CHO2_CANTT
ID CHO2_CANTT Reviewed; 866 AA.
AC C5M4D4;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 47.
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=CTRG_00924;
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; GG692395; EER36184.1; -; Genomic_DNA.
DR RefSeq; XP_002546142.1; XM_002546096.1.
DR AlphaFoldDB; C5M4D4; -.
DR SMR; C5M4D4; -.
DR STRING; 5482.XP_002546142.1; -.
DR EnsemblFungi; EER36184; EER36184; CTRG_00924.
DR GeneID; 8299973; -.
DR KEGG; ctp:CTRG_00924; -.
DR VEuPathDB; FungiDB:CTRG_00924; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR OrthoDB; 170424at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
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..866
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405885"
FT TOPO_DOM 1..65
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 87..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 115..175
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 197..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 229..263
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 285..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 308..353
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 375..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 401..425
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 447..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 475..523
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 545..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
SQ SEQUENCE 866 AA; 99648 MW; 2AF3E650C13EB1C0 CRC64;
MPSLTQTRST VSELNTSAIE TSTMSDSGHQ NKPKGPKGIT FSGETFIVPE THDMVKTLFD
PTIKKSNFEL IILGLLFSNL LVFLIPNNNL RISIFIGFYI FWRLSYNFGI GWLLQHQSND
HLLVQWAIKY KLFDKNNKNF LAKLVQSEIK SQRGDAYDIN SYPIEFNTWL IFRKFVDLIL
MSDFTTFICV VYACSINNDY QFIKNQPSWL TMSRIVGGSI LILFNYWVKV NAHNTIKDYA
WYWGDFFFRQ INNEELIFDG VFEMFPHPMY SVGYVGYYGF ALISKSYIVL LTAIFGHFLQ
MIFLHYIENP HIDKIYGPSK NEINLIKILK LKDLKNFDNL KPLVGLYNFN WMRASDVINL
VLSLTYGLII PVFAKSLKSL FVLTVATKLF ESLSINILLI LQSQFKFFTK WSLSNDIPIE
KSLNNWAVLY NSLINLTYSS LFGLNLGYFL QGTGSSLVTD YFYLRLFLGL CLIYTQSWIN
LSIIDSIGYF GWFYGDFFIP KSQSSIKNLT QAGVYRYLNN PEQIFGVCGV MGVFLIHPTV
ENLTCCILWM VNNFVRINFI EKIHMIRIYG EKEVNRDSGV TKTVKKHLIP DVIQRKMSND
DPKRRGGVAN GTSLGDSLDN FIKELRNSTT KLSQQKLIEL SQNLSFANSN YKLSIDGLKE
SNELKYTTIG TPITVSWQSP SNTHSIRDWV GLYKIVQTSY SRNKTILSSA GRWTYCTDSK
GVFTFEKEKL FWEEGVYEFR YHLDGKHDVA YISEPFEIKS VDIDVPGDIS EAGEFSKQLK
TEIFDKIIDI KSINESIAPI ANQADNVIEV YKLFSSLISK STQINVNYRI FLNNDNLSIS
DVAHKLIDIK QVLQELSFNS SEKKNL
