ID A0A090HWL1_9FIRM Unreviewed; 196 AA.
AC A0A090HWL1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN Name=plsC {ECO:0000313|EMBL:CDZ74462.1};
GN ORFNames=ING2D1G_0268 {ECO:0000313|EMBL:CDZ74462.1};
OS Peptoniphilus sp. ING2-D1G.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1912856 {ECO:0000313|EMBL:CDZ74462.1, ECO:0000313|Proteomes:UP000032409};
RN [1] {ECO:0000313|EMBL:CDZ74462.1, ECO:0000313|Proteomes:UP000032409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Peptoniphilus sp. ING2-D1G {ECO:0000313|Proteomes:UP000032409};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141,
CC ECO:0000256|RuleBase:RU361267};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004728}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC ECO:0000256|RuleBase:RU361267}.
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DR EMBL; LM997412; CDZ74462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090HWL1; -.
DR STRING; 1912856.ING2D1G_0268; -.
DR KEGG; ped:ING2D1G_0268; -.
DR PATRIC; fig|875453.3.peg.262; -.
DR HOGENOM; CLU_027938_4_5_9; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000032409; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW ECO:0000313|EMBL:CDZ74462.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Reference proteome {ECO:0000313|Proteomes:UP000032409};
KW Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:CDZ74462.1}.
FT DOMAIN 34..146
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 196 AA; 22243 MW; 4D46B3F00064D046 CRC64;
MLYKILRILV LIIFKIIFRC EIIGAEKIPA NTPVIISPNH KSNFDPFLVS ALVKPQIHWI
AKKELFEFKP LGALIYAVGG FPIDREKSNI KAIKTAMNIL KNNKILGLFP EGTRVKKPDF
ENPKSGVALI AHRTKSTVVP MYIDGNYTPF KKMKLIVRDP MDLSKLPKAE QKDYDSISLD
ILKSIYGVDE NKNYIS
//
