ID A0A0A3AM14_9PAST Unreviewed; 810 AA.
AC A0A0A3AM14;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=OA57_05845 {ECO:0000313|EMBL:KGQ70376.1};
OS Chelonobacter oris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Chelonobacter.
OX NCBI_TaxID=505317 {ECO:0000313|EMBL:KGQ70376.1, ECO:0000313|Proteomes:UP000030380};
RN [1] {ECO:0000313|EMBL:KGQ70376.1, ECO:0000313|Proteomes:UP000030380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1662 {ECO:0000313|EMBL:KGQ70376.1,
RC ECO:0000313|Proteomes:UP000030380};
RA Kudirkiene E., Hansen M.J., Bojesen A.M.;
RT "Draft genome sequence of Chelonobacter oris 1662T, associated with
RT respiratory disease in Hermann's Tortoises.";
RL Submitted (NOV-2014) 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:KGQ70376.1}.
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DR EMBL; JSUM01000010; KGQ70376.1; -; Genomic_DNA.
DR RefSeq; WP_034614806.1; NZ_JSUM01000010.1.
DR AlphaFoldDB; A0A0A3AM14; -.
DR STRING; 505317.OA57_05845; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000030380; 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:UP000030380};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 298..425
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 303..308
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 810 AA; 92465 MW; 4F5B76E9F12091D4 CRC64;
MSIFLDTYRK ALDFMLSLLV KSNPIPSDPV NELELDRQKC FLYLLPYTSQ TDLLILRRHC
LQLGLPDPLA RNKINGDSLP RFVFLDRGRR FFKSNQLTEN TRALFSKYFE LHRSHSELDV
QLVPVSVLWG RSPGHEKKLP HLRFLGRLQK LWAIAWFGRD NFVRFSKAVS LRDMANLKGS
DDDIALKLTR VAKIHFSKQR TSATGPRLPN RQAMFRQILQ SSAVQEAIAD EAKSKKIDHD
KATANAEAML NEIAANVSHE SLRLADRFLR WLWNKLYRGI DVKNGDRVRK LAIEGHEIVY
IPCHRSHIDY LLLSYILYHQ GLVPPHIAAG INLNFWPVGG RFRRWGAFFI RRTFSGNRLY
STVFRQYLSE LFRRGYAVEF FIEGGRSRTG RLLAPKTGML SMTLQALLEG HTRPISLVPV
YIGYEHVLEV DTYAKELRGA AKEKENAGLV LRVIKKLRNM GKGYVNFGEP ITLNTYLNQH
YPNWKESEGE ESKAWLGGAV DKLAVQVMRN INKAAAINAM NLIGTVLLAS RQRALAREQL
LSQLSIYQQL LNNVAYSRDV IVPQESPQAM LEHVLSLDKV GIIQEKDSFG EIIRLERSSA
VLMTYYRNNI QHLFVLPSLI ASIVIHHEAI QQSLLIDAVQ KIYPFLKSEL FLDIDENRLK
PWIKQILAEL QRQALINLHD EMVGINKRNI RSLQLLSAGI REIIQRYYIT LNFLQAEPTI
SRSNLEKESQ SVAQRLSVLH GINAPEFFDK AVFSTFIASL KENGYFTEQG GADSAKVEEL
AASLKALLSS EVYMTISSSV ESAVEKNKPE
//
