(data stored in SCRATCH zone)

SWISSPROT: B6H782_PENRW

ID   B6H782_PENRW            Unreviewed;       196 AA.
AC   B6H782;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 50.
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   ORFNames=Pc16g02100 {ECO:0000313|EMBL:CAP92880.1}, PCH_Pc16g02100
GN   {ECO:0000313|EMBL:CAP92880.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92880.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92880.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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: S-adenosyl-L-methionine + phosphatidyl-N-
CC       dimethylethanolamine = S-adenosyl-L-homocysteine +
CC       phosphatidylcholine. {ECO:0000256|HAMAP-Rule:MF_03216}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + phosphatidyl-N-
CC       methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-
CC       dimethylethanolamine. {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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03216}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM920431; CAP92880.1; -; Genomic_DNA.
DR   RefSeq; XP_002560583.1; XM_002560537.1.
DR   STRING; 500485.XP_002560583.1; -.
DR   EnsemblFungi; CAP92880; CAP92880; PCH_Pc16g02100.
DR   GeneID; 8313942; -.
DR   KEGG; pcs:Pc16g02100; -.
DR   eggNOG; KOG4142; Eukaryota.
DR   eggNOG; ENOG4111HY0; LUCA.
DR   HOGENOM; HOG000208789; -.
DR   KO; K00550; -.
DR   OMA; PFTEEIY; -.
DR   OrthoDB; EOG092C45C1; -.
DR   BioCyc; PCHR:PC16G02100-MONOMER; -.
DR   UniPathway; UPA00753; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
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-HAMAP.
DR   GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-HAMAP.
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; B6H782.
DR   SWISS-2DPAGE; B6H782.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
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:UP000000724};
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     12       Lumenal. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   INTRAMEM     13     33       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   TRANSMEM     15     33       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM     34     45       Lumenal. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   TRANSMEM     45     66       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     86    108       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM    112    154       Lumenal. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   TRANSMEM    152    173       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM    176    196       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03216}.
FT   REGION       95     97       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03216}.
FT   REGION      177    178       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03216}.
SQ   SEQUENCE   196 AA;  21869 MW;  D8A3D8F9BA9648B4 CRC64;
     MASLTDFVDF SSKPLLWSAA TIAFNPIFWN IVARAEYRNH FLTRLFGGAY NGCYFLAFTI
     FSLGILRDHL YQLALADQPF YAPVHQPIVG GVLFAIGSVL VLSSMWALGV TGTYLGDYFG
     ILMDAPVTGF PFNVTGSPMY WGSTLNFLGV ALYQGKVAGI LLTAQVFVLY WFALGWEDPF
     TAEIYAKRER ERAKKQ
//

If you have problems or comments...

PBIL Back to PBIL home page