ID A0A015L0A7_RHIIW Unreviewed; 929 AA.
AC A0A015L0A7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=RirG_061650 {ECO:0000313|EMBL:EXX73279.1};
OS Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX73279.1, ECO:0000313|Proteomes:UP000022910};
RN [1] {ECO:0000313|EMBL:EXX73279.1, ECO:0000313|Proteomes:UP000022910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA Huang S.;
RT "Single nucleus genome sequencing reveals high similarity among nuclei of
RT an endomycorrhizal fungus.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXX73279.1}.
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DR EMBL; JEMT01014767; EXX73279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A015L0A7; -.
DR STRING; 1432141.A0A015L0A7; -.
DR HOGENOM; CLU_005987_0_1_1; -.
DR OMA; RIWYSVG; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000022910; 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; 1.20.120.1630; -; 1.
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 InterPro; IPR041611; SKICH.
DR PANTHER; PTHR32138; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR32138:SF0; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR Pfam; PF04191; PEMT; 2.
DR Pfam; PF17751; SKICH; 1.
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:UP000022910};
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 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 78..99
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 362..381
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 388..411
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 471..492
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03217,
FT ECO:0000256|RuleBase:RU361122"
FT DOMAIN 718..811
FT /note="SKICH"
FT /evidence="ECO:0000259|Pfam:PF17751"
FT REGION 670..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 106071 MW; 6F7A3256B226FA8A CRC64;
MLNENQNDVK ANNDKDKEEI VYGKTHDAGV FQVPHTVDML TTVFDTKAKK STFDIFTFTV
IGCQVILFFV LPASTSRWLF LLLFFFWRFA YNVGLGIILK YQSDKRGVVL WIKRNKFFDK
EKNKKLYLFL KKELSTKMGS DYNFETAPLE FNAWLLFRQL VDLILLNDFT SYICFALANF
NIPEGSGVLI NIARWSGGLF LLWFNVWVKT DAHRVVKDFA WYWGDFFFLI DQSLTFDGVF
EMAPHPMYSV GYAGYYGISL MMASYKVLFV SLAAHAAQFA FLTFVENPHI EKTYNPPTPL
NAKLSKPIIS ETHEFTTSIN EVLSASNEIQ PTLPDLSNTS NYHFCRDLIV FKNFDLFRSN
DLFVIFIVIY AAIIPLSIAG ASNNAIKFFL VAQCLAWHIF HSYVLGAVLY FQSKNKFLTK
HYIKFGGNVS EAFSNWKSIY NLSLCMTYVT FLAAAWKMYY FPEDWTYGMV LLRHTLGMLL
IALHIWTSVS VFEVLGDFGW FYGDFFLDDY PTTLYYTGIY RFLNNPEKLI GHAAFWGITL
MANSWLIFGL ALFAQISSFL FLHYVESPHM RKLYGDKIRK DAGVTKTIKP PEFQVVKRVV
REVAETVEKV VEETAEVVGE IVEAARPRLQ GVVFETRSLL KNSTSAFIII IRRVTENIKN
QDLKQYSLAP VHPSNDLHNS SSNSMASLDN DKNETCSDAN PITFELGSPI CVKWTAPKNH
SRLDWIGIYK VTANSSKMVT SVSSKGRYFY VTPEEDDSDT GSKNIDNNDQ VETGDVCFKG
DKLPWEVGTY EFRYHHDKKY GVMAVSQPFE IAVNAPECVL DLPAIEQTVL TLVQRALDSN
PALIPYNTSD DYVLMKEVHA KRIVYGIKMM FGIDFAWEVV AIDGNVRRLA RRLLQACQAL
AILSSPPRRT EPWSGTNLPT SSPTDDLNI
//
