GPAT1_CUCMO
ID GPAT1_CUCMO Reviewed; 447 AA.
AC Q9FEQ0;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Glycerol-3-phosphate acyltransferase ATS11, chloroplastic {ECO:0000305};
DE Short=G3PAT {ECO:0000305};
DE Short=GPAT {ECO:0000303|PubMed:11134424};
DE EC=2.3.1.15 {ECO:0000305};
DE EC=2.3.1.n5 {ECO:0000269|Ref.2};
DE Flags: Precursor;
GN Name=ATS1;1 {ECO:0000303|PubMed:11134424}; Synonyms=AT1 {ECO:0000305};
OS Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var.
OS moschata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3662;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=11134424; DOI=10.1093/pcp/pcd072;
RA Nishida I., Sugiura M., Enju A., Nakamura M.;
RT "A second gene for acyl-(acyl-carrier-protein): glycerol-3-phosphate
RT acyltransferase in squash, Cucurbita moschata cv. Shirogikuza(*), codes for
RT an oleate-selective isozyme: molecular cloning and protein purification
RT studies.";
RL Plant Cell Physiol. 41:1381-1391(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RA Frentzen M., Nishida I., Murata N.;
RT "Properties of the plastidial acyl-(acyl-carrier-protein): glycerol-3-
RT phosphate acyltransferase from the chilling-sensitive plant squash
RT (Cucurbita moschata).";
RL Plant Cell Physiol. 28:1195-1201(1987).
CC -!- FUNCTION: Esterifies the acyl-group from acyl-acyl carrier proteins
CC (acyl-ACPs) to the sn-1 position of glycerol-3-phosphate (Ref.2). The
CC physiological acyl donors in chloroplasts are acyl-ACPs, but acyl-CoAs
CC are used as artificial donor for in vitro reactions (Probable). The
CC enzyme from chilling-resistant plants discriminates against non-fluid
CC palmitic acid and selects oleic acid whereas the enzyme from sensitive
CC plants accepts both fatty acids (Ref.2). Squash is chilling-sensitive
CC (Probable). Preferably utilizes oleoyl groups (18:1-ACP) and has lower
CC affinity to palmitoyl (16:0-ACP) and stearoyl groups (18:0-ACP)
CC (Ref.2). {ECO:0000269|Ref.2, ECO:0000305, ECO:0000305|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42300, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n5; Evidence={ECO:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42301;
CC Evidence={ECO:0000305};
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 Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000305}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; AB042400; BAB17754.1; -; mRNA.
DR EMBL; AB049134; BAB39688.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9FEQ0; -.
DR SMR; Q9FEQ0; -.
DR BRENDA; 2.3.1.15; 1739.
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; Direct protein sequencing;
KW Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..447
FT /note="Glycerol-3-phosphate acyltransferase ATS11,
FT chloroplastic"
FT /id="PRO_0000447695"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 217..222
FT /note="HXXXXD motif"
SQ SEQUENCE 447 AA; 49288 MW; 4C42F92C6B2C801E CRC64;
MFILSSSSSL PSPLSLSSSR VSLPPPSSSS LNLLPLSPHF QPPNLACSCS VASRSTAELL
HDFKHSAHTA ASADEARNHL PHSRAFLDVR SEQELLSYIR REAEAGKLPS NVAAGMEELY
QNYKNAVLKS GNPKADEIVL SNMTVALDRI LLDVEEPFVF SPHHKAVREP FDYYTFGQNY
VRPLIDFGNS FVGNPFLFKD IEEKLHQGHN VVLISNHQTE ADPAIISLLL EKTSPYIAEN
MIYVAGDRVI VDPLCKPFSI GRNLICVYSK KHMFDIPELA ETKRKANTRS LKEMALLLRG
GSQLIWIAPS GGRDRLDPSS GEWLPAPFDA SSMDNMRRLI QHSGVPGHLC PLALLCYDIM
PPPSKVEIEI GEKRVISFNG VGLSLAPAIS FEAIAATHRN PDEAREAYSK ALFDSVSMQY
NVLKAAIYGR QALRASTADV SLSQPWI
