ID A0A291IRU6_9MOLU Unreviewed; 299 AA.
AC A0A291IRU6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:ATG97474.1};
GN ORFNames=CP520_01750 {ECO:0000313|EMBL:ATG97474.1}, LD118_00408
GN {ECO:0000313|EMBL:MCL8216819.1};
OS Mesoplasma lactucae ATCC 49193.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Entomoplasmataceae; Mesoplasma.
OX NCBI_TaxID=81460 {ECO:0000313|EMBL:ATG97474.1, ECO:0000313|Proteomes:UP000232227};
RN [1] {ECO:0000313|EMBL:ATG97474.1, ECO:0000313|Proteomes:UP000232227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=831-C4 {ECO:0000313|EMBL:ATG97474.1,
RC ECO:0000313|Proteomes:UP000232227};
RA Knight T.F., Rubinstein R., Citino T.;
RT "SPAdes assembly of the Mesoplasma lactucae genome.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MCL8216819.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 49193 {ECO:0000313|EMBL:MCL8216819.1};
RA Green E.A., Klassen J.;
RT "Mollicute symbiont genomes associated with the fungus-growing ant,
RT Trachymyrmex septentrionalis.";
RL Submitted (FEB-2022) 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; CP023668; ATG97474.1; -; Genomic_DNA.
DR EMBL; JAKNSY010000002; MCL8216819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291IRU6; -.
DR KEGG; mlac:CP520_01750; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000232227; Chromosome.
DR Proteomes; UP001139645; Unassembled WGS sequence.
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:ATG97474.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000232227};
KW Transferase {ECO:0000313|EMBL:ATG97474.1}.
FT DOMAIN 85..204
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 264..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 34632 MW; DDCBA2728264040A CRC64;
MSKKQKEQPK EKFFVDKGKM VYDWPSALHT YKKAKKINKK NKKDPLAYSE QYRYDWLSKR
VQKAMPLFDV DIQVQGIENW LDKGVVLMPN HESNFDVIAL LAINDFQRQQ PLAFIAKKEL
WNDKKASRFL NLIDSVPLDR NSPRSALQAF KESKDLIVDF KRSMVLFPTG TRSYSNEIGE
IQPASMKLAK MANAPIIPVT FIDSYKVFAP NRKHGRVTVK VIFGKPIQGN KLLASSTTDL
ANLVQKEIEK NRDEYMDKEL TPLKELRMTP KQKAKFEKKQ AKKTNKKSKG FKDLFKVID
//
