ID PLSY_BLOFL Reviewed; 196 AA.
AC Q7VQQ8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 29-MAY-2013, entry version 63.
DE RecName: Full=Glycerol-3-phosphate acyltransferase;
DE AltName: Full=Acyl-PO4 G3P acyltransferase;
DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase;
DE AltName: Full=G3P acyltransferase;
DE Short=GPAT;
DE EC=2.3.1.n3;
DE AltName: Full=Lysophosphatidic acid synthase;
DE Short=LPA synthase;
GN Name=plsY; OrderedLocusNames=Bfl060;
OS Blochmannia floridanus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=203907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis
RT of reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-
CC phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form
CC lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate
CC as fatty acyl donor, but not acyl-CoA or acyl-ACP (By similarity).
CC -!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1-
CC acyl-sn-glycerol 3-phosphate + phosphate.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBUNIT: Probably interacts with PlsX (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the PlsY family.
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DR EMBL; BX248583; CAD83585.1; -; Genomic_DNA.
DR RefSeq; NP_878372.1; NC_005061.1.
DR STRING; 203907.Bfl060; -.
DR EnsemblBacteria; CAD83585; CAD83585; Bfl060.
DR GeneID; 1499260; -.
DR KEGG; bfl:Bfl060; -.
DR PATRIC; 31963711; VBICanBlo38691_0061.
DR eggNOG; COG0344; -.
DR HOGENOM; HOG000283806; -.
DR KO; K08591; -.
DR OMA; WRHRGNL; -.
DR ProtClustDB; CLSK2411639; -.
DR BioCyc; BFLO203907:GHF7-60-MONOMER; -.
DR UniPathway; UPA00085; -.
DR GO; GO:0016021; C:integral to 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:HAMAP.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_01043; PlsY; 1; -.
DR InterPro; IPR003811; G3P_acylTferase.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR TIGRFAMs; TIGR00023; TIGR00023; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Complete proteome;
KW Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 196 Glycerol-3-phosphate acyltransferase.
FT /FTId=PRO_0000188331.
FT TRANSMEM 1 21 Helical; (Potential).
FT TRANSMEM 55 75 Helical; (Potential).
FT TRANSMEM 81 101 Helical; (Potential).
FT TRANSMEM 118 138 Helical; (Potential).
FT TRANSMEM 140 160 Helical; (Potential).
SQ SEQUENCE 196 AA; 22711 MW; E160131FD04D426A CRC64;
MIIFTATLII ILAYFLGSIS GSILICKTLH FKDPRQHGSK NPGTTNILRI INYKIAIFVL
LFDSLKGAVP IWLGTYFHID PIYLYIIAIS ACIGHIYPIY FQFYGGKGVA TAFGALTAIS
INFFIIIIIT WILTVYLFRY ASLGSIVTFI VITFYVWYIQ YHHFEYIILL SLIILSQHKN
NIKRLWNHQE KHIWNR
//