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Database: UniProt
Entry: A0A0M5LRK7_9PSEU
LinkDB: A0A0M5LRK7_9PSEU
Original site: A0A0M5LRK7_9PSEU 
ID   A0A0M5LRK7_9PSEU        Unreviewed;       225 AA.
AC   A0A0M5LRK7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-phosphate glycerol 3-phosphate acyltransferase {ECO:0000313|EMBL:ALE79620.1};
GN   ORFNames=WY02_15570 {ECO:0000313|EMBL:ALE79620.1};
OS   Pseudonocardia sp. AL041005-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE79620.1, ECO:0000313|Proteomes:UP000067245};
RN   [1] {ECO:0000313|EMBL:ALE79620.1, ECO:0000313|Proteomes:UP000067245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE79620.1,
RC   ECO:0000313|Proteomes:UP000067245};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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; CP011862; ALE79620.1; -; Genomic_DNA.
DR   RefSeq; WP_062398772.1; NZ_CP011862.1.
DR   AlphaFoldDB; A0A0M5LRK7; -.
DR   STRING; 445576.WY02_15570; -.
DR   KEGG; psea:WY02_15570; -.
DR   PATRIC; fig|445576.3.peg.3419; -.
DR   OrthoDB; 9808424at2; -.
DR   Proteomes; UP000067245; 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:ALE79620.1};
KW   Transferase {ECO:0000313|EMBL:ALE79620.1}.
FT   DOMAIN          33..152
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   225 AA;  24177 MW;  EF622AE20046C1C9 CRC64;
     MQLFIRYVLA PLVRLVWRPR VRGADRIPAT GPVILAANHR AAVDTAFIPL VAPRKVAFLG
     KAEYFTGRGL RGRLMAAFLG ALGYIPVDRS NARAGLAALA AGRKVLDRGG AFGIYPEGTR
     SLDGKLHRGH TGVASLALST GAVVVPVGLI GTERVQPIGR LFPRLARVEI RFGRPLEFSR
     YEGLEGAPAI RRAVTDEIMD AIADLSGQTY VDSYHRRPDD SAAAA
//
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