ID A0A1E2VEF6_9GAMM Unreviewed; 815 AA.
AC A0A1E2VEF6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432, ECO:0000256|HAMAP-Rule:MF_00393};
DE Short=GPAT {ECO:0000256|HAMAP-Rule:MF_00393};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113, ECO:0000256|HAMAP-Rule:MF_00393};
GN Name=plsB {ECO:0000256|HAMAP-Rule:MF_00393};
GN ORFNames=BFW38_11010 {ECO:0000313|EMBL:ODC05379.1};
OS Terasakiispira papahanaumokuakeensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Terasakiispira.
OX NCBI_TaxID=197479 {ECO:0000313|EMBL:ODC05379.1, ECO:0000313|Proteomes:UP000094291};
RN [1] {ECO:0000313|EMBL:ODC05379.1, ECO:0000313|Proteomes:UP000094291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH27A {ECO:0000313|EMBL:ODC05379.1,
RC ECO:0000313|Proteomes:UP000094291};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000510, ECO:0000256|HAMAP-
CC Rule:MF_00393};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|HAMAP-Rule:MF_00393}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00393};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00393};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00393}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|HAMAP-Rule:MF_00393}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODC05379.1}.
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DR EMBL; MDTQ01000001; ODC05379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E2VEF6; -.
DR STRING; 197479.BFW38_11010; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000094291; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR03703; plsB; 1.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00393};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00393}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00393};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW Reference proteome {ECO:0000313|Proteomes:UP000094291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 290..417
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 295..300
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 815 AA; 93698 MW; FDE5CF9B512466D0 CRC64;
MRGILQLWIK PHWSTPGPEQ LELDPTLPVL YVLPRQSYTD RLVLEHVCRQ KGLPDIRPLA
LGDHWLGDNL VYLERPSRRG LSRRSPRLTQ AWEVLQARPQ DDLQVVPVSL FWGRAPGREH
SVMQLITVDS WSVVGRLRRL LRVIIHGRQL YMQWGQPLRL REVLGAQQLQ QKGAAYAINK
SSRLLGLYFR RVRTQVLGPD LSHRRTLVKG LLQSPRVKTA IETQVQQHGI SEQKAYHQAE
RYALEIASNV SYPVIRLLDR FLNWLWNRLY DGVKVHHLER LKDQAGQHTV VYVPCHRSHI
DYLLLSYVLF EHGLMTPHIA AGINLDMPVI GPLLRRGGAF FMRRSFRDNP LYSAVFNEYL
YTLFDRGHPV EYFIEGGRSR TGRTLAPRPG MLAMTLRAAL RGTQKPLVMV PVYIGYEHVL
EGRTYLGELQ GQEKRKESPL DLFRVLNSLR KDFGQVNVTF GEPLHLERFM QAHYPQWRQY
DKHAERPDWL QQAVPELGHE LAVRINQSAS LNPVALVALA LLASPHRALE ESVLVAHMQT
LVQLQRQAPL SPDIVLPEGT AEAWLSKAEK MDIIERVAHP MGDIIRVNES QGVLLTWYRN
NVLHLFALPG LIAYLFMNQR QHSQDRLQTQ VELLYPVLQN ELFLPWQTDQ LTPVVQQMIQ
VMCNNGLLVG HEHQRLRRPP GQTQGMMQLR LLGQLVQPAL ERGYLLLALL DRAGSNVLTR
DMLVEQAQAL AHRLAILQGL NAPEYFDARL FRGLIEAMIK QQLLNQDDTG YLSYDAPLRR
LIHAGRNLFD PRLRHSILQL AWTTPVPHNS ETQAD
//
