ID A0A0F7JQZ8_9DEIO Unreviewed; 557 AA.
AC A0A0F7JQZ8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE AltName: Full=G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE Short=GPAT {ECO:0000256|HAMAP-Rule:MF_01043};
DE EC=2.3.1.275 {ECO:0000256|HAMAP-Rule:MF_01043};
DE AltName: Full=Lysophosphatidic acid synthase {ECO:0000256|HAMAP-Rule:MF_01043};
DE Short=LPA synthase {ECO:0000256|HAMAP-Rule:MF_01043};
GN Name=plsY {ECO:0000256|HAMAP-Rule:MF_01043};
GN ORFNames=SY84_15440 {ECO:0000313|EMBL:AKH18182.1};
OS Deinococcus soli (ex Cha et al. 2016).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH18182.1, ECO:0000313|Proteomes:UP000034024};
RN [1] {ECO:0000313|EMBL:AKH18182.1, ECO:0000313|Proteomes:UP000034024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N5 {ECO:0000313|EMBL:AKH18182.1,
RC ECO:0000313|Proteomes:UP000034024};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus soli/N5/whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01043};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000256|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000256|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01043};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01043}.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000256|HAMAP-
CC Rule:MF_01043}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01043}.
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DR EMBL; CP011389; AKH18182.1; -; Genomic_DNA.
DR RefSeq; WP_046844749.1; NZ_CP011389.1.
DR AlphaFoldDB; A0A0F7JQZ8; -.
DR KEGG; dch:SY84_15440; -.
DR PATRIC; fig|1309411.5.peg.3150; -.
DR OrthoDB; 9808814at2; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000034024; Chromosome.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01043; PlsY; 1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR30309:SF0; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR30309; INNER MEMBRANE PROTEIN YGIH; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AKH18182.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01043};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01043};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01043};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01043};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_01043};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_01043}; Reference proteome {ECO:0000313|Proteomes:UP000034024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01043};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01043};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01043}.
FT TRANSMEM 111..130
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01043"
FT TRANSMEM 136..164
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01043"
FT TRANSMEM 171..187
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01043"
FT DOMAIN 372..487
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 557 AA; 58756 MW; A256E8F67F7FB81A CRC64;
MLFLSALLLI VAFLTGSAPL GHAVLSRAGV NVRVNNPHNL GVENVLYRVG PQLAAVTALL
DAAKGLLAVL MAASLGQPEV TVMAALAAYL GHLNPPRALY GDTPPRGRGN LVLLGVLAGL
AVTGALPLWV CALPVLVYAA VAGFFGFVSA ATLAGLLAFT LAVATLPLGP AAKLAALGLL
VAATWRFKEN IGRMLDGTEP RLGEAVPLAG RRSDEVVAAF MIHPMNLENF WSARRFAWLR
PLVEKGIVSE RSVRQMADSL RPMKIGELHG IRTVDGKSIR CYLLSSPLLP DVFRDNPDLA
TRRAIEGARL AQELGAEVFG LGAFWSVVGN KGIDVQAAVP ELTITNGGAY TSGTIKAAIP
GILEHFAAEG RDLKHATAAV VGANGVVAFG IARTIAPQVA KLIMIGRDAE RLERTAATLR
RAAKDTEIIA TTSYDTLKDA DLIFTATSDP NPVIFPQHVK PGAWIFDEGR PADVDESVQA
IPGVRVIPGG VVRPPGGMTS NIDLQFGEGQ VPACLAETLI IAATGEHHRK SLGQQTLTEN
INFFVDQAEK LGFQVVD
//
