ID   PLSY_ROSDO              Reviewed;         200 AA.
AC   Q163C2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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}; OrderedLocusNames=RD1_3430;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000362; ABG32921.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q163C2; -.
DR   SMR; Q163C2; -.
DR   STRING; 375451.RD1_3430; -.
DR   EnsemblBacteria; ABG32921; ABG32921; RD1_3430.
DR   KEGG; rde:RD1_3430; -.
DR   eggNOG; COG0344; Bacteria.
DR   HOGENOM; CLU_081254_1_0_5; -.
DR   OMA; WRHRGNL; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000007029; 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: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;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..200
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000250328"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ   SEQUENCE   200 AA;  20360 MW;  688E055E28EF3BE2 CRC64;
     MIESTLPALA LWGVIGYLLG SIPFGMVLAK VMGLGNLRDI GSGNIGATNV LRTGNKLAAA
     LTLVLDGGKG VVAVLAARAA GGEDLAQIAG LMAMIGHCYP VWLRFAGGKG VATFLGIVLA
     LAFPVGVGCC LAWLAGAFAT RISSMGALVA SVAAVPLAFL LGFPGAVVLL ILLGALIFWR
     HRGNIARIRT GTEPKIGQKK