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Glycerol-3-phosphate acyltransferase (GPAT) (EC 2.3.1.15)

 PLSB_ECOLI              Reviewed;         807 AA.
P0A7A7; P00482; Q2M6R3; Q9S683;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 117.
RecName: Full=Glycerol-3-phosphate acyltransferase;
Short=GPAT;
EC=2.3.1.15;
Name=plsB; OrderedLocusNames=b4041, JW4001;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6309817;
Lightner V.A., Bell R.M., Modrich P.;
"The DNA sequences encoding plsB and dgk loci of Escherichia coli.";
J. Biol. Chem. 258:10856-10861(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ALA-349.
STRAIN=K12;
PubMed=10074094;
Heath R.J., Rock C.O.;
"A missense mutation accounts for the defect in the glycerol-3-
phosphate acyltransferase expressed in the plsB26 mutant.";
J. Bacteriol. 181:1944-1946(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8265357; DOI=10.1093/nar/21.23.5408;
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the
region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 781-807.
STRAIN=K12;
PubMed=1644758; DOI=10.1128/jb.174.16.5309-5316.1992;
Nichols B.P., Green J.M.;
"Cloning and sequencing of Escherichia coli ubiC and purification of
chorismate lyase.";
J. Bacteriol. 174:5309-5316(1992).
[7]
PARTIAL PROTEIN SEQUENCE.
PubMed=6350296;
Green P.R., Vanaman T.C., Modrich P., Bell R.M.;
"Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide
analysis of Escherichia coli sn-glycerol-3-phosphate
acyltransferase.";
J. Biol. Chem. 258:10862-10866(1983).
[8]
SUBCELLULAR LOCATION.
PubMed=4943977; DOI=10.1016/0005-2736(71)90145-3;
White D.A., Albright F.R., Lennarz W.J., Schnaitman C.A.;
"Distribution of phospholipid-synthesizing enzymes in the wall and
membrane subfractions of the envelope of Escherichia coli.";
Biochim. Biophys. Acta 249:636-642(1971).
[9]
IDENTIFICATION.
STRAIN=K12;
PubMed=6251087;
Lightner V.A., Larson T.J., Tailleur P., Kantor G.D., Raetz C.R.,
Bell R.M., Modrich P.;
"Membrane phospholipid synthesis in Escherichia coli. Cloning of a
structural gene (plsB) of the sn-glycerol-3-phosphate
acyl/transferase.";
J. Biol. Chem. 255:9413-9420(1980).
[10]
FUNCTION.
STRAIN=K12;
PubMed=6997313;
Larson T.J., Lightner V.A., Green P.R., Modrich P., Bell R.M.;
"Membrane phospholipid synthesis in Escherichia coli. Identification
of the sn-glycerol-3-phosphate acyltransferase polypeptide as the plsB
gene product.";
J. Biol. Chem. 255:9421-9426(1980).
[11]
BIOPHYSICOCHEMICAL PROPERTIES, AND FATTY ACYL DONOR SPECIFICITY.
PubMed=7026564;
Green P.R., Merrill A.H. Jr., Bell R.M.;
"Membrane phospholipid synthesis in Escherichia coli. Purification,
reconstitution, and characterization of sn-glycerol-3-phosphate
acyltransferase.";
J. Biol. Chem. 256:11151-11159(1981).
[12]
MUTAGENESIS OF HIS-306 AND ASP-311.
STRAIN=K12;
PubMed=9515909;
Heath R.J., Rock C.O.;
"A conserved histidine is essential for glycerolipid acyltransferase
catalysis.";
J. Bacteriol. 180:1425-1430(1998).
[13]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-306; SER-308;
ASP-311; PHE-351; ILE-352; ARG-354; GLU-385; GLY-386; SER-389 AND
PRO-421.
STRAIN=K12;
PubMed=10231527; DOI=10.1021/bi982805d;
Lewin T.M., Wang P., Coleman R.A.;
"Analysis of amino acid motifs diagnostic for the sn-glycerol-3-
phosphate acyltransferase reaction.";
Biochemistry 38:5764-5771(1999).
