ID   PLSB_PSEPG              Reviewed;         828 AA.
AC   B0KS79;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00393};
DE            Short=GPAT {ECO:0000255|HAMAP-Rule:MF_00393};
DE            EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_00393};
GN   Name=plsB {ECO:0000255|HAMAP-Rule:MF_00393};
GN   OrderedLocusNames=PputGB1_1126;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00393};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00393}.
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DR   EMBL; CP000926; ABY97034.1; -; Genomic_DNA.
DR   RefSeq; WP_012270815.1; NC_010322.1.
DR   AlphaFoldDB; B0KS79; -.
DR   STRING; 76869.PputGB1_1126; -.
DR   EnsemblBacteria; ABY97034; ABY97034; PputGB1_1126.
DR   KEGG; ppg:PputGB1_1126; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002157; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
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   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR045520; GPAT_C.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; PTHR12563; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   PIRSF; PIRSF500064; GPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR03703; plsB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..828
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000080288"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   828 AA;  93622 MW;  450923A7373B3BB4 CRC64;
     MTRSPLHRLI FGGLRRLLYL WVRSETINQS SMTLNLDRSR PVFYALPSPS LTDLAVLDHE
     CTKAGLPRPV LPVAVGPLQE PAAFFYLTPD PDWLGRQDKS GAPPTLERLV AAVSQHAEED
     AQIIPVSVFW GQTPASESSP WKLLFADSWA VTGRLRRLLT VLILGRKTRV QFSAPIHLRE
     LVQHNKGHAR TVRMAQRLMR VHFRNLKTAV IGPDISHRRN LVKGLVHAPL VRQAIADEAQ
     RENLPLAKAE AQALRYGNEI ASDYTYTVIR FLEVVLSWFW NKIYDGIKVN HIEQVQGIAP
     GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHVAAGINLN MPVVGNLLRR GGAFFMRRTF
     KGNPLYTAVF NEYLHTLYTK GFPVEYFVEG GRSRTGRMLQ PRTGMLAITL RSFLRSSRTP
     IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESVLDIFKVF GALKQRFGQV YVNFGEPIRL
     AGFLDQQQPG WREQDHGPQY RPDWLNATTT RLGETVARHL NEAAAINPVN LVALALLSTS
     RLALDERALT RVLDLYLALL RQVPYSPHTT LPDGDGQALI EHVRSMNLVA EQKDALGRIL
     FLDEGNAVLM TYYRNNVLHI FALPALLASF FLSSSRMSRE LLGQYVHALY PYLQAELFLR
     WAPEQLDEVI DQWLAALVEQ GLLRQENDVY VRPAPSSRQF VLLTLLARTI TQTLQRFYMA
     TSLLINSGQN SLSAEALEDL CVMMAQRLSI LHGLNAPEFF DKTLFRHFIQ TLLQQGVLHT
     DTQGKLGYHD KLGELAEGVA KRVLSAELRL SIRQVALHRD DGLESSTI