PLSY_BRUSU
ID PLSY_BRUSU Reviewed; 201 AA.
AC P59246; G0KCX9;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_01043};
DE EC=2.3.1.275 {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Lysophosphatidic acid synthase {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=LPA synthase {ECO:0000255|HAMAP-Rule:MF_01043};
GN Name=plsY {ECO:0000255|HAMAP-Rule:MF_01043};
GN OrderedLocusNames=BRA0601, BS1330_II0596;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate
CC (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic
CC acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor,
CC but not acyl-CoA or acyl-ACP. {ECO:0000255|HAMAP-Rule:MF_01043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:59918; EC=2.3.1.275; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01043};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01043}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
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DR EMBL; AE014292; AAN33790.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20067.1; -; Genomic_DNA.
DR RefSeq; WP_004690218.1; NZ_KN046805.1.
DR AlphaFoldDB; P59246; -.
DR SMR; P59246; -.
DR EnsemblBacteria; AEM20067; AEM20067; BS1330_II0596.
DR GeneID; 45053637; -.
DR GeneID; 55592272; -.
DR KEGG; bms:BRA0601; -.
DR KEGG; bsi:BS1330_II0596; -.
DR PATRIC; fig|204722.21.peg.537; -.
DR HOGENOM; CLU_081254_1_0_5; -.
DR OMA; WRHRGNL; -.
DR PhylomeDB; P59246; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000007104; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01043; PlsY; 1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR PANTHER; PTHR30309; PTHR30309; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
DR TIGRFAMs; TIGR00023; TIGR00023; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..201
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188338"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ SEQUENCE 201 AA; 20607 MW; 0C2CA44592AE4DF1 CRC64;
MAEPGFFNAM LIGALIFGYV LGSIPFGLIL TRLAGLGDVR AIGSGNIGAT NVLRTGNKKL
AAATLILDAL KGTAAALIAA HFGQNAAIAA GFGAFIGHLF PVWIGFKGGK GVATYLGVLI
GLAWAGALVF AAAWIVTALL TRYSSLSALV ASLVVPIALY SRGNQALAAL FAIMTVIVFI
KHRANIRRLL NGTESKIGAK G
