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Database: UniProt
Entry: A0A1F8SZP9_9CHLR
LinkDB: A0A1F8SZP9_9CHLR
Original site: A0A1F8SZP9_9CHLR 
ID   A0A1F8SZP9_9CHLR        Unreviewed;       241 AA.
AC   A0A1F8SZP9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=A2Z45_05135 {ECO:0000313|EMBL:OGO65041.1};
OS   Chloroflexi bacterium RBG_19FT_COMBO_55_16.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797669 {ECO:0000313|EMBL:OGO65041.1, ECO:0000313|Proteomes:UP000177674};
RN   [1] {ECO:0000313|EMBL:OGO65041.1, ECO:0000313|Proteomes:UP000177674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO65041.1}.
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DR   EMBL; MGOK01000063; OGO65041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8SZP9; -.
DR   STRING; 1797669.A2Z45_05135; -.
DR   Proteomes; UP000177674; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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;
FT   DOMAIN          49..161
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   241 AA;  27213 MW;  825DD5BE30742723 CRC64;
     MTESFKDYQV SRSAIIFRKL FRPVFRGIFH LLSRVRIYGL ENVPARGAYL IAINHISIFE
     PPFILAFWPL APEAVGAVEI WERRGQSTLV RLYGGIPVHR GEYDRRIIDT MVSVLHSGHP
     LLIAPEGGRS HTPGMRAALP GVAYIIHRSK VPVIPVGIVG TTEDFLKRAL RGERRTLEMR
     IGGPLWLPEV AGRGKERRIA FQRNTDLIMH HIASLLPSEY RGVYAVSNID SIQAQERSYS
     I
//
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