ID G8MZP6_GEOTH Unreviewed; 197 AA.
AC G8MZP6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:AEV19817.1};
GN ORFNames=GTCCBUS3UF5_25140 {ECO:0000313|EMBL:AEV19817.1};
OS Geobacillus thermoleovorans CCB_US3_UF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV19817.1, ECO:0000313|Proteomes:UP000005636};
RN [1] {ECO:0000313|EMBL:AEV19817.1, ECO:0000313|Proteomes:UP000005636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV19817.1,
RC ECO:0000313|Proteomes:UP000005636};
RA Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT CCB_US3_UF5.";
RL Submitted (NOV-2011) 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};
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DR EMBL; CP003125; AEV19817.1; -; Genomic_DNA.
DR RefSeq; WP_014196210.1; NC_016593.1.
DR AlphaFoldDB; G8MZP6; -.
DR KEGG; gte:GTCCBUS3UF5_25140; -.
DR PATRIC; fig|1111068.3.peg.2426; -.
DR HOGENOM; CLU_027938_4_5_9; -.
DR Proteomes; UP000005636; Chromosome.
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:AEV19817.1};
KW Transferase {ECO:0000313|EMBL:AEV19817.1}.
FT DOMAIN 37..149
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 197 AA; 21762 MW; 07178B13B4DD411D CRC64;
MTVDFYSFAK GIVKGVLTPF YRIQTIGIEQ FPKEGGVLLC ANHISNLDPP VIGITAPRPI
RFMAKEELFR APVVKTLVKS LHAFPVKRGM NDRQALRTGL EVLKQGEVLG IFPEGTRSKD
GRLKKALPGV GFFALRTDAA VVPCAIVGPY RPFAPLKVVY GAPVDMAPLR ARKASPEEAA
DYIMDHIRRL LEEHQRA
//
