PLSY_ECOSE
ID PLSY_ECOSE Reviewed; 205 AA.
AC B6I430;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_01043};
DE EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_01043};
DE EC=2.3.1.n5 {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Lysophosphatidic acid synthase {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=LPA synthase {ECO:0000255|HAMAP-Rule:MF_01043};
GN Name=plsY {ECO:0000255|HAMAP-Rule:MF_01043}; Synonyms=ygiH;
GN OrderedLocusNames=ECSE_3339;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(2008).
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to
CC glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This
CC enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl-
CC PO(4). {ECO:0000255|HAMAP-Rule:MF_01043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01043};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42300, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n5; Evidence={ECO:0000255|HAMAP-Rule:MF_01043};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01043}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
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DR EMBL; AP009240; BAG78863.1; -; Genomic_DNA.
DR RefSeq; WP_001272796.1; NC_011415.1.
DR AlphaFoldDB; B6I430; -.
DR SMR; B6I430; -.
DR EnsemblBacteria; BAG78863; BAG78863; ECSE_3339.
DR GeneID; 66673042; -.
DR KEGG; ecy:ECSE_3339; -.
DR HOGENOM; CLU_081254_0_2_6; -.
DR OMA; WRHRGNL; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000008199; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:InterPro.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01043; PlsY; 1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR PANTHER; PTHR30309; PTHR30309; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
DR TIGRFAMs; TIGR00023; TIGR00023; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..205
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000136087"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TOPO_DOM 25..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TOPO_DOM 74..80
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TOPO_DOM 102..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TOPO_DOM 133..137
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TOPO_DOM 159..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ SEQUENCE 205 AA; 22193 MW; 13066C8FBA2543E2 CRC64;
MSAIAPGMIL IAYLCGSISS AILVCRLCGL PDPRTSGSGN PGATNVLRIG GKGAAVAVLI
FDVLKGMLPV WGAYELGVSP FWLGLIAIAA CLGHIWPVFF GFKGGKGVAT AFGAIAPIGW
DLTGVMAGTW LLTVLLSGYS SLGAIVSALI APFYVWWFKP QFTFPVSMLS CLILLRHHDN
IQRLWRRQET KIWTKFKRKR EKDPE
