ID A0A091AX11_9GAMM Unreviewed; 857 AA.
AC A0A091AX11;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=N789_07730 {ECO:0000313|EMBL:KFN43827.1};
OS Arenimonas oryziterrae DSM 21050 = YC6267.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121015 {ECO:0000313|EMBL:KFN43827.1, ECO:0000313|Proteomes:UP000029385};
RN [1] {ECO:0000313|EMBL:KFN43827.1, ECO:0000313|Proteomes:UP000029385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6267 {ECO:0000313|EMBL:KFN43827.1,
RC ECO:0000313|Proteomes:UP000029385};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas oryziterrae.";
RL Submitted (SEP-2013) 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:KFN43827.1}.
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DR EMBL; AVCI01000004; KFN43827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091AX11; -.
DR STRING; 1121015.GCA_000420545_01997; -.
DR PATRIC; fig|1121015.4.peg.1036; -.
DR eggNOG; COG2937; Bacteria.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000029385; 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:UP000029385};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 323..450
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 328..333
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 857 AA; 95986 MW; 264BD63D578921A0 CRC64;
MTEQPSLPLP PPPAPTPPPA PAGKRARPPL WARLIEKLLV PWIEIKREPA VPPFTLDRPV
CYVLENYGLS NTLILDRACR EAGLPSPLAT LPGDPLGRKR AYVALSRRGG GLWTRPKNKN
HSDGLSRLLM AHRLYPDQDV QVVPVSIFVG RAPSRQSGWF SVLFSENWAL VGRFRRLLAI
LLNGRDTVVQ FSPSVRVWEI LDEDLPHERT VRKVSRMLRA HFRKIRSAVI GPDLSTRRLL
VDRVLDAEPV RKAIADQARR DGSEYLEAWK KAHGFAWEIA ADYSNPVVRS ASFALTGFWN
RIYDGVDVHH LDKLKQIAPG HEVVYVPCHR SHMDYLLLSY LLYTHGIVPP HIVAGINLNM
PVIGSILRRG GAFFIRRSIR GNALYAVVLG EYVAQLVGEG FSIEYFIEGG RSRTGRLLAP
KGGMIAMTLK AFLRAPRRPV VFQPVYIGYE KVIEGKSYLD ELTGQPKQKE TIWALIRGVF
EILREHYGKV TVNFGEPVFM DAMLAKNAPD WRETADTDDK PAWFNDTVDE LAHQIQVNIN
RAADVNPINL LALALLSTPK HAMAESDLLA QLALSKKLLA ALPYSDRVTV TAKSPEEIIV
YGEKIGVLTR RKHPLGDVIG VEGETAVLQS YFRNNSLHLF SAAAWIALCF QNNRRLSRSS
LLRLGKTIYP FIQEELFLPW NEDEFSERLN ATIDLFIAEG LLSQVNEGED GYIARGPGQT
DEVFRLRAVA HSLQQAFERY FIAITTLVKN GPRTLSAGEL ETLCHLAAQR LSLLYAPAAP
EFFDKSLFRG FIGKLRELKL VWLCPNGKLD FDERLNTWEK DAKLVLSREL RHTITKISPE
AVSKVAAGAA GAAESKA
//
