CHO2_BOTFB
ID CHO2_BOTFB Reviewed; 972 AA.
AC A6S950;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PE methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217};
GN Name=CHO2; ORFNames=BC1G_08742;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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:0000255|HAMAP-Rule:MF_03217}.
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:0000255|HAMAP-Rule:MF_03217};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03217}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. CHO2 family. {ECO:0000255|HAMAP-Rule:MF_03217}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476899; EDN29728.1; -; Genomic_DNA.
DR RefSeq; XP_001552264.1; XM_001552214.1.
DR AlphaFoldDB; A6S950; -.
DR SMR; A6S950; -.
DR OMA; DWVGLYM; -.
DR UniPathway; UPA00753; -.
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: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 Pfam; PF04191; PEMT; 2.
DR PIRSF; PIRSF000383; PEAMT; 1.
DR PROSITE; PS51598; SAM_CHO2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Methyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..972
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405880"
FT TOPO_DOM 1..80
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 102..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 126..190
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 212..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 240..268
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 290..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 317..390
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 412..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 440..480
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 502..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 526..557
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 579..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 109834 MW; D77D0AF7B0737AA0 CRC64;
MSTSSMKSQD SNGLRERINN GSATNDDNMT ARCGSEPPSE DFELDKDKKT FGRTPDGTIP
QTHDMVSQLL DPRQPKNLSD LIVLVILALH IFALYALPSS LKRPVFAVIF LFWRGCYNVG
IGYLLHIQSH HKRIVAWAKK WNLFENPVTG KNPRPWLYQL IKTELETKIP EDYKFEQAPI
EYNTWLVFRR VVDLILMCDF TSYCLFAIAC GGAPSDEGLV MSTLRWGAGI ILVLFNLWVK
LDAHRVVKDY AWYWGDFFYL IDQELTFDGV FEMAPHPMYS VGYAGYYGIS MMAASYSVLA
ISIVAHMAQF AFLLVVENPH IDKTYNPPPP RKHQDNPTPS DIDHANALAS SKEGLEYSLD
SSPTQTPPLN TTQPLAVHNL MGLGNIDLFR ITDVSILLLL GYVFLITALT PSTPVYQALF
VINAMFWRLW YSVGLGIILD RQSSKKMWTR HFVKYGDSTE EAWRQWKGMY HLSMTMCYAS
FIAATWKMYS IPSDWAYGLV LLRHVLGAGL VSLQLWTAIS IYESLGEFGW FFGDFFFDHA
PKLTYSGIYR YLNNPERIIG LAGIWGAVFI TGSRAIFCLA LLSHTLTLAF LQFVEKPHMQ
KLYGRNLRSE AGLSKSIKRS LPPQIKKWHG NVDRVLEETG HFVEEFLDAA RPKLAAGVST
IFRDTSALFS QYPARLTLTR IAPDLAGYDP RDYSVTIEGT SSDSALHKRT TSKEGITARI
PQERMDGFKP LVFEYGAPIK VKWTAPTKHS KADWIVTRIP SAGRWVATVP NEYESSPADQ
GILVSNRFVS GSKRIDGSTQ DYVEGEMIFE GDKLFWTQGV FEFRYHHDGK HNVMAISLPF
EIRIPRFDDE NSNVNITLDS DNSQSQSLIR SAVEQALLPV VRNCFDRDPD IAPNSVDESF
GVLVARDGKY PRRVVHAVHF MFGIEFAPEV VRADGNVRNL AWRICNAKQV LAPYSMSHSK
GTNTPDVDGE KA
