CHO2_KOMPG
ID CHO2_KOMPG Reviewed; 890 AA.
AC C4QXE9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PE methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217};
GN Name=CHO2; OrderedLocusNames=PAS_chr1-4_0093;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
CC -!- FUNCTION: Catalyzes the first step of the methylation pathway of
CC phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine
CC (PMME). {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03217};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03217}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. CHO2 family. {ECO:0000255|HAMAP-Rule:MF_03217}.
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DR EMBL; FN392319; CAY67922.1; -; Genomic_DNA.
DR RefSeq; XP_002490203.1; XM_002490158.1.
DR AlphaFoldDB; C4QXE9; -.
DR STRING; 644223.C4QXE9; -.
DR EnsemblFungi; CAY67922; CAY67922; PAS_chr1-4_0093.
DR GeneID; 8197310; -.
DR KEGG; ppa:PAS_chr1-4_0093; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR InParanoid; C4QXE9; -.
DR OMA; DWVGLYM; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000000314; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03217; PEMT; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR Pfam; PF04191; PEMT; 2.
DR PIRSF; PIRSF000383; PEAMT; 1.
DR PROSITE; PS51598; SAM_CHO2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Methyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..890
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405908"
FT TOPO_DOM 1..51
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 73..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 97..150
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 172..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 201..227
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 249..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 280..330
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 352..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 376..446
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 490..531
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 553..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
SQ SEQUENCE 890 AA; 103146 MW; 7B1B7105FD619594 CRC64;
MVKESKFSYN SKDEKKYSLG KTFRGDIFNV PETHDMVRSL FDPTVKKSVS DYLIVLSLFI
NGIVYYYSPV TWRIPVFIVL YSFWRLGYNL GIGILLYKQS KSHSMFHWLK QIQINGGWAK
KFVELELSSK LNAQQLNSVP DEFKTWIVFR SLVNLILMND FTTYMCLVFA CSDGAFNQSL
SLIFLRWVLG ISFFIFNIIV KLNAHLIVKD YAWYWGDFFF RLHNNEELIF DGVFDLAPHP
MYSIGYAGYY GCALMTKSYT VLIMSIFGHL LQFLFLNYVE TPHIEKIYGD DNLSENTISV
NKRDDSVFIG TGGKPLVMLT KNFNWLRTND IFTVVLALYA SIVPIFLPAS YNNSIIILAI
VVKIGTSFVL NSVLYLQSRF KSWTLSFIKN YGTINISILD NKELLERLSF QNWTLLQNNT
LVLNYSMLFT ISVREVMYNE KFWQTEWLPL RFILAALMIL GQFLTVHQMI DSIGLFGWYY
GDFFIGVLSS HKSEVTTLSR SGIYHFLNNP ERVTSNLTVW ALYLLFNNSN KIFLVIALLF
TMNNLIVLNF IEKPHMVKLY GEQNVLKHTS GIEKSINSLF LPNHVQGTIV KLSGSIDKVI
QDSSKVIDEF IRNKHNQKPK ELSLKKRRNS FQQVIELIRG STDDTLTINL QELNDQGQLQ
LLNLLRKDDT DFYNLGDPIK VEWNMEDHKG KDKAWIGLYN IFQTSETRTK TLVSSKGYWI
PIHREKYINL SDKIRNEEDC ILEDELNRGV VQFSAELLPW VPGTYELRLH ANEKHEVLAI
SKPFDIVVKK IDVPTSDDIG DERLEDFANK LYQGFVSKLF PAVESIEDES NWFLQMHIKE
NARQVEKLCS TLSQSCGVHL TKKAIVDEKC LKDLSFKISK LRKMLDELML
