PEAM1_ARATH
ID PEAM1_ARATH Reviewed; 491 AA.
AC Q9FR44; Q9LVH3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Phosphoethanolamine N-methyltransferase 1;
DE Short=AtNMT1;
DE Short=PEAMT 1;
DE EC=2.1.1.103;
DE AltName: Full=Protein XIPOTL 1;
GN Name=NMT1; Synonyms=PEAMT, XPL1; OrderedLocusNames=At3g18000;
GN ORFNames=MEB5.22;
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 [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX PubMed=11115895; DOI=10.1104/pp.124.4.1800;
RA Bolognese C.P., McGraw P.;
RT "The isolation and characterization in yeast of a gene for Arabidopsis S-
RT adenosylmethionine:phospho-ethanolamine N-methyltransferase.";
RL Plant Physiol. 124:1800-1813(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15295103; DOI=10.1105/tpc.103.018648;
RA Cruz-Ramirez A., Lopez-Bucio J., Ramirez-Pimentel G., Zurita-Silva A.,
RA Sanchez-Calderon L., Ramirez-Chavez E., Gonzalez-Ortega E.,
RA Herrera-Estrella L.;
RT "The xipotl mutant of Arabidopsis reveals a critical role for phospholipid
RT metabolism in root system development and epidermal cell integrity.";
RL Plant Cell 16:2020-2034(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes N-methylation of phosphoethanolamine,
CC phosphomonomethylethanolamine and phosphodimethylethanolamine, the
CC three methylation steps required to convert phosphoethanolamine to
CC phosphocholine. Required for root system development and epidermal cell
CC integrity through its role in choline and phospholipid metabolism.
CC {ECO:0000269|PubMed:15295103}.
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:0000305}.
CC -!- DISRUPTION PHENOTYPE: Altered root development due to defect in primary
CC root elongation and root epidermal cell development.
CC {ECO:0000269|PubMed:15295103}.
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=BAB02720.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF197940; AAG41121.1; -; mRNA.
DR EMBL; AB019230; BAB02720.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76033.1; -; Genomic_DNA.
DR EMBL; AF367299; AAK32886.1; -; mRNA.
DR EMBL; AY058175; AAL25589.1; -; mRNA.
DR EMBL; AY091683; AAM10282.1; -; mRNA.
DR EMBL; AY093093; AAM13092.1; -; mRNA.
DR RefSeq; NP_188427.2; NM_112681.3.
DR PDB; 5WP4; X-ray; 1.34 A; A=1-491.
DR PDBsum; 5WP4; -.
DR AlphaFoldDB; Q9FR44; -.
DR SMR; Q9FR44; -.
DR BioGRID; 6657; 3.
DR STRING; 3702.AT3G18000.1; -.
DR iPTMnet; Q9FR44; -.
DR PaxDb; Q9FR44; -.
DR PRIDE; Q9FR44; -.
DR ProteomicsDB; 236339; -.
DR EnsemblPlants; AT3G18000.1; AT3G18000.1; AT3G18000.
DR GeneID; 821324; -.
DR Gramene; AT3G18000.1; AT3G18000.1; AT3G18000.
DR KEGG; ath:AT3G18000; -.
DR Araport; AT3G18000; -.
DR TAIR; locus:2088535; AT3G18000.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_029163_0_0_1; -.
DR InParanoid; Q9FR44; -.
DR OMA; EDFHKAN; -.
DR OrthoDB; 425421at2759; -.
DR PhylomeDB; Q9FR44; -.
DR BioCyc; ARA:AT3G18000-MON; -.
DR BRENDA; 2.1.1.103; 399.
DR UniPathway; UPA00753; UER00738.
DR PRO; PR:Q9FR44; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FR44; baseline and differential.
DR Genevisible; Q9FR44; AT.
DR GO; GO:0005737; C:cytoplasm; ISS:TAIR.
DR GO; GO:0008168; F:methyltransferase activity; ISS:TAIR.
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:0042425; P:choline biosynthetic process; IMP:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
DR GO; GO:0048528; P:post-embryonic root development; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
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 PANTHER; PTHR44307:SF6; PTHR44307:SF6; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51582; SAM_PEAMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Methyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..491
FT /note="Phosphoethanolamine N-methyltransferase 1"
FT /id="PRO_0000204426"
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:0007744|PubMed:22223895"
FT CONFLICT 333
FT /note="E -> G (in Ref. 4; AAM13092)"
FT /evidence="ECO:0000305"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 148..162
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:5WP4"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:5WP4"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:5WP4"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 375..388
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 432..448
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:5WP4"
FT HELIX 459..477
FT /evidence="ECO:0007829|PDB:5WP4"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:5WP4"
SQ SEQUENCE 491 AA; 56103 MW; DA4404EBED3FA8D5 CRC64;
MAASYEEERD IQKNYWIEHS ADLTVEAMML DSRASDLDKE ERPEVLSLLP PYEGKSVLEL
GAGIGRFTGE LAQKAGELIA LDFIDNVIKK NESINGHYKN VKFMCADVTS PDLKITDGSL
DLIFSNWLLM YLSDKEVELL AERMVGWIKV GGYIFFRESC FHQSGDSKRK SNPTHYREPR
FYSKVFQECQ TRDAAGNSFE LSMIGCKCIG AYVKNKKNQN QICWIWQKVS SENDRGFQRF
LDNVQYKSSG ILRYERVFGQ GFVSTGGLET TKEFVEKMNL KPGQKVLDVG CGIGGGDFYM
AEKFDVHVVG IDLSVNMISF ALERAIGLSC SVEFEVADCT TKHYPDNSFD VIYSRDTILH
IQDKPALFRT FFKWLKPGGK VLISDYCRSP KTPSAEFSEY IKQRGYDLHD VQAYGQMLKD
AGFTDVIAED RTDQFMQVLK RELDRVEKEK EKFISDFSKE DYDDIVGGWK SKLERCASDE
QKWGLFIANK N
