PLSB_PSEPK
ID PLSB_PSEPK Reviewed; 828 AA.
AC Q88MQ0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=PP_1520;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN67141.1; -; Genomic_DNA.
DR RefSeq; NP_743677.1; NC_002947.4.
DR RefSeq; WP_010952610.1; NC_002947.4.
DR AlphaFoldDB; Q88MQ0; -.
DR STRING; 160488.PP_1520; -.
DR EnsemblBacteria; AAN67141; AAN67141; PP_1520.
DR KEGG; ppu:PP_1520; -.
DR PATRIC; fig|160488.4.peg.1610; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR PhylomeDB; Q88MQ0; -.
DR BioCyc; PPUT160488:G1G01-1611-MON; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000000556; 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..828
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195229"
FT MOTIF 310..315
FT /note="HXXXXD motif"
SQ SEQUENCE 828 AA; 93693 MW; B10CE9CCEA9DD672 CRC64;
MTRSPLHRLI FGGLRRLLYL WVRSETINQS SMTLNLDRSR PVFYALPSPA LTDLAVLDHE
CTKAGLPRPV LPVAVGPLQE PAAFFYLTPD PDWLGRQDKS GAPPTLERLV AAVSQHAEED
AQIIPVSVFW GQTPASESSP WKLLFADSWA VTGRLRRLLT VLILGRKTRV QFSAPIHLRE
LVQHNKGHER TVRMAQRLMR VHFRNLKTAV IGPDISHRRT LVKGLVHAPQ VRQAIADEAQ
RENLPLAKAE AQALRYGNEI ASDYTYTAIR FLEVVLSWFW NKIYDGIKVN HIEQVQGIAP
GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHVAAGINLN MPVVGNLLRR GGAFFMRRTF
KGNPLYTAVF NEYLHTLYTK GFPVEYFVEG GRSRTGRMLQ PRTGMLAITL RSFLRSSRTP
IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESVLDIFKVF GALKQRFGQV YVNFGEPIRL
AGFLDQQQPG WREQDHGPQY RPEWLNATTA RLGETVARHL NEAAAINPVN LVALALLSTS
RLALDERALT RVLDLYLALL RQVPYSPHTT LPEGDGQALI EHVRSMNLVA EQKDALGRIL
YLDEGNAVLM TYYRNNVLHI FALPALLASF FLSSSRMSRQ LLGQYVHALY PYLQAELFLR
WTPEQLDEVI DQWLVALVEQ GLLRQDNDLY VRPAPSSRQF VLLTLLARTI TQTLQRFYMA
TSLLINSGQN SLSAEALEDL CVMMAQRLSI LHGLNAPEFF DKTLFRHFIQ TLLQQGVLHA
DAQGKLSYHD KLGELAEGVA KRVLSAELRL SIRQVALHRD DGLETSTL
