CHO2_ASHGO
ID CHO2_ASHGO Reviewed; 843 AA.
AC Q754G0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=AFR110C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53481.1; -; Genomic_DNA.
DR RefSeq; NP_985657.1; NM_211011.1.
DR AlphaFoldDB; Q754G0; -.
DR STRING; 33169.AAS53481; -.
DR EnsemblFungi; AAS53481; AAS53481; AGOS_AFR110C.
DR GeneID; 4621900; -.
DR KEGG; ago:AGOS_AFR110C; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR InParanoid; Q754G0; -.
DR OMA; DWVGLYM; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000000591; Chromosome VI.
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; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
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..843
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405872"
FT TOPO_DOM 1..52
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 74..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 105..166
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 188..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 221..246
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 268..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 301..348
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 349..366
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 367..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 393..419
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 441..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 474..512
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 534..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
SQ SEQUENCE 843 AA; 97840 MW; FBCD12EF2964D3A2 CRC64;
MTETKSGKAV APAAQDSVAG TLAVCRSSGE EFRVPKTHDM LRSLFDPRLR KSFLELCITL
SLVANCAFCY WSWRVMGGEW AMRMYLAQYL AWRLTYNLGI GLILHYQSHY EFLTEFAKRN
GLFASGAASK SWLASFCQFE IASKMPREYD MAQYPTEFNV WLLFRQFVDL VLMQDFTTYV
LYVLLSFSKS QVTWSLLQHL NWTSCRVYVG TLMLLLNVWV KMDAHRVVKD YAWYWGDFFF
LLKDSNLIFD GVFNISPHPM YSIGYMGYYG VSLITGDYRV LLVSILGHFL QFLFLKYVET
PHIERIYGPD QPSSIERVDD QIIKNNRNYT RPLMMTYFWF KNFDPLRPTD YFTVGTAAAS
ISAILLNPKK ETVFAITLFV KLVTSMVNFF ILRRQSTDKW FTKLFLRNGY TQLYSYQMWQ
FIYNFNLMLS YVTLALQTWI QFQALSQHDY TNVIFGFILV ALHIWADGEI LNALTEFGWF
YGDFFLTNYI QRPKLASHGI YRYLKNPECV LGVAGAWGTV LITDFSVENI ILATIWTLSN
HIMVTFVESP HVAKVYGNEM LARQSGVGKT LLGFTPIKHF SDWLDKFSGS LIDMLNVSTE
GRDQLEDVIA AALQATTRKL SPDSEFEINR DSENNSDGDF SFTIGDSIEI SWKLPRELYH
DEDWIGLYRV LETGEDRYRT LVSSRDHWCA TNTMGYPKSV KAIGAVKEFT KGDTCVQGRV
VFDHNLLYFE KGVYEFRYHS TSGHKVLMIS PPFKITVPQL DLDTPEALYQ STVKLLEKCH
CLNENGRFEH SKNKYLSERT LQKLFRNSTG ADISSDYMKR VNYEIREITE RIYEMKKILD
SLR
