRESC FHQSGDSKRK SNPTHYREPR
FYTKVFQECQ TRDASGNSFE LSMVGCKCIG AYVKNKKNQN QICWIWQKVS VENDKDFQRF
LDNVQYKSSG ILRYERVFGE GYVSTGGFET TKEFVAKMDL KPGQKVLDVG CGIGGGDFYM
AENFDVHVVG IDLSVNMISF ALERAIGLKC SVEFEVADCT TKTYPDNSFD VIYSRDTILH
IQDKPALFRT FFKWLKPGGK VLITDYCRSA ETPSPEFAEY IKQRGYDLHD VQAYGQMLKD
AGFDDVIAED RTDQFVQVLR RELEKVEKEK EEFISDFSEE DYNDIVGGWS AKLERTASGE
QKWGLFIADK K
