ID D7KHH3_ARALL Unreviewed; 459 AA.
AC D7KHH3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 ORFNames=ARALYDRAFT_473408 {ECO:0000313|EMBL:EFH69970.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348713; EFH69970.1; -; Genomic_DNA.
DR RefSeq; XP_002893711.1; XM_002893665.1.
DR AlphaFoldDB; D7KHH3; -.
DR STRING; 81972.D7KHH3; -.
DR EnsemblPlants; fgenesh2_kg.1__3362__AT1G32200.1; fgenesh2_kg.1__3362__AT1G32200.1; fgenesh2_kg.1__3362__AT1G32200.1.
DR Gramene; fgenesh2_kg.1__3362__AT1G32200.1; fgenesh2_kg.1__3362__AT1G32200.1; fgenesh2_kg.1__3362__AT1G32200.1.
DR eggNOG; ENOG502QRHE; Eukaryota.
DR HOGENOM; CLU_043091_1_0_1; -.
DR OrthoDB; 1229at2759; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000008694; 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 GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:EnsemblPlants.
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:UP000008694};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..459
FT /note="Glycerol-3-phosphate acyltransferase, chloroplastic"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003101436"
FT DOMAIN 223..369
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 229..234
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|PIRSR:PIRSR000431-2"
SQ SEQUENCE 459 AA; 50482 MW; 9F41B6CECD0D18C8 CRC64;
MTLTFSSSAA TVAVAAATVT SSARVPVYPL ASSTLRGFVS FRLTAKKLFL PPLRSRGGVS
VRAMSELVQD KESSVSASIA LNETAGETPS ELNHSRTFLD ARSEQDLLSG IKKEAEAGRL
PANVASGMEE LYWNYKNAVL SSGASRADET VISNMSVAFD RMLLGVEDPY TFNPYHKAVR
EPFDYYMFVH TYIRPLIDFK NSYVGNASIF SELEDKIRQG HNIVLISNHQ SEADPAVISL
LLEAQSPFIG ENIKCVAGDR VITDPLCKPF SMGRNLICVY SKKHMNDDPE LVDMKRKANT
RSLKEMATML RSGGQLIWIA PSGGRDRPNP STGEWFPAPF DSSSVDNMRR LVEHSGAPGH
IYPMSLLCYD IMPPPPQVEK EIGEKRLVGF HGTGLSIAPE INFSDVTADC ENPNEAKEAY
SQALYKSVNE QYEILNSAIK HRRGVEASTS AVSLSQPWN
//