ID A0A091BCU6_9GAMM Unreviewed; 836 AA.
AC A0A091BCU6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=P873_10405 {ECO:0000313|EMBL:KFN49556.1};
OS Arenimonas composti TR7-09 = DSM 18010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121013 {ECO:0000313|EMBL:KFN49556.1, ECO:0000313|Proteomes:UP000029391};
RN [1] {ECO:0000313|EMBL:KFN49556.1, ECO:0000313|Proteomes:UP000029391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR7-09 {ECO:0000313|EMBL:KFN49556.1,
RC ECO:0000313|Proteomes:UP000029391};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas composti.";
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:KFN49556.1}.
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DR EMBL; AWXU01000033; KFN49556.1; -; Genomic_DNA.
DR RefSeq; WP_051240032.1; NZ_AWXU01000033.1.
DR AlphaFoldDB; A0A091BCU6; -.
DR STRING; 1121013.GCA_000426365_02507; -.
DR eggNOG; COG2937; Bacteria.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000029391; 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:UP000029391};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 313..440
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 318..323
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 836 AA; 93873 MW; B5B49876BEBB7FE8 CRC64;
MDSPSPPAPR PSLQTARPPL WARLMEKLLQ PWIEIHREPD IPPFQLDRPV CYVIEHYGLS
NTLILDRACR EAGLPSPLAP LPGDPLGRKR AYVALSRRQG GLFRRPKNRR HSDGLSRLLM
AHRLYPDQDV QLVPVSIFVG RAPARQSGWF SVLFSENWAL VGRFRRLLAI LLNGRDTVVQ
FSPSVRVWEI LDEQIPHERQ VRKVARVLRA HFRRIKTAVI GPDLSTRRLL VDHVLDAEPV
RKAIADQARR DNSQYLEAWK KAHAFAWEIA ADYSNPVVRS ASFALTGFWN RIYDGVVVNH
LDSLRQVAPG HEIIYVPSHR SHMDYLLLSY LLYTKGIVPP HIVAGINLNM PVIGPILRRG
GAFFIRRSIR GNALYAAVLA EYVAQLVGEG FSLEYFIEGG RSRTGRLLAP KGGMIAMTLK
AFLRAPRRPV VFQPIYIGYE KLIEGKSYLD ELSGQPKEKE TIWALVKAGA GILRQRYGKV
AVNFGEPIFL DRVLETHAPD WKAQAAEDRP VWLNDAVEDI AHRIQVNINR AADVNPVNLL
ALSVLSTPKH AMSEADLLAQ LALNKKLLAT LPYSERVTVT TLSPAEIIAY GEKMGVLSRT
VHPLGDVLGM EGETAVLQSY FRNNVLHLFS AAAWVALCFQ NNRRMSRAGL LRLGRTIYPF
VQEELFLTWD AEGFAAQLNA TIDLFVGEGL LSVASEDEGG IISRGPGQTD EVFRLRAVAH
SLQQAFERYF IAITTLVKNG PRMLSAGELE TLCQLTAQRL SLLYAPAAPE FFDKSLFRGF
IQKLRELKLV WVAENGKLDF DEQLALWEKD AKVVLGRELR HTIAKLSPEA VREVSS
//
