ID   PLSB_PSEE4              Reviewed;         828 AA.
AC   Q1I610;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=PSEEN4236;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK16925.1; -; Genomic_DNA.
DR   RefSeq; WP_011535296.1; NC_008027.1.
DR   AlphaFoldDB; Q1I610; -.
DR   STRING; 384676.PSEEN4236; -.
DR   EnsemblBacteria; CAK16925; CAK16925; PSEEN4236.
DR   KEGG; pen:PSEEN4236; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000658; 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_1000049444"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   828 AA;  94000 MW;  FC1A95361CE8CB31 CRC64;
     MTRSPLRRLI FGALRRVLYL WVRSETINQS SLTLKLDRSR PVFYALSSPS LTDLAVVDHE
     CTKAGLPRPV LPVAVGPLQE PAGFFYLTPD PDWLGRQDKR GAPPTLERLV AAISQHAEED
     TQIIPVSVFW GQTPASESSP WKLLFADSWA VTGRLRRLLS VLILGRKTRV QFSAPIHLRE
     LVDHNKGHER TVRMAQRVMR VHFRNLKTAV IGPDISHRRN LVKGLVHDPL VRQAISDEAE
     REKIPYAKAE AKALHYGNEI ASDYTYTAIR FLEVVLSWFW NKIYDGVKVN HIEQVQGIAP
     GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVIGGLLRR GGAFFMRRTF
     KGNPLYTAVF NEYLHTLFTK GFPVEYFVEG GRSRTGRMLQ PRTGMLAITL RSFLRSSRTP
     IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESIFDIFKVI GALKQRFGQV YVNFGEPIRL
     AGFLDEQQPG WREQELGPQF RPTWLNETTT RLGETVARHL NEAAAINPVN LVALALLSTS
     RLALDERALT RVLDLYLALL RQVPYSPHTT LPEGDGQALI KHVLGMDLLA EQKDAMGRIL
     YLDEANAVLM TYYRNNVLHI FALPGLLASF FLSSSRMSRD LLGQYVRALY PYLQAELFLR
     WTPEQLDEVI DQWLAALVSQ GLLRQENDIY MRPAPSSRQF VLLTLLARTI TQTLQRFYMA
     TSLLLNSGQH TLSAEELEEL CVMMAQRLSI LHGLNAPEFF DKTLFRHFIQ TLVREGVLQP
     DGDGKLGYHD KLAELAEGVA KRVLSAELRL SIRQVALHRD EPQENPET