ID   PLSB_PSEMY              Reviewed;         827 AA.
AC   A4XWX9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=Pmen_3091;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
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., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-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; CP000680; ABP85845.1; -; Genomic_DNA.
DR   RefSeq; WP_012019215.1; NC_009439.1.
DR   AlphaFoldDB; A4XWX9; -.
DR   STRING; 399739.Pmen_3091; -.
DR   PRIDE; A4XWX9; -.
DR   EnsemblBacteria; ABP85845; ABP85845; Pmen_3091.
DR   KEGG; pmy:Pmen_3091; -.
DR   PATRIC; fig|399739.8.peg.3131; -.
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..827
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049447"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   827 AA;  93815 MW;  3512E74B4FA3A49D CRC64;
     MTRSPLRRLA FGALRRLLYL WVRSETINQS AFTLKLDRSK PVFYVLQQPS VSDLAVVDRE
     CTKAGLPRPV LPVAVGEHIE PAAFFYLTPE PDWFGRQDKR GISPTLDRVV TALGQHAVDD
     AQIVPVSVFW GQSPDRETSA WKLLFADSWA VTGRLRRLVS ILILGRKTRV QFSTPIHLRE
     LVEQDKGQER TLRMVHRILR VHFRNQKAAV IGPDVSHRRN LVKGLVHDPL VRQAIAEEAE
     REKISLEKAE AQALRYGNEI ASDYTYTVIR FLELVLSWFW NKIYDGIKVH NVEGVRDIAQ
     GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVIGGLLRR GGAFFMRRTF
     KGNPLYTAVF NEYLHTLFSK GFPVEYFVEG GRSRTGRMLR PKTGMLAITL RSFLRSHRLP
     IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESIFDLFKVL GALKQRFGQV SVNFGEPIKL
     AEFLDQQQPG WRQQELGPQY RPAWLNDTTN RLGERVARHL NEAASINPVN LVALALLSTS
     KLALDDRALA RVLDLYLALL RAVPYSPHTT LPDGDGAALI EHVKGMDLLA EQKDALGKIL
     YLDEQNAVLM TYYRNNVLHI FALPALLASF FQSSARISRE QILRFTKALY PYLQAELFIR
     WEIEQLDDVV DQWLAAFVEQ GLLKVEGDVY VRPAPSSRQF VLLTLLSRSV AQTLQRFYMA
     IALLLNAGQN AISAEELEDL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ SLLDQGVLRQ
     DEAGKLSHHP LLSELAEGAA KRVLPAEIRL SIRQVALDRN EDEPAAP