PLSB_PSEFS
ID PLSB_PSEFS Reviewed; 839 AA.
AC C3K4R1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=PFLU_1255;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; AM181176; CAY47512.1; -; Genomic_DNA.
DR RefSeq; WP_012722581.1; NC_012660.1.
DR AlphaFoldDB; C3K4R1; -.
DR STRING; 294.SRM1_01112; -.
DR PRIDE; C3K4R1; -.
DR EnsemblBacteria; CAY47512; CAY47512; PFLU_1255.
DR KEGG; pfs:PFLU_1255; -.
DR PATRIC; fig|216595.4.peg.1485; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002332; 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..839
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000205852"
FT MOTIF 309..314
FT /note="HXXXXD motif"
SQ SEQUENCE 839 AA; 95386 MW; D997AB5D518AF75B CRC64;
MTRSPFRRLV FGTLRRLLYL WVRSETINQS SLTLNLDRSR PVFYVLQSPS LSELAVVDAE
CTKAGLPRPV LPVSVGPLME PAAFFYLTPE PDWLGRQDKR GAPPTLTRLV NTLSEHAEEN
AQIIPVSVFW GQSPESESSP WKLLFADSWA VTGRLRRLLS ILILGRKTRV QFSAPINLRE
LIEHNKGHER TVRMAQRILR VHFRNLKTAV IGPDLSHRRN LVKGLVNMPL VRQAIADEAE
REKITPEKAK AQALRYGNEI ASDYTYTAIR FLEVVLSWFW NKIYDGIKVN NIEGVQKVAQ
GYEVIYVPCH RSHIDYLLLS YLLFKNGLTP PHIAAGINLN MPVIGSLLRR GGAFFMRRTF
KGNPLYTSVF NEYLHTLFTK GFPVEYFVEG GRSRTGRMLQ PKTGMLAITL RSFLRSSRMP
IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESIFDIFKVV GALKQRFGQV AVNFGEPIKL
AEFLDAEQPD WRSQELGPNY KPAWLNETTN RLGEQVARHL NEAAAVNPVN LVALALLSTT
RLALDEQAMA RQLDLYLALL RRVPYSPHTT LPDGDGLALI KHVKDMDLLS EQSDALGKIL
YLDEQNAVLM TYYRNNVLHI FALPALLASF FQSSSRMSRD QILRYTHALY PYLQSELFIR
WSLDELDTVV DQWLEAFVEQ GLLRFENNVY LRPAPSSRHF VLLTLLSKTV AQTLQRFYMA
ISLLLNSGQN SISAEELEDL CTIMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLEQDVLRR
DEAGKLSYHD LLGELAEGAA KRVLPAEIRL SIRQVALHRV DGAAEAAVEP QPPKPEESR
