ID Q9SDN3_PRUDU Unreviewed; 306 AA.
AC Q9SDN3;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 22-FEB-2023, entry version 58.
DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000256|ARBA:ARBA00013211};
DE EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211};
OS Prunus dulcis (Almond) (Amygdalus dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3755 {ECO:0000313|EMBL:AAF20003.1};
RN [1] {ECO:0000313|EMBL:AAF20003.1}
RP NUCLEOTIDE SEQUENCE.
RA Campalans A., Pages M., Messeguer R.;
RT "Identification of differentially expressed genes during dehydration in
RT almond (Prunus amygdalus) using the cDNA-AFLP technique.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004728}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; AF213937; AAF20003.1; -; mRNA.
DR AlphaFoldDB; Q9SDN3; -.
DR UniPathway; UPA00557; UER00613.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR10983:SF24; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 3, ISOFORM E-RELATED; 1.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:AAF20003.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAF20003.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..128
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 280..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 33994 MW; CBD334496E25908D CRC64;
MGKEHALVIS NHRSDIDWLV GWVLAQRSGC LGSSLAVMKK SSKFLPVIGW SMWFSEYLFL
ERSWAKDEGT LKSGVQRLKD FPQPFWLALF VEGTRFTQAK LLAAQEYAAA TGLPVPRNVL
IPRTKGFVTA VSQMRSFAPA IYDVTVAIPK SSPAPTMLRL FEGRPSVVHV HIKRHVMRDL
PETDEAVAQW CKDIFVAKDA LLDKHTVEQT FGDQQLKVTG RPLKSLLVVT AWACLLILGA
LKFLYWSSLL SSWKGIAFSA LGLGVVTVLM QILIRFSQSE RSTPAPVAPT NNKNKGESSG
KPEKQQ
//
