ID A0A0C4EXP2_PUCT1 Unreviewed; 1108 AA.
AC A0A0C4EXP2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122};
DE Short=PE methyltransferase {ECO:0000256|HAMAP-Rule:MF_03217};
DE Short=PEAMT {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122};
DE Short=PEMT {ECO:0000256|HAMAP-Rule:MF_03217};
DE EC=2.1.1.17 {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122};
GN ORFNames=PTTG_05591 {ECO:0000313|EMBL:OAV93214.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EnsemblFungi:PTTG_05591P0, ECO:0000313|Proteomes:UP000005240};
RN [1] {ECO:0000313|EMBL:OAV93214.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV93214.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|Proteomes:UP000005240};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Fellers J., Bakkeren G., Szabo L., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblFungi:PTTG_05591P0}
RP IDENTIFICATION.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_05591P0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:OAV93214.1, ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV93214.1}, and Isolate 1-1
RC / race 1 (BBBD) {ECO:0000313|Proteomes:UP000005240};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EnsemblFungi:PTTG_05591P0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_05591P0};
RX PubMed=27913634; DOI=10.1534/g3.116.032797;
RA Cuomo C.A., Bakkeren G., Khalil H.B., Panwar V., Joly D., Linning R.,
RA Sakthikumar S., Song X., Adiconis X., Fan L., Goldberg J.M., Levin J.Z.,
RA Young S., Zeng Q., Anikster Y., Bruce M., Wang M., Yin C., McCallum B.,
RA Szabo L.J., Hulbert S., Chen X., Fellers J.P.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL G3 (Bethesda) 7:361-376(2017).
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:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122}.
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:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03217, ECO:0000256|RuleBase:RU361122};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. CHO2 family. {ECO:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03217,
CC ECO:0000256|RuleBase:RU361122}.
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DR EMBL; ADAS01006510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADAS02000053; OAV93214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4EXP2; -.
DR STRING; 630390.A0A0C4EXP2; -.
DR EnsemblFungi; PTTG_05591T0; PTTG_05591P0; PTTG_05591.
DR VEuPathDB; FungiDB:PTTG_05591; -.
DR OMA; RIWYSVG; -.
DR OrthoDB; 1561at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000005240; Unassembled 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 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 PROSITE; PS51598; SAM_CHO2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03217};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_03217};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_03217};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03217};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03217,
KW ECO:0000256|RuleBase:RU361122};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_03217};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_03217}; Reference proteome {ECO:0000313|Proteomes:UP000005240};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03217,
KW ECO:0000256|RuleBase:RU361122};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03217,
KW ECO:0000256|RuleBase:RU361122};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03217};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03217}.
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 238..255
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 299..332
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 470..488
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 592..610
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 667..686
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 128807 MW; F78AB9A3119211F5 CRC64;
MVDDSTTSRK PGVVVVAPSP PADENPKTNS PQKAEAEIEP DRKHDEQGKN RQKSTYGKTM
DGTVFKIPET HNMISSLFDP RLPKSSLDLI TLSTLIAQTI PLMIFPRRTL KTFYMVSFLF
WRLTYNVGLG WVLKKQSENK FLIKIIRNLN LFNSKFNPRL SNWIEKQLKS KMSTNNLNYD
LNKYPIEFNV WLLFRQLVDI ILLNDFFSYF CLSYCSLKLP HQQQSQQEPQ HQSNLSVFLI
RWALGVILVG FNIWVKLDAH RIVHDFAWYW GDAFFLSLQE LVFDGVFEMA PHPMYSIGYA
GFYGASLITG SQSVFFVSLF AHLCQFGFLV YFENPHIQRT YGPQARPLTA ASPRHQLRSR
SHPRKKIQPL NFNSPNETPK VVSPDYRDTH HDTSSAHGSN TFQEPTQHPV DPAEVREQLE
HRLFRRKEMI MIDNFDKFRS IDFVTILVIA YNFLILFIKE DDSRGSKKIY NNKGLLISSL
NAIAWRIWFS FGLGFRLKQQ SQNKMMVKHF LTKYYYPIGK FRHSAQKHED EIHNADDHND
LIDDLKFEVI EECFQNWKGI YNLSLIMTYV SFAIMSVKFH KLENQWELSS ELIRITFGLC
LVGIHVWTAI STYEVLGKFG WFYGDFFVDD YPMELSYAGI YRYLNNPERS MGGAGFIGMS
LMSGNKLVFA LALCSVLCHW WFLSFVETPH MKKVYGDRIR KEAGLTKVLK QNAQKLAARR
KNLDLRIDRE SASSLGGGKI DEKEGKGFER RFKEVQGTFE FIYDETVQAL DEFLEKSAPR
LSGVVRDTKV LLQSSGERLI LTRIANDLSS YDTTQYRLTM QESRYHRPRD PECNRLRFHM
GEPIRLQWTS PWNHSRADWI GCYRRGSNKS GLVTEVTSSG RWCGLFEEEW EGDMHIGKRR
EQGEESLDPQ GKDLKVENDS AKPPKTGWVE FKGERLPWEE GVYEFRFHHG GKYNVMAVTE
PFEIYVERIE EDVEHMKQIE DKLRNLVGYG LGMEPDLIPL RLRKESERIL SRDEPRPPTQ
NGVRHENNGQ HSEEILAKGE DGQSDEEVEE EDRFTVMSLE EAKRIQRLIG IGIGIELGIE
IILEDCEIYR LAKRIVFVKS LLKPFLNK
//
