(data stored in SCRATCH zone)

SWISSPROT: C5DC91_LACTC

ID   C5DC91_LACTC            Unreviewed;       217 AA.
AC   C5DC91;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 52.
DE   RecName: Full=Phosphatidyl-N-methylethanolamine N-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03216};
DE            EC=2.1.1.71 {ECO:0000256|HAMAP-Rule:MF_03216};
DE   AltName: Full=Phospholipid methyltransferase {ECO:0000256|HAMAP-Rule:MF_03216};
DE            Short=PLMT {ECO:0000256|HAMAP-Rule:MF_03216};
GN   OrderedLocusNames=KLTH0B01122g {ECO:0000313|EMBL:CAR21402.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21402.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21402.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Catalyzes the second two steps of the methylation
CC       pathway of phosphatidylcholine biosynthesis, the SAM-dependent
CC       methylation of phosphatidylmonomethylethanolamine (PMME) to
CC       phosphatidyldimethylethanolamine (PDME) and of PDME to
CC       phosphatidylcholine (PC). {ECO:0000256|HAMAP-Rule:MF_03216}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine
CC         + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-
CC         phosphocholine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:32739, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03216};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-
CC         adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-
CC         dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573;
CC         EC=2.1.1.71; Evidence={ECO:0000256|HAMAP-Rule:MF_03216};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03216}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03216}. Mitochondrion membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03216}.
CC   -!- SIMILARITY: Belongs to the class VI-like SAM-binding
CC       methyltransferase superfamily. PEMT/PEM2 methyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03216}.
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DR   EMBL; CU928166; CAR21402.1; -; Genomic_DNA.
DR   RefSeq; XP_002551840.1; XM_002551794.1.
DR   STRING; 381046.XP_002551840.1; -.
DR   EnsemblFungi; CAR21402; CAR21402; KLTH0B01122g.
DR   GeneID; 8290666; -.
DR   KEGG; lth:KLTH0B01122g; -.
DR   HOGENOM; HOG000208789; -.
DR   InParanoid; C5DC91; -.
DR   KO; K00551; -.
DR   OMA; PFTEEIY; -.
DR   OrthoDB; 1395721at2759; -.
DR   UniPathway; UPA00753; -.
DR   Proteomes; UP000002036; Chromosome B.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03216; PLMT; 1.
DR   InterPro; IPR024960; PEMT/MFAP.
DR   InterPro; IPR007318; Phopholipid_MeTrfase.
DR   PANTHER; PTHR15458; PTHR15458; 1.
DR   Pfam; PF04191; PEMT; 1.
DR   PIRSF; PIRSF005444; PEMT; 1.
DR   PROSITE; PS51599; SAM_PEMT_PEM2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DC91.
DR   SWISS-2DPAGE; C5DC91.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03216, ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03216};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_03216,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03216,
KW   ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM      1     29       Lumenal. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   INTRAMEM     30     50       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   TOPO_DOM     51     62       Lumenal. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   TRANSMEM     70     89       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM     84    110       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   TRANSMEM    109    128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM    132    174       Lumenal. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   TRANSMEM    172    190       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM    196    217       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   REGION      115    117       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03216}.
FT   REGION      197    198       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03216}.
SQ   SEQUENCE   217 AA;  24294 MW;  8EC2AC167377FD97 CRC64;
     MDLFNDLTGK LGKVQDVYIE MLSEVVTDEK NLKLALFFIV FNPLFWNTAA RLEYKTHFLT
     KITGSAKRGC YVLAVTIFSL GIVRDYFFHQ ALMQQPTSRV LDTDAVRKAG MVLSAFGQVL
     VATSMYQLGV TGTYLGDYFG ILMDNIVTAF PFNVSNNPMY HGSTLTFLGT SLYYGKAAGV
     FATVLVNLVY NIAQQFEEPF TAQIYAKRDA ERTKKSS
//

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