PLSB_SPIOL
ID PLSB_SPIOL Reviewed; 472 AA.
AC Q43869;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Glycerol-3-phosphate acyltransferase, chloroplastic;
DE Short=GPAT;
DE EC=2.3.1.15;
DE Flags: Precursor;
GN Name=GAT; Synonyms=ACT1;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Birofure; TISSUE=Seedling;
RA Ishikazi-Nishizawa O., Azuma M., Ohtani T., Murata N., Toguri T.;
RT "Nucleotide sequence of cDNA from Spinacia oleracea encoding plastid
RT glycerol-3-phosphate acyltransferase.";
RL (er) Plant Gene Register PGR95-014(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Melody; TISSUE=Leaf;
RA Wolter F.P.;
RT "Conserved intron position in 3' untranslated region of a cDNA encoding the
RT plastidial sn-glycerol-3-phosphate acyltransferase of spinach.";
RL (er) Plant Gene Register PGR96-118(1996).
RN [3]
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 -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; X77370; CAA54559.1; -; mRNA.
DR EMBL; Z49091; CAA88913.1; -; mRNA.
DR PIR; S51768; S51768.
DR AlphaFoldDB; Q43869; -.
DR SMR; Q43869; -.
DR OrthoDB; 1233168at2759; -.
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 1: Evidence at protein level;
KW Acyltransferase; Chloroplast; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Plastid; Transferase;
KW Transit peptide.
FT TRANSIT 1..102
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 103..472
FT /note="Glycerol-3-phosphate acyltransferase, chloroplastic"
FT /id="PRO_0000024700"
FT MOTIF 241..246
FT /note="HXXXXD motif"
SQ SEQUENCE 472 AA; 52180 MW; A0EE1FED064111CC CRC64;
MLVLSSSAPP VLEVCKDRVS SSFSTSSSSS SSAFSAVVFR RSFFTRFNSS LICCCSSKLK
LMADTALPSS SSSTSASASY SAAAKSVEEE NHEIPVKKED DNQLLRSRTY RNVRSAEELI
SEIKRESEIG RLPKSVAYAM EGLFHYYRNA VLSSGISHAD EIVLSNMSVM LDFVLLDIED
PFVFPPFHKA IREPADYYSF GQDYIRPLVD FGNSYVGNIA IFQEMEEKLK QGDNIILMSN
HQSEADPAVI ALLLEKTNSL IAENLIYIAG DRVITDPLCK PFSMGRNLLC VYSKKHMYDD
PELVDVKKRA NTRSLKELVL LLRGGSKIIW IAPSGGRDRP DAVTGEWYPG TFDFAALDNM
RRLVEHAGRP GHIYPLALLC YDIMPPPAQV EKEIGEKRVM SFHGVGVSVE PEINYNDVSL
GCKNDEEAKS VYGQALYNSV NEQYNVLKAA IHGKQGSGAS TPTTSLSQPW AS