ID   PLSB_HAMD5              Reviewed;         816 AA.
AC   C4K8M7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=HDEF_0089;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00393};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00393};
CC       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; CP001277; ACQ66864.1; -; Genomic_DNA.
DR   RefSeq; WP_012737829.1; NC_012751.1.
DR   AlphaFoldDB; C4K8M7; -.
DR   SMR; C4K8M7; -.
DR   STRING; 572265.HDEF_0089; -.
DR   EnsemblBacteria; ACQ66864; ACQ66864; HDEF_0089.
DR   GeneID; 66260030; -.
DR   KEGG; hde:HDEF_0089; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002334; 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 membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..816
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000205850"
FT   MOTIF           298..303
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   816 AA;  94735 MW;  24E83ECC48B7A056 CRC64;
     MSDRCKIYYQ SLYLFVKIFI KSKLIPKNFV TDSGLDSSSP IFYILPSRSK MDLIILREES
     LKQGLPDPLT PLKVDEIQIP RYLFIDDIKE SHGHSPSSAE TLFSRYLGLY SKNSTLDITI
     LPVSVMIGRR PISICQNRKI NRLQKFFTAF WLGRDSFVHF SNPISLSRII NAHSKDLRIV
     YKLARVARIH FFRQYLSSVG RALPVHSDLF KKLLSSEAIE KALLDEARSK KISPQKAHDN
     ALRLMKEIAS QVSYETIRLS DRVLGWMWNR FYQGIHVHNA DCVRQLAYKG HSIVYVPCHR
     SHMDYLLLSY VLYYEGLATP HIAAGINLNF WPAGAIFRRL GAFFIRRNFK GNKLYSTIFR
     AYLDELFTGG YPVEYFIEGG RSRTGLLLEP KTGTLSMTIQ AMLRDISPSI TLIPVYIGYE
     HVIEVLSYTK ELRGERKKKE NFFQMIGGLR QLRHLGQGYV NFGEPIQLKL YLDKNVPDWR
     ESIRPINKIE ATRPHWLAST VKDLAYQIMI NINHAAAINA INLCSTALLA SENQALTRPE
     LLEQLNCYLQ LMRHAPHNQY SSVTDQMPEE LLDHALHMNK FVVQKNHPHE RICLPKEQVP
     LMRYYRNNIQ HLLILPSLIA TTVLCHHNIS RQEIIRQITL LYPVFKIRWF LYYSEKQLLE
     ALNLLMDELI RQKCVENKNH HFVVNLSSGM MTLKILASGI KEILQHYSII FFLLTVYPDI
     DRKSLEKESR AMAKHLCILE NMPSAEFFHS SIFSGLLTLL FEKREKMVSN DYSAQKNIEE
     IFNILKGLIS SQMISVMQEN FSLKKEWLTY KKKTTD