PLSY_SALAR
ID PLSY_SALAR Reviewed; 205 AA.
AC A9MPV6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=SARI_04422;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX24199.1; -; Genomic_DNA.
DR RefSeq; WP_001272781.1; NC_010067.1.
DR AlphaFoldDB; A9MPV6; -.
DR SMR; A9MPV6; -.
DR STRING; 41514.SARI_04422; -.
DR EnsemblBacteria; ABX24199; ABX24199; SARI_04422.
DR KEGG; ses:SARI_04422; -.
DR HOGENOM; CLU_081254_0_2_6; -.
DR OMA; WRHRGNL; -.
DR OrthoDB; 1691856at2; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000002084; 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;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..205
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000084392"
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; 22130 MW; AB5887C469DE4733 CRC64;
MSAIAPGMIL FAYLCGSISS AILVCRIAGL PDPRESGSGN PGATNVLRIG GKGAAVAVLI
FDILKGMLPV WGAYALGITP FWLGLIAIAA CLGHIWPVFF GFKGGKGVAT AFGAIAPIGW
DLTGVIAGTW LLTVLLSGYS SLGAIVSALI APFYVWWFKP QFTFPVSMLS CLILLRHHDN
IQRLWRRQET KIWTKLKKKR EKESK
