ID E7A1N9_SPORE Unreviewed; 1056 AA.
AC E7A1N9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=sr14055 {ECO:0000313|EMBL:CBQ73396.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ73396.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ73396.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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; FQ311472; CBQ73396.1; -; Genomic_DNA.
DR AlphaFoldDB; E7A1N9; -.
DR EnsemblFungi; CBQ73396; CBQ73396; sr14055.
DR VEuPathDB; FungiDB:sr14055; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR OrthoDB; 1561at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000008867; Chromosome 7.
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 PIRSF; PIRSF000383; PEAMT; 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};
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 109..131
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 187..208
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 284..306
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 474..492
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 118432 MW; 28EC8512BA956732 CRC64;
MATTDVPGTV PSDGLRNRKQ QPAGSDSPRS DSTEHASPSP RDAKESDTIK QHSNVLGRTP
DVFTVPHTPD MLSSIFDPRQ PKTPLDIVTV VSLSLQILLY FALSRRAAQI FFFLYFAFWR
ASYNAGLGWI LKQQSEKGWI IRQVKQHGWM DAQRRPRVHN WVKQQLVTKM DKDYVFDAMP
LDYNVWLMFR SMVDVVLLND FVAYSLFAFS CTRLPEGHSV AMHVLRWIAG WALIFFNLWV
KIDAHRVVKD YAWYWGDCFF LCLQSLVFDG VYEIAPDPMY SIGYAGYYGL SLVSGSYAVL
FVSLAAHFSQ FLFMTFFEGP HIERTYGERK PIAARVPLRQ APFNAASRKA AHADDGAADT
AQDLKVGASA TTPTQPSRST NETDFEGPTP SQTEGSTALD TEDDTSDDGH SRAFKRTALR
SSSSSNDAIQ HHLSGIDASH IQRPVTTLHD LHHRIFRKDT VVFRNLDLMR ANDLLLLVAS
VYALVPLSLP SLGPRARLTL LFLNALAWRT FHSFGLGVAL SRQSESKWIV RHFLKHYHYA
QPQDAVFEAF SHWKVVYNTS LVMTYISFGA LAWNCYTPVG HPDWTVGPEL LRHTLGLLLV
ALHCWTANSS YEVLGPFGWL YGDFFVDEYP HQLYYTGIYR FLNNPERSMG GAAFFGLALI
AGSKVTLLMA IVSYVAHWGF LSFVEGPHMR KLYGEAALRK DSGLTKQLKS QWVAAKDSDL
FRLAQEHPTI KNVQGTIEKV QRDAAEAFEE FFRQSRPRFE GMLEETKVLL QQSKDRLLIV
RVEDDHKMRS KGVDKSMYSL TVRPSGTGAK FHLGEPIAVE WRAAPNHSRR DWIGLYLLSR
LGGQQGADDA SLVTKISSQG KWLGVAEEEW IGDVHHASAR AHAGSAMASG VSVFRDTRLP
WVPGMYEFRY HHDGKHNVLA RSAPLEIYVG TLAPHTADLT QTTAIIRNIV HYSVPTSKPL
RLSISQPTPR ASVPEQALDE ASASPLVRPV GDDGDADDFT IWDRAQAARI STAIKWAFAL
ELSPEVVIAE ANVAKLAMDV VHGRRVLEPA FTPLMS
//
