PLSB_EDWI9
ID PLSB_EDWI9 Reviewed; 818 AA.
AC C5B706;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=NT01EI_0225;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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; CP001600; ACR67468.1; -; Genomic_DNA.
DR RefSeq; WP_015869677.1; NC_012779.2.
DR AlphaFoldDB; C5B706; -.
DR SMR; C5B706; -.
DR STRING; 67780.B6E78_12250; -.
DR PRIDE; C5B706; -.
DR EnsemblBacteria; ACR67468; ACR67468; NT01EI_0225.
DR GeneID; 7960249; -.
DR KEGG; eic:NT01EI_0225; -.
DR PATRIC; fig|634503.3.peg.201; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000001485; 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..818
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000205849"
FT MOTIF 305..310
FT /note="HXXXXD motif"
SQ SEQUENCE 818 AA; 92827 MW; C22D7ADC3D55C290 CRC64;
MSGWRKIYYK LLNLILKLLV KSKVIPTDPV AELRLDTTRP VFYVLPYNSK VDLLTLRDRC
LALDLPDPLD DNEIDGVILP RYVFIDDGPR VFRYYAPKQA SVKLFLDYLD LHRGNPSLDI
QMIPVSVMFG RAPGREDHKG APQLRLLNGI QKFFAVLWLG RDSFVRFSNT VSLRYMADEH
GTDKTIAQKL ARVARMHFSR LRLAAVGPRL PDRQALFNKL LGSKAIEKAV EDEARSKKIS
REKAQQNAVA LMEEIAADFT YEAVRLSDRV LSWTWNRLYQ GINVHNAERV RQLAQDGHEI
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK
LYSTVFREYL GELFSRGYSV EYFMEGGRSR TGRLLEPKTG TLAMTLQAML RGGKRPITLV
PVYIGYEHVM EVATYAKELR GATKEKESLP QMVRGLRKLR NLGQGYVNFG EPISLNVWLN
QHVPEWREAI DPIEAQRPHW LPASVNSIAG EVMVNINKAA AANAMNLCAT ALLASRQRAL
TREQLLEQLE CYLQLLQNVP YAPDATLPQR TPQELLDHAL QMNKFEVEKD NIGDLIILPR
EQAVLMTYYR NNIQHMLVLP ALVASMVIHH RQISRDELLR QAAVIYPMLK QELFMHYVPE
TLPQVLSPII DELCRQQLIS LQDDTLIINP PRIRSLQLLA AGVRETLQRY AITFSLLSAN
PSISRGALEK ESRILAQRLS LLHGINAPEF FDKAVFATLV ATLRAEGYIN DVGDAVREQT
LEIYNLLADL LTPEIRLTIE SVSIAALEDT GGADGGTA
