ID   PLSB_CUCSA              Reviewed;         470 AA.
AC   Q39639;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase, chloroplastic;
DE            Short=GPAT;
DE            EC=2.3.1.15;
DE   Flags: Precursor;
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16668954; DOI=10.1104/pp.99.2.771;
RA   Johnson T.C., Schneider J.C., Somerville C.;
RT   "Nucleotide sequence of acyl-acyl carrier protein: glycerol-3-phosphate
RT   acyltransferase from cucumber.";
RL   Plant Physiol. 99:771-772(1992).
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; M80571; AAA33122.1; -; mRNA.
DR   PIR; T10193; T10193.
DR   RefSeq; NP_001292631.1; NM_001305702.1.
DR   AlphaFoldDB; Q39639; -.
DR   SMR; Q39639; -.
DR   STRING; 3659.XP_004163205.1; -.
DR   GeneID; 101213494; -.
DR   KEGG; csv:101213494; -.
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   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..101
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           102..470
FT                   /note="Glycerol-3-phosphate acyltransferase, chloroplastic"
FT                   /id="PRO_0000024697"
FT   REGION          87..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           240..245
FT                   /note="HXXXXD motif"
FT   COMPBIAS        88..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  51876 MW;  AF60144E19D2B39B CRC64;
     MFILSAVSSS SSSSSSVPSS LPPFSLSPSI SLSFSRVSLP PSSSSSSSSL KLFLPLSLHF
     TPPKLSSPHS FLRFSASRAM AELIQDKESA HTPSTTDVTR NDPPHSRAFL DLRSEEELLS
     CIRRETEAGK LPSNVAAGME ELYQNYKNAV FESGNPKADE IVLSNMTVAL DRILLDVEDP
     FMFSPHHKAI REPFDYYTFG QNYVRPLIDF ENSFVGNLSL FKDIEEKLHQ GHNVVLISNH
     QTEADPAIIS LLLEKTNPYI AENMIYVAGD RVIADPLCKP FSIGRNLICV YSKKHMLDIP
     ELAETKRKAN TRSLKEMALL LRGGSQLIWI APSGGRDRPD PSTGEWYPAP FDASSVDNMR
     RLLQHSGAPG HLYPLALLCY DIMPPPSQVE IEIGEKRVIS FNGTGLSVGP EISFDEIAAS
     RDNPDEVREA YSKALYDSVA KQYNVLKAAI DGKQELEASV ADVSLSQPWI