(data stored in ACNUC7421 zone)

SWISSPROT: PLSY_PSEAB

ID   PLSY_PSEAB              Reviewed;         189 AA.
AC   Q02TI2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 69.
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.n3 {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=PA14_07580;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01043}.
CC   -!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1-
CC       acyl-sn-glycerol 3-phosphate + phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01043}.
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; CP000438; ABJ15545.1; -; Genomic_DNA.
DR   RefSeq; WP_003085061.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15545; ABJ15545; PA14_07580.
DR   KEGG; pau:PA14_07580; -.
DR   HOGENOM; HOG000283806; -.
DR   KO; K08591; -.
DR   OMA; HSQYPKI; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000653; Chromosome.
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:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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;
DR   PRODOM; Q02TI2.
DR   SWISS-2DPAGE; Q02TI2.
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    189       Glycerol-3-phosphate acyltransferase.
FT                                /FTId=PRO_1000064209.
FT   TRANSMEM      1     21       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
FT   TRANSMEM     50     70       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
FT   TRANSMEM     72     92       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
FT   TRANSMEM    111    131       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
FT   TRANSMEM    151    171       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
SQ   SEQUENCE   189 AA;  20225 MW;  905408C2FD6FD514 CRC64;
     MVWLLAILAY LLGSLSFAVL LSRWFGTQDP RASGSGNPGA TNMLRVAGKK LAILTLLGDV
     GKGLLPVLVA RWLGLGVMEE AWVGIAAVIG HLYPLYFNFR GGKGVATAAG MLLGLYPPAV
     LLAAAAWLLT FKLSRTSSLA SLVATPLTLP LLAWQQPGAL LPMTVLTGLI VWRHRANLRD
     LFAGRERHF
//

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