PLSB_PSEPF
ID PLSB_PSEPF Reviewed; 834 AA.
AC Q3KHC9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=Pfl01_1084;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
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; CP000094; ABA72827.1; -; Genomic_DNA.
DR RefSeq; WP_011332667.1; NC_007492.2.
DR AlphaFoldDB; Q3KHC9; -.
DR STRING; 205922.Pfl01_1084; -.
DR EnsemblBacteria; ABA72827; ABA72827; Pfl01_1084.
DR KEGG; pfo:Pfl01_1084; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002704; 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..834
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000049449"
FT MOTIF 309..314
FT /note="HXXXXD motif"
SQ SEQUENCE 834 AA; 94908 MW; 520AA312D5FB8437 CRC64;
MTRSPFRRLV FGTLRRLLYL WVRSETINQS SFTLNLDRSR PVFYVLQNPS LTDLAVVDTE
CTKAGLPRPV LPVSVGSLIE PAAFFYLTPD PDWLGRQDKR GAPPTLTRLV SALSQNAAED
AQIIPVSVFW GQSPDSENSP WKLLFADSWA VTGRLRRLLS IMILGRKTRV QFSAPIHLRE
LIEHNKGHER TVRMAQRILR VHFRNLKAAV IGPDISHRRN LVKGLLNQPL VKQAILDEAE
RENISPEKAK AQALRYGNEI ASDYTYTAIR FLEVVLSWFW NKIYDGIKVN HIEGVQKVAQ
GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVIGSLLRR GGAFFMRRTF
KGNPLYTSVF NEYLHTLFTK GFPVEYFVEG GRSRTGRMLQ PKTGMLAITL RSFLRSSRMP
IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESIFDIFKVI GALKQRFGQV AVNFGEPIKL
AEFLDSEQPG WRQQELGPQF KPAWLNETTN RLGEKVAQHL NEAAAINPVN LVALALLSTT
RLALDDRAMA RVLDLYLALL RKVPYSPHTT LPEGDGRALI EHVKDMDLLS EQNDALGKIL
YLDEQNAVLM TYYRNNVLHI FALPALLASF FQSTSRMSRE QILRYTRALY PYLQSELFIR
WTLDELDAVI DQWLEAFVEQ GLLRFEKDVY LRPAPSSRHF VLLTLLSKSI AQTLQRFYMT
VSLLLNSGQN SISAEELEDL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLDLDVLRR
DEAGKLSYHE LLGELAEGAA KRVLPAEIRL SIRQVALHRS EDAADQVAPP VQND
