ID A0A0F6A0I0_9GAMM Unreviewed; 810 AA.
AC A0A0F6A0I0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=RN22_06145 {ECO:0000313|EMBL:KKD61374.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD61374.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD61374.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD61374.1,
RC ECO:0000313|Proteomes:UP000033732};
RA Adrian T.-G.-S., Chan K.-G.;
RT "Genome sequencing of Grimontia sp. AD028.";
RL Submitted (APR-2015) 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:KKD61374.1}.
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DR EMBL; LASY01000025; KKD61374.1; -; Genomic_DNA.
DR RefSeq; WP_046303552.1; NZ_LASY01000025.1.
DR AlphaFoldDB; A0A0F6A0I0; -.
DR PATRIC; fig|1581149.3.peg.1780; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000033732; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 301..428
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 306..311
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 810 AA; 91440 MW; B0A4FFDEB395093E CRC64;
MSACQSIYHK LLNLPLSVLV KTISIPSDPI NQLDLDLSRP MVYVLPFRSH TDLLTLRSSC
LQLGLPDPLE PLELGGKSLP RYVCVSEGKR MFKDSDPVPA DSLTLFTEWL ELHKRDTELD
IQMVPASVVW NRDPGNESRP AAPALQAMNG LQKCYTIFTL GRDSMVRFSN AVSLRFMADK
HGTDTTIANK LARVAKIHFS RQKMAASGPG LPDRQLLFKR LLASKAIDKA VQDEAASRDV
PVEKVRKEAI DMMEEIAADF SPSLIRYADR LLTWLWNKLY QGLNINNSER VRKLAQDGHE
IVYVPCHRSH MDYLLLSYVL YKEGLVPPHI AAGVNLNFFP AGPIFRRGGA FFLRRTFKGN
RLYSTVFREY LAELFAKGYS VEYFSEGGRS RTGRLLPAKT GMLAMTIQAM LRGLKRPVTL
VPVYIGYEHV MEVSTYAKEL QGKRKEKESF GQVLGILRKL RNYGKGYVNF GEPIPVNHFL
NEKAPDWQKD IDPIEPQRPD WLLPAVNELA ERMMTKINDA AAANALTLCA TALLASRQSA
LSREALEEQL TIYLELLRQV PYSATSTVPD DSAQELVEHA LSLNKFVVEK DSLGEVISLD
RQQAILMTFY RNNIIHLFAV PSLIAQMLVF KTRVSRENLM DSIRQLYPLL KAELFMSFDD
AALQSYIDAT LIELERQSLI TVDGDTISRN NGKLTQLQLL GRTIAETLQR YAITLTLFSH
EPDTSKSDLE QQSQMMAQRL SRLHGINAPE FFDKGVFATL LNSLREQGYL NDDDHARADR
VEALRECVFG LISPEVQLTI QAILNQPSED
//
