ID A0A3D8YZ63_9BACL Unreviewed; 193 AA.
AC A0A3D8YZ63;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:REB09886.1};
GN ORFNames=DVB69_03495 {ECO:0000313|EMBL:REB09886.1};
OS Sporosarcina sp. BI001-red.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=2282866 {ECO:0000313|EMBL:REB09886.1, ECO:0000313|Proteomes:UP000256461};
RN [1] {ECO:0000313|EMBL:REB09886.1, ECO:0000313|Proteomes:UP000256461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI001-red {ECO:0000313|EMBL:REB09886.1,
RC ECO:0000313|Proteomes:UP000256461};
RA Rajandas H., Sivachandran P., Mai C.W., Cheong K.W., Teh C.S.J.,
RA Lim E.S.H., Yap I.K.S., Convey P., Chong C.W.;
RT "Draft Genome of Sporosarcina subantarcticus.";
RL Submitted (JUL-2018) 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:REB09886.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QQAK01000009; REB09886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8YZ63; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000256461; 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:REB09886.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000256461};
KW Transferase {ECO:0000313|EMBL:REB09886.1}.
FT DOMAIN 35..147
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 193 AA; 21364 MW; D103F762C7656C99 CRC64;
MNLYPLGKAL CTVVLKPFYR IKVLGLENFP KDKGVLLCTN HIDNLDPPVV GLTAPRPVHF
MAKEELFQLP ILKSVLPNVN AFPVKRGLSD RQAIRKALEL LRSGQVVGMF PEGTRSKTGE
LGKGLTGAGF FALKGDAYVM PCAIIGSYRP FKQLRVIYGE PIDMTPLRER KASAEEATEV
IMSAIQQLLE KNR
//