[14]
SUBCELLULAR LOCATION, AND INTERACTION WITH ACP; YBGC AND PSSA.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16294310; DOI=10.1002/pmic.200500115;
Gully D., Bouveret E.;
"A protein network for phospholipid synthesis uncovered by a variant
of the tandem affinity purification method in Escherichia coli.";
Proteomics 6:282-293(2006).
[15]
FUNCTION IN PHOSPHOLIPID BIOSYNTHESIS.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=17645809; DOI=10.1186/1471-2180-7-69;
Yoshimura M., Oshima T., Ogasawara N.;
"Involvement of the YneS/YgiH and PlsX proteins in phospholipid
biosynthesis in both Bacillus subtilis and Escherichia coli.";
BMC Microbiol. 7:69-69(2007).
-!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to
glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA).
This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty
acyl donor. {ECO:0000269|PubMed:17645809,
ECO:0000269|PubMed:6997313}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
acyl-sn-glycerol 3-phosphate.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=49 uM for glycerol-3-phosphate {ECO:0000269|PubMed:10231527,
ECO:0000269|PubMed:7026564};
Vmax=13.1 nmol/min/mg enzyme with glycerol-3-phosphate as
substrate {ECO:0000269|PubMed:10231527,
ECO:0000269|PubMed:7026564};
pH dependence:
Optimum pH is 8.5. {ECO:0000269|PubMed:10231527,
ECO:0000269|PubMed:7026564};
-!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
-!- SUBUNIT: Interacts with ACP, YbgC and PssA, forming altogether a
complex at the inner membrane. {ECO:0000269|PubMed:16294310}.
-!- INTERACTION:
P0A6A8:acpP; NbExp=3; IntAct=EBI-542961, EBI-542566;
P0A8Z3:ybgC; NbExp=3; IntAct=EBI-542961, EBI-543276;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:16294310, ECO:0000269|PubMed:4943977};
Peripheral membrane protein {ECO:0000269|PubMed:16294310,
ECO:0000269|PubMed:4943977}; Cytoplasmic side
{ECO:0000269|PubMed:16294310, ECO:0000269|PubMed:4943977}.
-!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
and may constitute the binding site for the phosphate moiety of
the glycerol-3-phosphate.
-!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC43135.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; K00127; AAA24395.1; -; Genomic_DNA.
EMBL; AF106625; AAD20588.1; -; Genomic_DNA.
EMBL; U00006; AAC43135.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC77011.2; -; Genomic_DNA.
EMBL; AP009048; BAE78043.1; -; Genomic_DNA.
EMBL; M93413; AAA24718.1; -; Genomic_DNA.
EMBL; M93136; AAA24713.1; -; Genomic_DNA.
PIR; A00565; XUECAG.
RefSeq; NP_418465.4; NC_000913.3.
RefSeq; WP_000017354.1; NZ_LN832404.1.
ProteinModelPortal; P0A7A7; -.
BioGrid; 4261720; 246.
DIP; DIP-29380N; -.
IntAct; P0A7A7; 37.
STRING; 316385.ECDH10B_4230; -.
SwissLipids; SLP:000001804; -.
EPD; P0A7A7; -.
PaxDb; P0A7A7; -.
PRIDE; P0A7A7; -.
EnsemblBacteria; AAC77011; AAC77011; b4041.
EnsemblBacteria; BAE78043; BAE78043; BAE78043.
GeneID; 948541; -.
KEGG; ecj:JW4001; -.
KEGG; eco:b4041; -.
PATRIC; fig|511145.12.peg.4158; -.
EchoBASE; EB0733; -.
EcoGene; EG10740; plsB.
eggNOG; ENOG4105E55; Bacteria.
eggNOG; COG2937; LUCA.
HOGENOM; HOG000218231; -.
InParanoid; P0A7A7; -.
KO; K00631; -.
OMA; EVIYVPC; -.
