ID D3GT22_ECO44 Unreviewed; 807 AA.
AC D3GT22;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432, ECO:0000256|HAMAP-Rule:MF_00393};
DE Short=GPAT {ECO:0000256|HAMAP-Rule:MF_00393};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113, ECO:0000256|HAMAP-Rule:MF_00393};
GN Name=plsB {ECO:0000256|HAMAP-Rule:MF_00393,
GN ECO:0000313|EMBL:CBG37234.1};
GN OrderedLocusNames=EC042_4410 {ECO:0000313|EMBL:CBG37234.1};
OS Escherichia coli O44:H18 (strain 042 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG37234.1, ECO:0000313|Proteomes:UP000001407};
RN [1] {ECO:0000313|EMBL:CBG37234.1, ECO:0000313|Proteomes:UP000001407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT "Complete genome sequence and comparative metabolic profiling of the
RT prototypical enteroaggregative Escherichia coli strain 042.";
RL PLoS ONE 5:E8801-E8801(2010).
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:0000256|ARBA:ARBA00000510, ECO:0000256|HAMAP-
CC Rule:MF_00393};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|HAMAP-Rule:MF_00393}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00393}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00393}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00393}.
CC Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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:0000256|HAMAP-Rule:MF_00393}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|HAMAP-Rule:MF_00393}.
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DR EMBL; FN554766; CBG37234.1; -; Genomic_DNA.
DR RefSeq; WP_014639378.1; NC_017626.1.
DR AlphaFoldDB; D3GT22; -.
DR KEGG; elo:EC042_4410; -.
DR PATRIC; fig|216592.3.peg.4578; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000001407; 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; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR03703; plsB; 1.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 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 SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00393}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00393};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00393};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00393};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00393};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00393};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 300..427
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 305..310
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 807 AA; 91367 MW; A4A93892981D7BAB CRC64;
MSGWPRIYYK LLNLPLSILV KSKSIPADPA PELGLDTSRP IMYVLPYNSK ADLLTLRAQC
LAHDLPDPLE PLEIDGTLLP RYVFIHGGPR VFTYYTPKEE SIKLFHDYLD LHRSNPNLDV
QMVPVSVMFG RAPGREKGEV NPPLRMLNGV QKFFAVLWLG RDSFVRFSPS VSLRRMADEH
GTDKTIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL LASRAIAKAV EDEARSKKIS
HEKAQQNAIA LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEL
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK
LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG TLSMTIQAML RGGTRPITLI
PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLRGLSKLR NLGQGYVNFG EPMPLMTYLN
QHVPDWRESI DPIEAVRPAW LTPTVNNIAA DLMVRINNAG AANAMNLCCT ALLASRQRSL
TREQLTEQLN CYLDLMRNVP YSTDSTVPSA SASELIDHAL QMNKFEVEKD TIGDIIILPR
EQAVLMTYYR NNIAHMLVLP SLMAAIVTQH RHISRDVLME HVNVLYPMLK AELFLRWDRD
ELPDVIDALA NEMQRQGLIT LQDDELHINP AHSRSLQLLA AGARETLQRY AITFWLLSAN
PSINRGTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DSGDAEPAET
MKVYQLLAEL ITSDVRLTIE SATQGEG
//
