ID CHO2_PARBA Reviewed; 979 AA.
AC C1GZK1;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-MAY-2023, entry version 63.
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; ORFNames=PAAG_03945;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN294000; EEH42024.2; -; Genomic_DNA.
DR RefSeq; XP_002794352.2; XM_002794306.2.
DR AlphaFoldDB; C1GZK1; -.
DR SMR; C1GZK1; -.
DR STRING; 502779.C1GZK1; -.
DR GeneID; 9097550; -.
DR KEGG; pbl:PAAG_03945; -.
DR VEuPathDB; FungiDB:PAAG_03945; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_0_1; -.
DR OMA; RIWYSVG; -.
DR OrthoDB; 1561at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 2.60.40.2840; -; 1.
DR HAMAP; MF_03217; PEMT; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR PANTHER; PTHR32138; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR32138:SF0; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
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..979
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405901"
FT TOPO_DOM 1..89
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 111..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 135..199
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 221..227
FT /note="Cytoplasmic"
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..281
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 303..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 326..398
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 399..418
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 419..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 423..445
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 446..474
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 475..494
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 495..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 521..565
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 587..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 110825 MW; 06E5437C136FF2E4 CRC64;
MSGPASSTGF HIHAEGLHER NVQPSKPTSD GGVAPKALDD KSRVEEDERT DSEKKTFGRT
PGGTIFTVPP TRDMVSQLLS PSEPKNLSDI FVLAIISCHI FLLRFLPSSF RVAAFAIIFL
FWRAAYNIGI GWLLHMQSNG RTLVCWAKKS NIFVNPSTGR NPHPVLYNLL KWELETKIPE
QYSFEDAPTE YNTWLVFRRV VDLILMCDFT SYCLFAIACG GRPAGEGFIM LALRWITGMS
LVLFNLWVKL DAHRVVKDFA WYWGDFFYLI DQDLTFDGVF EMAPHPMYSV GYAGYYGISL
MAASYKLLFI SILAHAAQFA FLVLVENPHI EKTYNAPPPR KRVAVDTDNV KPQDDDVSQD
SSVINDNEYS GKAVATLEPS SMHNLLGPHN FDLYRITDSS VLLIQILFSA LAILTPSTPV
YQFFFVLNAA LWRVWYSVGI GYILNRQSHC KMWTRHFVKY GESNQEAWQQ WKGTYHLSMT
MTYASFIAAT WKMYSFPQDW GYGLVLLRHI LGASLIALQI WTSASIYESL GEFGWFFGDF
FFDQSPKLTY SGIYRYLNNP ERVLGLAGVW GAVLITSTKS VISLALLSHT LTIAFIQLVE
RPHMQKLYGQ SLRRDAGLVR SLKRSLPPSL KQFHGSVDKI LDDSIEFIEE FIEAARPKLA
AGVKTFVKDT SALFQKYPAR ITISRLEPDL AGYDQKDYSI SLEGTQSSEP AQFERASDKE
GEKARSMPDR RGEQVNLMFE YGAPIKVKWT APLNHSKKDW IGLYMVTDNT SREITRISSQ
GRWIGTNKAS FDSLTCEQGL ISSDIVINKF REDGEPKDVA SGEMVFSGDK LWWTQGVFEF
RYHHNGKHNV MAVSRPFEIR IGRFDDDAIY GDRYGLVRAA IESALLPVVQ NCFDRDPDIA
PQTVEEQYGS LVDRNGKYSR RVVFAVHQMF GIEFAPEVVR ADGNVRNLAW RICNAKKVLA
PYSMSRTNGA TTPTAEHES
//
