(data stored in ACNUC7421 zone)

SWISSPROT: PLSY_EDWI9

ID   PLSY_EDWI9              Reviewed;         222 AA.
AC   C5BHG2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
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=NT01EI_0528;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR67761.1; -; Genomic_DNA.
DR   RefSeq; WP_015869961.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0528; -.
DR   EnsemblBacteria; ACR67761; ACR67761; NT01EI_0528.
DR   GeneID; 7961553; -.
DR   KEGG; eic:NT01EI_0528; -.
DR   PATRIC; fig|634503.3.peg.478; -.
DR   eggNOG; ENOG4105K7Z; Bacteria.
DR   eggNOG; COG0344; LUCA.
DR   HOGENOM; HOG000283806; -.
DR   KO; K08591; -.
DR   OMA; HSQYPKI; -.
DR   OrthoDB; POG091H01XN; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001485; 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; C5BHG2.
DR   SWISS-2DPAGE; C5BHG2.
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    222       Glycerol-3-phosphate acyltransferase.
FT                                /FTId=PRO_1000213409.
FT   TRANSMEM      5     25       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
FT   TRANSMEM     53     73       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
FT   TRANSMEM     80    100       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
FT   TRANSMEM    112    132       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
FT   TRANSMEM    138    158       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01043}.
SQ   SEQUENCE   222 AA;  23893 MW;  EBE17A2998C6212D CRC64;
     MSATALGMII FAYLCGSISS AILVCKAAGL PDPRENGSGN PGATNVLRNG GRLAAAAVLI
     FDVLKGMIPV WLAYTLEMSP FYLGLTAIAA CLGHIYPVFF RFRGGKGVAT AFGAIAPIGW
     DLTGLMVGTW LLTVLLSGYS SLGAIVSALI APFYVWWFKP QFTFPVAMLS CLILVRHHDN
     IQRLWRGKEG KIWRKKGAKS AQNSERPASA SPPHDDEPQT PR
//

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