PLSB_SHEB5
ID PLSB_SHEB5 Reviewed; 807 AA.
AC A3CYX8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=Sbal_0157;
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091;
RG US DOE Joint Genome Institute;
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 Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) 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}.
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DR EMBL; CP000563; ABN59691.1; -; Genomic_DNA.
DR RefSeq; WP_011845444.1; NC_009052.1.
DR AlphaFoldDB; A3CYX8; -.
DR SMR; A3CYX8; -.
DR STRING; 325240.Sbal_0157; -.
DR EnsemblBacteria; ABN59691; ABN59691; Sbal_0157.
DR KEGG; sbl:Sbal_0157; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000001557; 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_1000049454"
FT MOTIF 308..313
FT /note="HXXXXD motif"
SQ SEQUENCE 807 AA; 91245 MW; 18EF14E0B6A9EB68 CRC64;
MPKHDSLWLK SLRWIQKHLV HTIVVPQDPF ADLNLDASRP LAYVMKTESL SDIAALSEIT
AKLGLPSPYE PLVANGVIAP RVVCLQGRKP LFGERAGNEP FLECFMRLLA VHKERPELDI
QLVPVSLYWG RTPGKEDDTM KAAVFERENP TWLRKCLMIL FLGRHNFVQF SNAVSLRYMA
DEHGTDMGIA HKLARVARVH FRRQRKVMTG PVLPNRQALF HSLLKSESLR KAIQEEAANK
KISETQARET AIEYLDEIAA DYSDSLVRIA ERFLTWLWNK LYSGINIKGA EQVRQLHHDG
HEIVYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFN
GNKLYTAVFR EYLDQLFAKG YSVEYFSEGG RSRTGRLLAP KTGMIAMTMN SVLRGIERPV
TLVPVYLGYD HVMEVATYHK ELSGKKKKKE SVWQVFGAIR KLGNFGQGYV NFGEPITLQN
FLNERAPNWR TELADDPEQK PSWLTPAVNV LANRVMTNIN DAAAASSVTL TSLVLLATDQ
NALERSLLER QLDLYLTLLK KVPYTTYTSV AEGDGKHLVQ QGLELNKFVV CADPLGEIVS
IEASQAVSMT YYRNNIIHLF IVPSLIASCL THNKQIPRQQ VVSIVADFYP LLKAELFMGI
KDVPAYVNQV LDFFIEQGLV VETDTLTVVP EHTSQLLLLA SSVSETLQRY AIIFNLLANR
PKMERSELES ESHLLAQRLG ALHGITAPEF YDKKLYGTLS VKLKELGYLA DNQDKSNINR
IRDQANSLLR PSVKQTIVAS VTAEHTV