ID R9ANH3_WALI9 Unreviewed; 995 AA.
AC R9ANH3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=J056_003907 {ECO:0000313|EMBL:EOR01671.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR01671.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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; KE007229; EOR01671.1; -; Genomic_DNA.
DR RefSeq; XP_009267391.1; XM_009269116.1.
DR AlphaFoldDB; R9ANH3; -.
DR STRING; 1299270.R9ANH3; -.
DR GeneID; 20376859; -.
DR KEGG; wic:J056_003907; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR OMA; RIWYSVG; -.
DR OrthoDB; 1561at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000014064; 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 Gene3D; 2.60.40.2840; -; 1.
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; 1.
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:UP000014064};
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 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 528..546
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 591..618
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 995 AA; 112701 MW; 89E0817FDB57C753 CRC64;
MEPEERIKST QSTLRQRGQV EVEEDADNAI NADAHTHSEE ILGKTPDGTM FAVPPTADVI
SSLFHPKYPK THVDILTLAI LGLQVLGFAL MPLSTSRVVY LYVFIFWRLS YNVGLGWVLS
RQSRSQWIVN WVKQHGFLDA NKRPAMRNWV ENQIKTKMGP GYSFDKCPPE FNTWIFFRHA
VDIILLSDFV AYVCFAWAHC RLPTGHGVLW HVLRWAAGWT MILFNLWVKI DAHRVIHDYA
WYWGDTFFQQ IQSLKFDGVF ELAPHPMYSI GYAGFYGLSL VVGSYQVLCV SLLAHALQFG
FLLWFENPHI ERTYGERKPL AERVPFALRE DTVHAEHAEH DAHIPPTPAA TDATTDTDTD
VDECVTQFDD KPTPATKVEG YPHSPNNLHD LEHKYFSRDL IIFKNFDVFR SNDFSTALVV
AYAVVGSFMP NFSYGTSLTL HISHVIAWRT FHSVGLGYLL KAQSEEKYLI KHYLKYYAHV
NANEAKRSAF DSWKRVYNLS LIMVYVSFVG LALKTYTLPQ QWTVGTELLK HVVGILLIIL
QVWCSLESHE VLGNFGWFFG NFFLEEFPSR LNYTGIYRYV NDPERSMGGA ALFGISLISG
SATTFALAVF SYILHWWFLS CVENPHTKKL FGSGVRTTGG AARTLTKAVK DGRRRSSSSL
FNQNSLDRFD RVAKDVQGQV HRVYGETVDV VEDFLKSAKP SVDKMVQDTR VLLHQSRERL
VITRVDKDLS AYDVSKYSLS LKPSISPRQP TSYHLGEPIE VEWTAPANHS RKDWIGIYRV
GANTDHLVTR ISSRGKWQPI HDGEFDGARP IPDRPTSHVG KSSAAAATAT QEEEGQRGVV
SFCSNSLPWS VGRYELRYHH AGKHNVMASC GPLELYVDKP TDGDDFESVR NTLSRCVAFA
LNCDPALVPA SSWHHLPENT IHSYRRNTPD VDRDDDDMVI MDDEQARRIA VVIRVACSVD
FTPSVVVADA NLSRLAQRVL DTRRVLGIDD GEGDT
//
