ID PLSY_NEIM0 Reviewed; 200 AA.
AC A9LYY1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 45.
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=NMCC_0978;
OS Neisseria meningitidis serogroup C (strain 053442).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Neisseria.
OX NCBI_TaxID=374833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=053442;
RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X.,
RA Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y.,
RA Shao Z., Liang X., Xu J., Jin Q.;
RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT clone.";
RL Genomics 91:78-87(2008).
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; CP000381; ABX73158.1; -; Genomic_DNA.
DR RefSeq; YP_001599114.1; NC_010120.1.
DR STRING; 374833.NMCC_0978; -.
DR EnsemblBacteria; ABX73158; ABX73158; NMCC_0978.
DR GeneID; 5796076; -.
DR KEGG; nmn:NMCC_0978; -.
DR PATRIC; 20346556; VBINeiMen117761_1197.
DR eggNOG; COG0344; -.
DR HOGENOM; HOG000283806; -.
DR KO; K08591; -.
DR OMA; WRHRGNL; -.
DR ProtClustDB; CLSK2300446; -.
DR BioCyc; NMEN374833:GJ7Z-976-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 1 200 Glycerol-3-phosphate acyltransferase.
FT /FTId=PRO_1000084388.
FT TRANSMEM 2 22 Helical; (Potential).
FT TRANSMEM 51 71 Helical; (Potential).
FT TRANSMEM 84 104 Helical; (Potential).
FT TRANSMEM 114 134 Helical; (Potential).
FT TRANSMEM 159 179 Helical; (Potential).
SQ SEQUENCE 200 AA; 20787 MW; D16A33DCA964B3A2 CRC64;
MFNISAVAVS YLIGSLSFAV IVSKYYGMDD PRTYGSGNPG ATNVLRSGKK KAAALTLLGD
AAKGLVAVLL ARVLQEPLGL SDSAIAAVAL AALVGHMWPV FFGFKGGKGV ATALGVLLAL
SPATALVCAL IWLVMAFGFK VSSLAALTAT IAAPLAALFF MPHTSWIWAT LLIALLVLFR
HKSNIVKLLE GRESKIGGSR
//
