ID   PLSB_PSEP1              Reviewed;         828 AA.
AC   A5W867;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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}; OrderedLocusNames=Pput_4203;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) 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; CP000712; ABQ80327.1; -; Genomic_DNA.
DR   RefSeq; WP_012053555.1; NC_009512.1.
DR   AlphaFoldDB; A5W867; -.
DR   STRING; 351746.Pput_4203; -.
DR   EnsemblBacteria; ABQ80327; ABQ80327; Pput_4203.
DR   KEGG; ppf:Pput_4203; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
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_1000049448"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   828 AA;  93590 MW;  0416D77634A197B9 CRC64;
     MTRSPLHRLI FGGLRRLLYL WVRSETINQS SMTLNLDRSR PVFYALPSPA LTDLAVLDHE
     CTKAGLPRPV LPVAVGPLQE PAAFFYLTPD PDWLGRQDKS GAPPTLERLV AAVSQHAEED
     AQIIPVSVFW GQTPASESSP WKLLFADSWA VTGRLRRLLT VLILGRKTRV QFSAPIHLRE
     LVQHNKGHER TVRMAQRLMR VHFRNLKAAV IGPDISHRRT LVKGLVHAPQ VRQAIADEAQ
     RENLPLAKAE AQALRYGNEI ASDYTYTAIR FLEVVLSWFW NKIYDGIKVN HIEQVQGIAP
     GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHVAAGINLN MPVVGNLLRR GGAFFMRRTF
     KGNPLYTAVF NEYLHTLYTK GFPVEYFVEG GRSRTGRMLQ PRTGMLAITL RSFLRSSRTP
     IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESVLDIFKVF GALKQRFGQV YVNFGEPIRL
     AGFLDQQQPG WREQDHGPQY RPDWLNAATA RLGETVARHL NEAAAINPVN LVALALLSTS
     RLALDERALT RVLDLYLALL RQVPYSPHTT LPEGDGQALI EHVRSMNLVA EQKDALGRIL
     YLDEGNAVLM TYYRNNVLHI FALPALLASF FLSSSRMSRE LLGQYVHALY PYLQAELFLR
     WTPEQLDEVI DQWLVALVEQ GLLRQDNDLY VRPAPSSRQF VLLTLLARTI TQTLQRFYMA
     TSLLINSGQN SLSAEALEDL CVMMAQRLSI LHGLNAPEFF DKTLFRHFIQ TLLQQGVLHA
     DAQGKLGYHD KLGELAEGVA KRVLSAELRL SIRQVALHRD DGLETSTL