PLSB_SHESA
ID PLSB_SHESA Reviewed; 807 AA.
AC A0L2D7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=Shewana3_3988;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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; CP000469; ABK50206.1; -; Genomic_DNA.
DR RefSeq; WP_011718706.1; NC_008577.1.
DR AlphaFoldDB; A0L2D7; -.
DR SMR; A0L2D7; -.
DR STRING; 94122.Shewana3_3988; -.
DR PRIDE; A0L2D7; -.
DR EnsemblBacteria; ABK50206; ABK50206; Shewana3_3988.
DR KEGG; shn:Shewana3_3988; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002589; 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..807
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000049460"
FT MOTIF 308..313
FT /note="HXXXXD motif"
SQ SEQUENCE 807 AA; 91373 MW; A9F2422AB2AFCE6C CRC64;
MPKQDSLWLK SLRWIQKHLV HTIVVPQDPF ADLNLDASRP LAYVMKTESL SDIAALSEIT
TKLGLPSPYE PLVVNGVVAP RVVCLEGRKP LFGERASNEP FLECFMRLLA VHKEKPELDI
QLVPVSLYWG RTPGKEDDTM KAAVLERENP TWLRKCLMIL FLGRHNFVQF SNAVSLRYMA
DEHGTDMGIA HKLARVARVH FRRQRKVMTG PVLPNRQAMF HSLLKSESLR 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 TEVADDPEQK PTWLTPAVNV LANRVMTRIN DAAAASSITL TSLVLLASEQ
NALERCLLER QLDLYLTLLK RVPYTSFTSV AEGDGKHLVQ QGLELNKFSI HADPLGEIVS
IDANQAISMT YYRNNIIHLF IIPSLIASCL TNNKQISRAH ILGIVSDFYP LLKAELFMGI
KDLPSYVNQV LDLLIEQGLV QESDTLSVVT EHTSQMLLLA GSVSETLQRY AIIFNLLAHR
PKMERSELES ESHLLAQRLG ALHGITAPEF YDKKLYNTLS VKLKELGYFS EKEDKSDVER
IRDQANSLLR ASVRQTIVAS VTAEHIV
