ID A0A0J0YJA9_9ACTN Unreviewed; 251 AA.
AC A0A0J0YJA9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:KLR61058.1};
DE EC=2.3.1.51 {ECO:0000313|EMBL:KLR61058.1};
GN ORFNames=IMCC26207_109576 {ECO:0000313|EMBL:KLR61058.1};
OS Actinobacteria bacterium IMCC26207.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1641811 {ECO:0000313|EMBL:KLR61058.1, ECO:0000313|Proteomes:UP000036180};
RN [1] {ECO:0000313|EMBL:KLR61058.1, ECO:0000313|Proteomes:UP000036180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26207 {ECO:0000313|EMBL:KLR61058.1,
RC ECO:0000313|Proteomes:UP000036180};
RA Kim S., Cho J.-C.;
RT "Genome sequence of freshwater Actinobacteria.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLR61058.1}.
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DR EMBL; LCZK01000009; KLR61058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J0YJA9; -.
DR STRING; 1641811.IMCC26207_109576; -.
DR PATRIC; fig|1641811.3.peg.2201; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000036180; Unassembled WGS sequence.
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 CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:KLR61058.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000036180};
KW Transferase {ECO:0000313|EMBL:KLR61058.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..192
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 251 AA; 28530 MW; FD56610AC4E7922D CRC64;
MKNLSLTLWS IWSWFVFGLG IALLLPTMAV VWLVTAPFDP SRYWTGFLFR KITVVHQKLN
PLWTFRLGGE YPANPRNPYV VVSNHESFVD ILLISNLPWE MKWLSKKENF KIPVAGWLMK
MAKDIELDRK DPKSAAEAMR QCALRLDDHV SVMIFPEGTR STTGDLLPFK DGAFRLAIES
GVPILPIAVF GTSTALRPHD WRFGKSVAQL RVLEPISTEG LGVDDVADLR EQTRSRIITE
LKDMGRDFGE N
//
