ID A0A1G8SNB0_9PSED Unreviewed; 269 AA.
AC A0A1G8SNB0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferases {ECO:0000313|EMBL:SDJ30653.1};
GN ORFNames=SAMN05216186_101116 {ECO:0000313|EMBL:SDJ30653.1};
OS Pseudomonas indica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=137658 {ECO:0000313|EMBL:SDJ30653.1, ECO:0000313|Proteomes:UP000198706};
RN [1] {ECO:0000313|EMBL:SDJ30653.1, ECO:0000313|Proteomes:UP000198706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21544 {ECO:0000313|EMBL:SDJ30653.1,
RC ECO:0000313|Proteomes:UP000198706};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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DR EMBL; FNFD01000001; SDJ30653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8SNB0; -.
DR STRING; 137658.SAMN05216186_101116; -.
DR OrthoDB; 9812274at2; -.
DR Proteomes; UP000198706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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:SDJ30653.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198706};
KW Transferase {ECO:0000313|EMBL:SDJ30653.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..203
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 269 AA; 29977 MW; E7B510CA6CE5CBAD CRC64;
MELATQPLKP RANAPYLWRL IATGLSFALF GIGGLCLRVL VFPLLALLPG DTLTHRRRAR
ATVSRLFWLF VQFMYRSGVL TYEVEGVERL GRPGQMIIAN HPSLIDVVVL IAFIRDANCV
VKQSLWDNPC MRGPIRAAQY ISNSGSMDML DEAADALREG QTLIVFPEGT RTTPGKAPEF
HRGAAAIALR GARLVTPVVI SVEPTTLTKA EPWYRIPSRR FHFRLRVGED IDPQAFAAQG
SAPIASRKLN DYLHQHFMKE LALDERTGT
//
