ID N9V790_9GAMM Unreviewed; 808 AA.
AC N9V790;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=G114_14726 {ECO:0000313|EMBL:ENY71132.1};
OS Aeromonas diversa CDC 2478-85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY71132.1, ECO:0000313|Proteomes:UP000023775};
RN [1] {ECO:0000313|EMBL:ENY71132.1, ECO:0000313|Proteomes:UP000023775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2478-85 {ECO:0000313|EMBL:ENY71132.1,
RC ECO:0000313|Proteomes:UP000023775};
RX PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA Fuste M.C.;
RT "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL Genome Announc. 1:S69-S82(2013).
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:ENY71132.1}.
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DR EMBL; APVG01000043; ENY71132.1; -; Genomic_DNA.
DR RefSeq; WP_005357048.1; NZ_CDCE01000036.1.
DR AlphaFoldDB; N9V790; -.
DR PATRIC; fig|1268237.3.peg.2901; -.
DR eggNOG; COG2937; Bacteria.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000023775; 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 304..431
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 309..314
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 808 AA; 91565 MW; AC41D8744E7F8D05 CRC64;
MSLGQRISRA ALQWPINWLV NHKSLPENPI AELKLDPARP IVFALKTSSI TDLLTLQQCC
ADLGLPGPFT PLELAGRPLP RYVCLDRPPP LFGSRIKPLP FLQEFEQLLD LHKQDPDLDV
QLVPVTLFWG RAPGREEEEV SSFNIISALA PNMLKKALIV ALKGRENLVR FSPPVSLRYM
ADKHGTDQAI AHKLARVARV HFGRQQLAAT GPKLPNRHLL FQQLLDSATI QDAIREEAGR
DSISEEKARK RALGYMDEIA SDFSYRLIRI GDSFLGWLWN KLYRGLSVHG AEKVRQLAQE
GHEIVYVPCH RSHMDYLLLS YVIYHQGMVP PHIAAGINLN FWPAGPLFRR GGAFFIRRTF
KGNPLYSTVF REYLNLLFTK GYSVEFFTEG GRSRTGRLLP PKTGMLAMTL QAMMRGLDRP
LTFVPVYLGY EHVMEVNTYH RELQGSRKEK ESFLQVLGIL KKLRNYGRGF VNFGEPLTLN
NYLSEHVPEW REHIGQEERP EWMSPTVNQL ADLLMTRINA AAAVNGLTLS AVALLASERH
ALTRDELEAQ ITTYLTLLRE VPYGPYNTIP QSSAAELLDQ ALELNKLQVT EDRLGQIISL
DRYQAILLTY YRNNVLHLLA LPSLVAALIE RCEGIGRSEL IGRCVDIYPL LKNELFLHFE
EQALPELIDN LLRAFAAQQL ITERDGGFWV NPGNQMRLLL LAESIQETLQ RYAIVLTRLL
EQPSIEAEQL EADAMMMAER MGTLHGINAP EFFDQKLFTT LIHTFRSEGY LDPSCKPDLG
RFQALADNVL PLLSSKVQRT IRACCPSN
//
