ID A0A3B7M166_9GAMM Unreviewed; 854 AA.
AC A0A3B7M166;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ECO:0000313|EMBL:AXY59000.1};
GN ORFNames=CDG61_02450 {ECO:0000313|EMBL:AXY59000.1};
OS Acinetobacter sp. WCHAc010052.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=2004647 {ECO:0000313|EMBL:AXY59000.1, ECO:0000313|Proteomes:UP000264387};
RN [1] {ECO:0000313|EMBL:AXY59000.1, ECO:0000313|Proteomes:UP000264387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHAc010052 {ECO:0000313|EMBL:AXY59000.1,
RC ECO:0000313|Proteomes:UP000264387};
RA Hu Y., Long H., Feng Y., Zong Z.;
RT "The complete genome of Acinetobacter sp. strain WCHAc010052.";
RL Submitted (SEP-2018) 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}.
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DR EMBL; CP032143; AXY59000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B7M166; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000264387; Chromosome.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 314..441
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 319..324
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 854 AA; 96730 MW; D33A45AF70C86C0C CRC64;
MSQRGFGQMY RQLSSKLLDL VVTPHVLGEV PAEPTATADS EQTPQKVVCY VLQNYSRSNA
LVVDGETRRL KLPPALDSLN IAAHKEKASI LFLQHHNENN LLNPPLHAFP PRLLRLIEVL
EKHPETDIEL IPVTVLWGRS PDKEDSLLKL LFTDTWATPG TVKQLVNIGL HGRQSYLEFH
QGQSLRQLVD YAKTTHPNLS PATYIANTLN DFLDNEREVV LGPDLSDRRN VMHSLIKSHD
VQDAIRRESI RSKISMIESE RRAIGYLNEI VSDYSHSAVR FADMALTRLW TQLYDGVEVH
NFSTVRELAK DYEIIYTPCH RSHIDYLLLS YVIYKRGMMV PYIAAGDNLN MPFVGQLLRG
GGAFFIRRTF RGNGLYTTVF KEYLYSILSR NTPLEYFIEG GRSRTGRLLP PKTGMLAMTV
HGHLRGRAKP IVFVPTYVGY ERLMEGSTYV GEMNGKPKES ESIIGILKTL RKIERIFGKV
HVNFGEPVFL DDMLKQHNAE QIKIESNDAP VPEAVSAAVN SSANAILENI NRAVVINPVS
LLSLILLATP KHTLDEEICI KQLDTYRNLL TALPYDERTQ VTPLSGKEII AYGLKLKLIK
RVQHVLGDII AIEDNQAILL TYFRNNILHA FVLPSLVAAL VEHNGKISKA DLINVIRTLY
PFLKAELFLK WKDGEIKAQV EEYVNALAQA NLIFVDDADL IYSPTPNSED HNQLKVLAVP
VRQSLERYYM TLALITQRGS GNISIRQVEE LSHLVGQRLS VLYEFNSPEF FDKALFQSFV
KVLTEQGYIK TNEDNAIVFD AQFRNVAQYA NLVLDDVTLQ MLQHITSFTD DELKEALDAL
AAQQAKKRLK RKKK
//
