ID   PLSB_SHEON              Reviewed;         809 AA.
AC   Q8E8Q9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=SO_4602;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN57562.1; -; Genomic_DNA.
DR   RefSeq; NP_720118.1; NC_004347.2.
DR   RefSeq; WP_011074199.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8E8Q9; -.
DR   SMR; Q8E8Q9; -.
DR   STRING; 211586.SO_4602; -.
DR   PaxDb; Q8E8Q9; -.
DR   KEGG; son:SO_4602; -.
DR   PATRIC; fig|211586.12.peg.4460; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   PhylomeDB; Q8E8Q9; -.
DR   BioCyc; SONE211586:G1GMP-4252-MON; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
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   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
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..809
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000195233"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   809 AA;  91562 MW;  9E5DD163FAB93DD3 CRC64;
     MPKQDSLWLK SLRWIQKYLV HTIVVPQDPF ADLNLDASRP LAYVMKTESL SDIAALSEIT
     AKLGLPSPYE PLVVNGVVAP RVVCLEGRKP LFGDRASNEP FLECFMRLLA VHKEKPELDI
     QLVPVSLYWG RTPGKEDDTM KAAVLERENP TWLRKCLMIL FLGRHNFVQF SNAVSLRYMA
     DEHGTDMGIA HKLARVARVH FRRQRKVMTG PVLPNRQALF DSLLKSESLR KAIQEEAASK
     KISETQARET AIEYLDEIAA NYSDSLVRIA ERFLTWLWNK LYSGINIKGA EQIRQLHHDG
     HEIVYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPLFRRG GAFFIRRSFN
     GNKLYTAVFR EYLDQLFAKG YSVEYFSEGG RSRTGRLLAP KTGMIAMTIN SVLRGIERPV
     TLVPVYLGYD HVMEVATYHK ELSGKKKQKE SVWQVFGAIR KLGNFGQGYV NFGEPITLQN
     FLNETAPNWR SEVADDPEQK PTWLTPAVNV LANRVMTRIN DAAAASSITL TSLVLLASEQ
     NALERCLLER QLDLYLTLLK RVPYTSFTSV AEGDGKHLVQ QGLELNKFSI SADPLGEIVS
     IDDKQAISMT YYRNNIIHLF IIPSLIASCL INNKQISRAQ IFGVVNDFYP LLKAELFMGI
     KDLPSYVDQV LDLFIEQGLV EETELLSVAT ERASQMLLLA GSVNETLQRY AIIFNLLAHR
     PKMERSDLES ESHLLAQRLG ALHGITAPEF YDKKLYNTLS VKLKELGYFS GKEDKSDVER
     IREQANNLLR ASVRQTIVAS VTAEQSFNG