PLSY_AQUAE
ID PLSY_AQUAE Reviewed; 192 AA.
AC O66905;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=aq_676;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06869.1; -; Genomic_DNA.
DR PIR; E70359; E70359.
DR RefSeq; NP_213465.1; NC_000918.1.
DR RefSeq; WP_010880403.1; NC_000918.1.
DR PDB; 5XJ5; X-ray; 1.48 A; A=3-192.
DR PDB; 5XJ6; X-ray; 2.37 A; A=3-192.
DR PDB; 5XJ7; X-ray; 1.77 A; A=3-192.
DR PDB; 5XJ8; X-ray; 2.41 A; A/B=3-192.
DR PDB; 5XJ9; X-ray; 1.83 A; A=3-192.
DR PDB; 7CQM; X-ray; 1.80 A; A/B=3-192.
DR PDBsum; 5XJ5; -.
DR PDBsum; 5XJ6; -.
DR PDBsum; 5XJ7; -.
DR PDBsum; 5XJ8; -.
DR PDBsum; 5XJ9; -.
DR PDBsum; 7CQM; -.
DR AlphaFoldDB; O66905; -.
DR SMR; O66905; -.
DR STRING; 224324.aq_676; -.
DR EnsemblBacteria; AAC06869; AAC06869; aq_676.
DR KEGG; aae:aq_676; -.
DR PATRIC; fig|224324.8.peg.547; -.
DR eggNOG; COG0344; Bacteria.
DR HOGENOM; CLU_081254_0_0_0; -.
DR InParanoid; O66905; -.
DR OMA; WRHRGNL; -.
DR OrthoDB; 1691856at2; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..192
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188312"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 49..74
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 79..93
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 118..135
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:5XJ5"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:5XJ5"
SQ SEQUENCE 192 AA; 20940 MW; EAD53C4016D63C00 CRC64;
MKALFLVIFA YLLGSITFGE VIAKLKGVDL RNVGSGNVGA TNVTRALGKK YGVLVFFLDF
LKGFIPALIA VKSFGIDSWV LTFTGLASVL GHMYPVFFGF KGGKGVATAL GVVFAVSPSV
ALFSFLVWLG IFLWKRYVSL ASITATISAF LFLFVAGYPV NVLFMAIVIG ALIIYRHREN
INRLLTGREH RF
