ID   PLSY_RHOPA              Reviewed;         203 AA.
AC   P60929;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=RPA3119;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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}.
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DR   EMBL; BX572603; CAE28560.1; -; Genomic_DNA.
DR   RefSeq; WP_011158664.1; NC_005296.1.
DR   AlphaFoldDB; P60929; -.
DR   SMR; P60929; -.
DR   STRING; 258594.RPA3119; -.
DR   PRIDE; P60929; -.
DR   EnsemblBacteria; CAE28560; CAE28560; RPA3119.
DR   GeneID; 66894201; -.
DR   KEGG; rpa:RPA3119; -.
DR   eggNOG; COG0344; Bacteria.
DR   HOGENOM; CLU_081254_1_0_5; -.
DR   OMA; WRHRGNL; -.
DR   PhylomeDB; P60929; -.
DR   BioCyc; RPAL258594:TX73_RS15905-MON; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001426; 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..203
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000188438"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        118..138
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   203 AA;  21526 MW;  F8592B72123C8B7E CRC64;
     MMIGIYIAAL VIGYLFGSIP FGLILTKIAG TQDLRSIGSG NIGATNVLRT GRKGLAAATL
     LLDALKGTAA VIVAAYLASG TDAIAANAAM LAALGAFLGH LFPVWLKFKG GKGVAVYIGV
     LIGLFWPAAV VFCIMWLATA FTSRYSSLSA LVASFVTPIF LWWFGHDSLA SLFAVLTLLL
     FWMHRENIKR LQAGTESKIG QKK