ID A0PTL7_MYCUA Unreviewed; 243 AA.
AC A0PTL7;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:ABL05686.1};
GN OrderedLocusNames=MUL_3537 {ECO:0000313|EMBL:ABL05686.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL05686.1, ECO:0000313|Proteomes:UP000000765};
RN [1] {ECO:0000313|EMBL:ABL05686.1, ECO:0000313|Proteomes:UP000000765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL05686.1,
RC ECO:0000313|Proteomes:UP000000765};
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL05686.1; -; Genomic_DNA.
DR RefSeq; WP_011741292.1; NC_008611.1.
DR AlphaFoldDB; A0PTL7; -.
DR GeneID; 72433205; -.
DR KEGG; mul:MUL_3537; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_0_11; -.
DR Proteomes; UP000000765; 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:ABL05686.1};
KW Transferase {ECO:0000313|EMBL:ABL05686.1}.
FT DOMAIN 35..154
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 224..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 26639 MW; A21DA2508FFC5735 CRC64;
MWYYLFKYIF MGWLFTLLGR PKVEGLEHIP SSGPAILASN HLAVADSFYL PLVVRRRITF
LAKAEYFTGT GVKGWINRWF YSVSGQVPID RTNSDAAQAA LETAAGLLRQ GKLLGMYPEG
TRSPDGRLYK GKTGLARLAL HTGVPVIPVA MIGTNVVNPP GRKMLRFGRV IVRFGKPMDF
SRFEGLAGNH FIERAVTDEV MYELMGLSGQ EYVDIYAASI KNGGKGDDDG SGDAVRIPET
AAG
//
