PLSB_PEA
ID PLSB_PEA Reviewed; 457 AA.
AC P30706;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Glycerol-3-phosphate acyltransferase, chloroplastic;
DE Short=GPAT;
DE EC=2.3.1.15;
DE Flags: Precursor;
GN Name=GPAT;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 112-134; 310-323 AND
RP 326-345.
RC STRAIN=cv. Little Marvel; TISSUE=Seedling;
RX PubMed=1932680; DOI=10.1007/bf00037145;
RA Weber S., Wolter F.-P., Buck F., Frentzen M., Heinz E.;
RT "Purification and cDNA sequencing of an oleate-selective acyl-ACP:sn-
RT glycerol-3-phosphate acyltransferase from pea chloroplasts.";
RL Plant Mol. Biol. 17:1067-1076(1991).
RN [2]
RP CHARACTERIZATION.
RX PubMed=6825679; DOI=10.1111/j.1432-1033.1983.tb07096.x;
RA Frentzen M., Heinz E., McKeon T.A., Stumpf P.K.;
RT "Specificities and selectivities of glycerol-3-phosphate acyltransferase
RT and monoacylglycerol-3-phosphate acyltransferase from pea and spinach
RT chloroplasts.";
RL Eur. J. Biochem. 129:629-636(1983).
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of
CC glycerol-3-phosphate. The enzyme from chilling-resistant plants
CC discriminates against non-fluid palmitic acid and selects oleic acid
CC whereas the enzyme from sensitive plants accepts both fatty acids. This
CC is an oleate-selective acyltransferase.
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 -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
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:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; X59041; CAA41769.1; -; mRNA.
DR PIR; S18239; S18239.
DR AlphaFoldDB; P30706; -.
DR SMR; P30706; -.
DR PRIDE; P30706; -.
DR KEGG; ag:CAA41769; -.
DR UniPathway; UPA00557; UER00612.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:EnsemblPlants.
DR Gene3D; 1.10.1200.50; -; 1.
DR InterPro; IPR016222; G3P_O-acylTrfase_chlp.
DR InterPro; IPR023083; G3P_O-acylTrfase_N.
DR InterPro; IPR038114; GPAT_N_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR35695; PTHR35695; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF14829; GPAT_N; 1.
DR PIRSF; PIRSF000431; Glycerol-3-P_O-acyltransfrase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Chloroplast; Direct protein sequencing;
KW Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..88
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 89..457
FT /note="Glycerol-3-phosphate acyltransferase, chloroplastic"
FT /id="PRO_0000024698"
FT MOTIF 227..232
FT /note="HXXXXD motif"
SQ SEQUENCE 457 AA; 50760 MW; C50F52102E4C4EB0 CRC64;
MTDSFAHCAS HINYRHKMKT MFIFSTPCCS PSTAFFSPFR ASNSKPLRST LSLRSSISSS
SITSTSHCSL AFNIVKHKEK NVVSANMTSS VSSRTFLNAQ NEQDVLSGIK KEVEAGTLPA
SIAAGMEEVY LNYKSAVIKS GDPKANEIVL SNMTALLDRI FLDVKEPFVF EAHHKAKREP
FDYYMFGQNY IRPLVDFETS YVGNMPLFIQ MEEQLKQGHN IILMSNHQSE ADPAIIALLL
EMRLPHIAEN LIYVAGDRVI TVPLCKPFSI GRNLICVYSK KHMLDNPELV DMKRKANTRS
RKEMAMLLRS GSQIIWIAPS GGRDRPVANS GEWAPAPFDS SSVDNMRRLV DHSGPPGHIY
PLAILCHDIM PPPLKVEKEI GEKRIISYHG TGISTAPEIS FSNTTAACEN PEKAKDAYTK
ALYDSVTEQY DVLKSAIHGK KGLQASTPVV SLSQPWK