ID   PLSB_CARTI              Reviewed;         463 AA.
AC   Q42713;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase, chloroplastic;
DE            Short=GPAT;
DE            EC=2.3.1.15;
DE   Flags: Precursor;
OS   Carthamus tinctorius (Safflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Centaureinae; Carthamus.
OX   NCBI_TaxID=4222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cotyledon;
RX   PubMed=7846182; DOI=10.1104/pp.106.4.1713;
RA   Bhella R.S., Mackenzie S.L.;
RT   "Nucleotide sequence of a cDNA from Carthamus tinctorius encoding a
RT   glycerol-3-phosphate acyl transferase.";
RL   Plant Physiol. 106:1713-1714(1994).
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; L33841; AAA74319.1; -; mRNA.
DR   AlphaFoldDB; Q42713; -.
DR   SMR; Q42713; -.
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   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..91
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           92..463
FT                   /note="Glycerol-3-phosphate acyltransferase, chloroplastic"
FT                   /id="PRO_0000024695"
FT   REGION          18..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           229..234
FT                   /note="HXXXXD motif"
FT   COMPBIAS        70..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  50835 MW;  5792E933068A534D CRC64;
     MSIFFSPSSP TLFFSTTNAN PRVSPSSSPS SAFTPPLSSS RLRPILRGFP CLAFSAPANA
     AHGTAETVHG NKWPSPSSSS SAATQPSAGS DHGHSRTFID ARSEQDLLSG IQRELEAGTL
     PKHIAQAMEE LYQNYKNAVL QSAAPHAEDI VLSNMRVAFD RMFLDVKEPF EFSPYHEAIL
     EPFNYYMFGQ NYIRPLVNFR ESYVGNVSVF GVMEEQLKQG DKVVLISNHQ TEADPAVIAL
     MLETTNPHIS ENIIYVAGDR VITDPLCKPF SMGRNLLCVY SKKHMNDVPE LAEMKKRSNT
     RSLKGRMALL LRGGSKIIWI APSGGRDRPD PITNQWFPAP FDATSLDNMR RLVDHAGLVG
     HIYPLAILCH DIMPPPLQVE KEIGEKSWIS FHGTGISVAP EINFQEVTAS CGSPEEAKAA
     YSQALYDSVC EQYKVLHSAV HGGKGLEAST PSVSLSQPLQ FLD