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Database: UniProt
Entry: A0A2T0X8W7_9RHOB
LinkDB: A0A2T0X8W7_9RHOB
Original site: A0A2T0X8W7_9RHOB 
ID   A0A2T0X8W7_9RHOB        Unreviewed;       220 AA.
AC   A0A2T0X8W7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Acyltransferase-like protein {ECO:0000313|EMBL:PRY95355.1};
GN   ORFNames=BCF33_0973 {ECO:0000313|EMBL:PRY95355.1};
OS   Hasllibacter halocynthiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Hasllibacter.
OX   NCBI_TaxID=595589 {ECO:0000313|EMBL:PRY95355.1, ECO:0000313|Proteomes:UP000238801};
RN   [1] {ECO:0000313|EMBL:PRY95355.1, ECO:0000313|Proteomes:UP000238801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29318 {ECO:0000313|EMBL:PRY95355.1,
RC   ECO:0000313|Proteomes:UP000238801};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-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   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:PRY95355.1}.
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DR   EMBL; PVTT01000001; PRY95355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0X8W7; -.
DR   Proteomes; UP000238801; 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:PRY95355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238801};
KW   Transferase {ECO:0000313|EMBL:PRY95355.1}.
FT   DOMAIN          44..168
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   220 AA;  24467 MW;  20754BDBA41DA0D0 CRC64;
     MRRAAGVLRD LAAFLAGRAI ALVMRLFAAP RTVWVQGGPL ARQRIYFANH TSNADLPLIW
     TVLPPDLRVR TRPVAAADYW LKGPVRAFFG RDVFGAVLVE RRPEARGEGE DPMATIRAAL
     DRGDSLIIFP EGRRNETVKK LLPLKAGLFN MALSHPEVEL VPVWIENLNK MMPRGEVVPI
     PLISTIAFGR PMQRAEGEGK DDFLARAREA LLALRERATS
//
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