ID A0A8A0RIU0_9FIRM Unreviewed; 189 AA. AC A0A8A0RIU0; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 12-OCT-2022, entry version 4. 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_2 {ECO:0000313|EMBL:QSQ08205.1}; GN Synonyms=plsY {ECO:0000256|HAMAP-Rule:MF_01043}; GN ORFNames=H0A61_00525 {ECO:0000313|EMBL:QSQ08205.1}; OS Koleobacter methoxysyntrophicus. OC Bacteria; Firmicutes; Clostridia; Koleobacterales; Koleobacteraceae; OC Koleobacter. OX NCBI_TaxID=2751313 {ECO:0000313|EMBL:QSQ08205.1, ECO:0000313|Proteomes:UP000662904}; RN [1] {ECO:0000313|EMBL:QSQ08205.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRmbB1 {ECO:0000313|EMBL:QSQ08205.1}; RA Sakamoto S., Tamaki H.; RT "Koleobacter methoxysyntrophicus gen. nov., sp. nov., a novel anaerobic RT bacterium isolated from deep subsurface oil field and proposal of RT Koleobacterales ord. nov. in the phylum Firmicutes."; RL Submitted (JUL-2020) 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 --------------------------------------------------------------------------- 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; CP059066; QSQ08205.1; -; Genomic_DNA. DR KEGG; kme:H0A61_00525; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000662904; 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. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:QSQ08205.1}; 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:UP000662904}; 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 6..27 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01043" FT TRANSMEM 48..72 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01043" FT TRANSMEM 78..98 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01043" FT TRANSMEM 110..135 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01043" FT TRANSMEM 147..175 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01043" SQ SEQUENCE 189 AA; 20724 MW; 5CAD38C9BD9EB0E2 CRC64; MKAMMFLVLS YILGSIPSAF VVTKIITGRD IRKIGSGNVG TMNTLRHVGL IPGIMTFLID FSKGALATWA ALSSTQSYFI VYASALFVMI GHNWPLLLRF KGGKGLAATA GSLAVINIKI CVIVYTVIGI TSLLLKNTDR ASIIGFLVYP FLLFLIYNNF QIFVIGLVHF SLVFIRHYPG LKKGKMLIT //