ID   PLSB_PHAVU              Reviewed;         461 AA.
AC   Q43822;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase, chloroplastic;
DE            Short=GPAT;
DE            EC=2.3.1.15;
DE   Flags: Precursor;
GN   Name=PLSB;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Annabel; TISSUE=Leaf;
RX   PubMed=7716242; DOI=10.1104/pp.107.3.1039;
RA   Fritz M., Heinz E., Wolter F.P.;
RT   "Cloning and sequencing of a full-length cDNA coding for sn-glycerol-3-
RT   phosphate acyltransferase from Phaseolus vulgaris.";
RL   Plant Physiol. 107:1039-1040(1995).
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.
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   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR   EMBL; X79722; CAA56159.1; -; mRNA.
DR   PIR; T11819; T11819.
DR   AlphaFoldDB; Q43822; -.
DR   SMR; Q43822; -.
DR   STRING; 3885.XP_007158248.1; -.
DR   eggNOG; ENOG502QRHE; Eukaryota.
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   2: Evidence at transcript level;
KW   Acyltransferase; Chloroplast; Lipid biosynthesis; Lipid metabolism;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Plastid; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..96
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           97..461
FT                   /note="Glycerol-3-phosphate acyltransferase, chloroplastic"
FT                   /id="PRO_0000024699"
FT   REGION          47..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           231..236
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   461 AA;  50697 MW;  EAC4FC837908B38A CRC64;
     MSMTGSSAYY VAHAIPPFLR LSNKTMLLLS TPPTTFFPTS TTPRVTLLSS TSSSSSSSIS
     LRSSTAPSPS CSSVTPKDNC LASAKHSPPN MSASVSSRTF LNAQSEQDVF AGIKKEVEAG
     SLPANVAAGM EEVYNNYKKA VIQSGDPKAN EIVLSNMIAL LDRVFLDVTD PFVFQPHHKA
     KREPFDYYVF GQNYIRPLVD FKNAYVGNMP LFIEMEEKLK QGHNIILMSN HQTEADPAII
     SLLLETRLPY IAENLTYVAG DRVITDPLSK PFSIGRNLIC VYSKKHMLDD PALVEMKRTA
     NIRALKEMAM LLRNGSQLVW IAPSGGRDRP DAQTREWVPA PFDISSVDNM RRLVEHSGPP
     GHVYPLAILC HDIMPPPLKV EKEIGEKRII CFHGAGISVA PAISFSETTA TCENPEKAKE
     VFSKALYNSV TEQYNVLKSA IQGKKGFEAS TPVVTLSQPW K