ID A0A183DNW0_9BILA Unreviewed; 378 AA.
AC A0A183DNW0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001041401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0001041401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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|RuleBase:RU361267};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004728}.
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:0000256|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC ECO:0000256|RuleBase:RU361267}.
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DR WBParaSite; GPUH_0001041401-mRNA-1; GPUH_0001041401-mRNA-1; GPUH_0001041401.
DR Proteomes; UP000050760; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF11; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Transferase {ECO:0000256|RuleBase:RU361267};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..318
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 378 AA; 42378 MW; 3B6A02D689FDA6C3 CRC64;
LNMESAAAAA DAPHSSCIVC QLSICVSLLI ILLYLLSLNS RCLYFIKMTG IYLTIIINAV
IVCCCWPLYF FGDVSFFXXX XCFLQVPRVG KQGICCGRLN MESAGADASH SSCIICQLSI
CVSLLIILLY LLSLNSRCLY FIKMTGIYLT IIINAVIVCC CWPLYFFGDV SKFIFDSYRV
LTAWTGVDVI VRNADILRRQ GPFVFVCNHQ SSLDIVVLSH FWPPRCTVMM KQSLKYIPFF
NFASFLSRAV FVDRFNREKA MKSLEECAKK ITSQKLSVLI FPEGTRNHGD GMLEFKKGAF
NVAVFAQIPI IPIVISSYKP FYSKESRCFA DSGYVVVEVM EPIQTTGVSY LRNPPVHFDA
VAIALIVYSF SSLIFTTS
//
