CHO2_ASPNC
ID CHO2_ASPNC Reviewed; 1077 AA.
AC A2R616;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 54.
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=An15g06310;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270348; CAK42583.1; -; Genomic_DNA.
DR AlphaFoldDB; A2R616; -.
DR SMR; A2R616; -.
DR PaxDb; A2R616; -.
DR EnsemblFungi; CAK42583; CAK42583; An15g06310.
DR HOGENOM; CLU_005987_0_0_1; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000006706; Chromosome 3R.
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..1077
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405877"
FT TOPO_DOM 1..85
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 107..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 131..195
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 217..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 245..277
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 299..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 322..392
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 414..419
FT /note="Cytoplasmic"
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..482
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 504..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 528..575
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 597..1077
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT REGION 330..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 121697 MW; 29B154B24F83D6CD CRC64;
MDRGLSTGTH IGDDGLRERF QASQSDSSLG AGALTAAGEV EAKDGTSQNK KTFGRTPDGT
VFTVPQTHDM VSQLLSPSEP KNLSDVIVLA ILGAHILLLW WLPDFAKIPV FAVIYLFWRA
AYNAGIGWLL HNQSHHKTLV RWAEKTRIFV NPSTNQNPHP KLYNLLKREL ETKIPTDYSF
EEAPIEYNTW LVFRRLVDLI LMCDFTSYCL FAIACSHHPV GESMLMTVSR WSAGIVLVLF
NLWVKLDAHR VVKDYAWYWG DFFYLIDQEL TFDGVFEMAP HPMYSVGYAG YYGISLMAAS
YKVLFISIIA HAAQFAFLVF VENPHIDKTY NPPPPRKRMT EQDSVSTSSQ ATEPSVASAS
TDEPLPQATT PPSGPPPSVH NLLGFNNLDL YRITDTSSIL IQLLVFALTV LTPSTPRYQF
LFVANAAVWR LVFSVGIGYL LTEQSDCKAW TRHFLKYGET PNEAWNQWKG TYHLSMIMCY
ASFIAAVWKM YTLPADWGYG LVLLRHVLGA GLISLQIWTS ASIYESLGEF GWFYGDFFFE
GAHKLTYNGI YRFLNNPERV LGLAGVWGAV LITSSGAITF LALLSHILSL AFIQFVERPH
MQKLYGRSLR QDAGLVKSLK RTLPPTLRQL HGSVDKIFDD SFEFIEELID TARPKLAAGV
NTFVKDTTAL FQKYPARVTI TRIDEDLAGL DSRDYALEIE GTDSSSLEER GDLKNLVFEY
GSPIKVKWTA PLNHSKKDWV SLYRVTDNTS REVSRVSSQG RWVATNEGFY DNLTCEKGII
TSDIVTENSE HRDVATGEVI FSGDKLFWTQ GVFEFRYHHN GKHNVMAISR PFEIRIRRFD
EESFEDNQAS VEKSLLPVVR NCFDRDPEIA PETVEEQFGS LVERDGKFAK RVVFAVHQMF
GIEFAPEVVR ADGTVRNLAW RICNAKRVLA PYSMTRDGAT TPTEAHEKDE AFTKARVTAM
IRRRTRRDSK SAGRRESQLT IHENVVLRYR AWTPFKRIEY MEGSAKPGNS SHPLPVPIPR
QAIQNERRGG KKALTQVRHN KQADADNADN NDVACLSRTP QPSSLERLPS SRGKKRA
