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Database: UniProt
Entry: S9SAG6_9RHOB
LinkDB: S9SAG6_9RHOB
Original site: S9SAG6_9RHOB 
ID   S9SAG6_9RHOB            Unreviewed;       479 AA.
AC   S9SAG6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432};
DE            EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113};
GN   ORFNames=ruthe_02874 {ECO:0000313|EMBL:EPX83249.1};
OS   Rubellimicrobium thermophilum DSM 16684.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX83249.1, ECO:0000313|Proteomes:UP000015346};
RN   [1] {ECO:0000313|EMBL:EPX83249.1, ECO:0000313|Proteomes:UP000015346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX83249.1,
RC   ECO:0000313|Proteomes:UP000015346};
RX   PubMed=24501632; DOI=10.4056/sigs.4247911;
RA   Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT   "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT   type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL   Stand. Genomic Sci. 8:480-490(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00000510};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004765}.
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:EPX83249.1}.
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DR   EMBL; AOLV01000033; EPX83249.1; -; Genomic_DNA.
DR   RefSeq; WP_021098938.1; NZ_KE557324.1.
DR   AlphaFoldDB; S9SAG6; -.
DR   STRING; 1123069.ruthe_02874; -.
DR   PATRIC; fig|1123069.3.peg.2845; -.
DR   HOGENOM; CLU_611008_0_0_5; -.
DR   OrthoDB; 335193at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000015346; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:EPX83249.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPX83249.1}.
FT   DOMAIN          151..274
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   479 AA;  53747 MW;  0E5FAB69A825E7D1 CRC64;
     MTRTVELPLW LLVLILLFAG VTFASHFLVP SVRWFFRRRM ERVVARLNTR LSRPIAPFKL
     ARRHDMIERL VYDPEVVKAV AEDAHARGIP ESVAWEEARR HAREIVPAFS ATLYFGWGAR
     LARWISRGLY RVRLSENDLA AIDALPQDAS VVFVMNHRSN MDYVLVTWLV SERAALSYAV
     GEWARVWPLS SLIRMMGAYF IRRQNRSALY RRVLARYVQM ATDGGVTQAI FPEGRLSLDG
     RMGPPRLGLL SYIAEDGLAR RRDVIFVPVA LNYDRVIEDR FLIRAHVTGI RRFRPTPGEV
     LKGLAAHLWD WLRGRFRGFG TVRASFGPPL SLKAFLAEGP ERPAEALGAE LMARIACAMP
     ALPVPLVARA LLLERDRPLS RERVEARVRA DIAWLAARGG VVPRRGVGLV VGEALSLLAA
     RGILTEDADG RIRLRDGEET LLAYYAGSIA HLFGEEPQTG AQGAAIRAGR PGDPHFTSW
//
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