PLSB_SHEAM
ID PLSB_SHEAM Reviewed; 807 AA.
AC A1SBC6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Sama_3480;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-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; CP000507; ABM01683.1; -; Genomic_DNA.
DR RefSeq; WP_011761586.1; NC_008700.1.
DR AlphaFoldDB; A1SBC6; -.
DR SMR; A1SBC6; -.
DR STRING; 326297.Sama_3480; -.
DR EnsemblBacteria; ABM01683; ABM01683; Sama_3480.
DR KEGG; saz:Sama_3480; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000009175; 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..807
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000049453"
FT MOTIF 308..313
FT /note="HXXXXD motif"
SQ SEQUENCE 807 AA; 92011 MW; 247CFDC15679CC0A CRC64;
MSAHESFWFK SLRWIQKQLV HTIVVPQDPF ADLNLDPSRP LVYVMKTESV SDIAALHEIT
GKLGLPSPYQ MLEIDGIKTP RVVCLEGRKP LFGKRDSNEP FLQTFQQLLA LHRQQQELDI
QLVPVSLYWG RTPGKEDDTM RAAVLEREDP TWLRKCLMIL FLGRHNFVQF SRAVSLRHMA
DEHGTDKRIA HKLARVARVH FRRQRKVMTG PVLPNRQAMF HALLKSDNLK KAIAEEASSK
KISEEKARET AIQYLDEIAA DYSDSLVRIA ERFLTWLWNK LYKGISIKGA EQIRQLHHDG
HEIVYVPCHR SHMDYLLLSY ILYYEGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFN
GNKLYTAVFR EYLDQLFAKG YSVEYFTEGG RSRTGRLLAP KTGMLAMTLS SVIRGIERPV
TLVPVYLGYD HVMEVATYHK ELSGKKKEKE SVWQVFGAIR KLGNFGRGYV NFGQPITLQN
FLTEKVPNWR EEVGEDPEQK PSWLTPVVNA LANRVMTRIN DAAAASSVTL SSMVLLASEQ
NALERNQLER QIDLYLSLLK SVPYTSYASV TEGCGKELVD RGIELNKLTE TKDDLGTIIS
IDDSLAISMT YYRNNIIHLF VIPSLIATVM VRHEEVSREE LQELVAEFYP LLKAELFMGV
TDLPAYVDAL VECFKSEGLI TGDNRLKLVD DRINQLLLLA GVVGETLKRY AIIFNLLGEQ
PRMERADLEH HSHRLASRLG AIHGVMAPEF YDKKLYALLS SKLKDLGYLS DKADGDKVRK
IRDHANGLLR SSVRQTIIET LNQEQDD
