ID   PLSB_HAEDU              Reviewed;         811 AA.
AC   Q7VNI5;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=HD_0546;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017143; AAP95485.1; -; Genomic_DNA.
DR   RefSeq; WP_010944538.1; NC_002940.2.
DR   AlphaFoldDB; Q7VNI5; -.
DR   STRING; 233412.HD_0546; -.
DR   EnsemblBacteria; AAP95485; AAP95485; HD_0546.
DR   KEGG; hdu:HD_0546; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001022; 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; Reference proteome; Transferase.
FT   CHAIN           1..811
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000195221"
FT   MOTIF           303..308
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   811 AA;  92885 MW;  8F449267F8B77E2C CRC64;
     MSSLLSFYRN ILNFPLSLLV KSQAIPTDPV SELGLNLEQP IIYVLPYTSQ TDLLILQKNC
     LALNLPDPLV ENDIQGQSLP RYVFLDEGHR FFKSKGVKSE TESLFYRYLD LHKTDETLDV
     QLVPVSVLWG RSPGKETAPS LRLLSRFQRI IAMIWFGRDN FVRFSQAVSL CYMVKEYGAE
     KGIAQKLARV AKIHFAKQRY SAMGPRLPER QAMFDKLIQL PTIVQAIEDE AKTKKIPIPK
     ARQEAEKILD EIAADVSHGT LRMADRVLSW LWNKLYQGIN VQNADRVRKL ALEGHEIIYV
     PCHRSHMDYL LLSYILYHQG VVPPHIAAGI NLNFWPAGPF FRRGGAFFIR RTFKGNRLYS
     TVFREYLAEL FYRGYSVEYF IEGGRSRTGR LLEPKTGMVS MTLQALQRGL NRPISIVPVY
     IGYEHVLEVD TYAKELRGAA KEKENAELVL RVIKKLRNLG QGYVNFGKPI QVNSYLNQHF
     PEWKLPPVEN VRPKWLNEAV DAIAKQVMVN INNAAAVNAK NLIGSVLLAS RQRALSREQL
     IEQVESYLQL FQNVSYSSDI ILPTESADEM LEHVLALPRS GVMSEKDNFG EMIRLDRESA
     VLMTYYRNNI QHLFVLPSLV ASIVLHNEAA SKTLIRETVS HIYPFLKAEL FLHFDEKEVL
     EQVELILTEF IRQQIVKYDG DVLTINRRRL PTLQLHAAGI REILQRYYIS LSLLLECPAI
     SRTLLEKESR MIAQRLSILH GINAPEFFDK AIFSTFTASL KAQGYFDLEG HTVIEKVEEV
     AHILRRLISV EVQLTIQGAM DKVDQIDEKL E