PhylomeDB; P0A7A7; -.
BioCyc; EcoCyc:GLYCEROL-3-P-ACYLTRANSFER-MONOMER; -.
BioCyc; MetaCyc:GLYCEROL-3-P-ACYLTRANSFER-MONOMER; -.
SABIO-RK; P0A7A7; -.
UniPathway; UPA00557; UER00612.
PRO; PR:P0A7A7; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IMP:EcoliWiki.
GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006631; P:fatty acid metabolic process; IMP:EcoliWiki.
GO; GO:0008654; P:phospholipid biosynthetic process; IMP:EcoliWiki.
HAMAP; MF_00393; Glyc3P_acyltrans; 1.
InterPro; IPR022284; GPAT/DHAPAT.
InterPro; IPR028354; GPAT_PlsB.
InterPro; IPR002123; Plipid/glycerol_acylTrfase.
PANTHER; PTHR12563; PTHR12563; 1.
Pfam; PF01553; Acyltransferase; 1.
PIRSF; PIRSF500064; GPAT; 1.
PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
SMART; SM00563; PlsC; 1.
TIGRFAMs; TIGR03703; plsB; 1.
1: Evidence at protein level;
Acyltransferase; Cell inner membrane; Cell membrane;
Complete proteome; Direct protein sequencing; Lipid biosynthesis;
Lipid metabolism; Membrane; Phospholipid biosynthesis;
Phospholipid metabolism; Reference proteome; Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 807 Glycerol-3-phosphate acyltransferase.
/FTId=PRO_0000195218.
MOTIF 306 311 HXXXXD motif.
MUTAGEN 306 306 H->A: Abolishes acyltransferase activity.
{ECO:0000269|PubMed:10231527,
ECO:0000269|PubMed:9515909}.
MUTAGEN 306 306 H->G: Reduced acyltransferase activity.
{ECO:0000269|PubMed:10231527,
ECO:0000269|PubMed:9515909}.
MUTAGEN 308 308 S->A: No effect.
{ECO:0000269|PubMed:10231527}.
MUTAGEN 311 311 D->A: Prevents assembly into the
membrane, suggesting that it paticipates
to folding. {ECO:0000269|PubMed:10231527,
ECO:0000269|PubMed:9515909}.
MUTAGEN 311 311 D->G: Strongly reduced acyltransferase
activity. {ECO:0000269|PubMed:10231527,
ECO:0000269|PubMed:9515909}.
MUTAGEN 349 349 A->T: In plsB26; results in high KM for
glycerol-3-phosphate and reduced specific
activity. {ECO:0000269|PubMed:10074094}.
MUTAGEN 351 351 F->A: Strongly reduced acyltransferase
activity. {ECO:0000269|PubMed:10231527}.
MUTAGEN 352 352 I->A: Reduced acyltransferase activity.
{ECO:0000269|PubMed:10231527}.
MUTAGEN 354 354 R->C: Reduced acyltransferase activity.
{ECO:0000269|PubMed:10231527}.
MUTAGEN 354 354 R->K: No effect.
{ECO:0000269|PubMed:10231527}.
MUTAGEN 385 385 E->R: Strongly reduced acyltransferase
activity. {ECO:0000269|PubMed:10231527}.
MUTAGEN 386 386 G->A: No effect.
{ECO:0000269|PubMed:10231527}.
MUTAGEN 386 386 G->L: Reduced acyltransferase activity.
{ECO:0000269|PubMed:10231527}.
MUTAGEN 389 389 S->A: No effect.
{ECO:0000269|PubMed:10231527}.
MUTAGEN 421 421 P->S: Reduced acyltransferase activity.
{ECO:0000269|PubMed:10231527}.
SEQUENCE 807 AA; 91381 MW; D6FC6892981D7EFE 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 AHSRTLQLLA AGARETLQRY AITFWLLSAN
PSINRGTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DSGDAEPAET
MKVYQLLAEL ITSDVRLTIE SATQGEG


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