ID A0A078FG84_BRANA Unreviewed; 443 AA.
AC A0A078FG84;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycerol-3-phosphate acyltransferase, chloroplastic {ECO:0000256|PIRNR:PIRNR000431};
DE Short=GPAT {ECO:0000256|PIRNR:PIRNR000431};
DE EC=2.3.1.15 {ECO:0000256|PIRNR:PIRNR000431};
GN Name=BnaA09g24560D {ECO:0000313|EMBL:CDY12256.1};
GN ORFNames=DARMORV10_A09P34000.1 {ECO:0000313|EMBL:CAF2044260.1},
GN GSBRNA2T00061302001 {ECO:0000313|EMBL:CDY12256.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY12256.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY12256.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
RN [2] {ECO:0000313|EMBL:CDY12256.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAF2044260.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope - CEA;
RA William W.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|PIRNR:PIRNR000431}.
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:0000256|PIRNR:PIRNR000431};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|PIRNR:PIRNR000431}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470, ECO:0000256|PIRNR:PIRNR000431}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|PIRNR:PIRNR000431}.
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DR EMBL; HG994363; CAF2044260.1; -; Genomic_DNA.
DR EMBL; LK032019; CDY12256.1; -; Genomic_DNA.
DR STRING; 3708.A0A078FG84; -.
DR PaxDb; 3708-A0A078FG84; -.
DR EnsemblPlants; CDY12256; CDY12256; GSBRNA2T00061302001.
DR Gramene; CDY12256; CDY12256; GSBRNA2T00061302001.
DR OMA; AYSQAMH; -.
DR OrthoDB; 1229at2759; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
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 CDD; cd07985; LPLAT_GPAT; 1.
DR Gene3D; 3.40.1130.10; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR Gene3D; 1.10.1200.50; Glycerol-3-phosphate acyltransferase, alpha helical bundle, N-terminal; 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; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR35695:SF1; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE, CHLOROPLASTIC; 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.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000431};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|PIRNR:PIRNR000431};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR000431};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|PIRNR:PIRNR000431};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000431};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..443
FT /note="Glycerol-3-phosphate acyltransferase, chloroplastic"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040561364"
FT DOMAIN 207..353
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 213..218
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|PIRSR:PIRSR000431-2"
SQ SEQUENCE 443 AA; 48882 MW; 128BCE3D215BC6A3 CRC64;
MTLMPLTFSS SIAVAAAAAA TVTSSPRFSL VSLRGFKKLP LRCALSVRAM SELVQDKESV
VAATTSSFSN TTPTELNHSR TFLDARTEED LISGLRKEIE AGRLPPNVAS GMEELFCNYK
NAVLSSGAPR AAHTVISNMS VAFDRMLLGV EHPFTFNPYH KAIREPFDYY QFVHTYIRPL
IDFKNSYVGN VSLFSELEDK IRQGHNIVLI SNHQSEADPA VISLLLEAQC PYIGENIKCV
AGDRVITDPL CKPFSMGRNL ICVYSKKHMN DDPELVDMKR KANTRSLKEM AKLLRSGSQL
IWIAPSGGRD RPDPSTGEWF PAPFDPSSVD NMRRLVEHSG APGHIYPMSL LCYDIMPPPP
KVEKEIGEKR LVGFHGTGLS IAPEISFSDV TADCNNPNEA KEAYSQAMHK SVNEQYKTLN
SAINHGRGIE ASTSTVSLSQ PWN
//
