ID F3L552_9GAMM Unreviewed; 519 AA.
AC F3L552;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00016139, ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211, ECO:0000256|RuleBase:RU361267};
GN ORFNames=EYZ66_01690 {ECO:0000313|EMBL:QHJ87090.1}, IMCC3088_2831
GN {ECO:0000313|EMBL:EGG28553.1};
OS Aequoribacter fuscus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Aequoribacter.
OX NCBI_TaxID=2518989 {ECO:0000313|EMBL:EGG28553.1, ECO:0000313|Proteomes:UP000005615};
RN [1] {ECO:0000313|EMBL:EGG28553.1, ECO:0000313|Proteomes:UP000005615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG28553.1,
RC ECO:0000313|Proteomes:UP000005615};
RX PubMed=21551310; DOI=10.1128/JB.05111-11;
RA Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.;
RT "Genome sequence of strain IMCC3088, a proteorhodopsin-containing marine
RT bacterium belonging to the OM60/NOR5 clade.";
RL J. Bacteriol. 193:3415-3416(2011).
RN [2] {ECO:0000313|EMBL:QHJ87090.1, ECO:0000313|Proteomes:UP000464557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3088 {ECO:0000313|EMBL:QHJ87090.1,
RC ECO:0000313|Proteomes:UP000464557};
RA Li S.-H.;
RT "Halieaceae_genomes.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141,
CC ECO:0000256|RuleBase:RU361267};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004728}.
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|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC ECO:0000256|RuleBase:RU361267}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEIG01000095; EGG28553.1; -; Genomic_DNA.
DR EMBL; CP036423; QHJ87090.1; -; Genomic_DNA.
DR RefSeq; WP_009576976.1; NZ_CP036423.1.
DR AlphaFoldDB; F3L552; -.
DR STRING; 2518989.IMCC3088_2831; -.
DR KEGG; afus:EYZ66_01690; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0560; Bacteria.
DR OrthoDB; 9784466at2; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000005615; Unassembled WGS sequence.
DR Proteomes; UP000464557; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02612; HAD_PGPPase; 1.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.1440.100; SG protein - dephosphorylation function; 1.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006385; HAD_hydro_SerB1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR NCBIfam; TIGR01490; HAD-SF-IB-hyp1; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF12710; HAD; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW ECO:0000313|EMBL:EGG28553.1}; Hydrolase {ECO:0000313|EMBL:QHJ87090.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Reference proteome {ECO:0000313|Proteomes:UP000005615};
KW Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:EGG28553.1}.
FT DOMAIN 308..423
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 475..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56525 MW; ED461C3B8E623AC5 CRC64;
MSKINELIGA IEAAPKGPKT AALFDFDGTI IYGYSAFHFL RAQVMKGDLD IKDLMSTLQA
MTQFGFGNID FASLIALTAQ FMAGYSKTDY DTFAQTVYDK HIGRLVYPEA RQLIDAHKAA
GHTIALVSSA TRFQVEPAAR DLGIDHIYCT ELAVNNDTFT GDIDGPPCFG TGKVDAAKKL
LKQTKGRLAN TFFYSDSTDD SELLIASGHP VALNPSRALR EMARENHWAQ ASFDSRGTPT
LSQFIRSLAA TTSVVSAFAA GIPVFALTGS MRQSRNFSYA LFAETASALV GLELDVKGEA
NIWKQRPAVF IFNHQSKTDV IIAAKLVRQD MAGVGKQEIK KLPIIGKVME WGGVVMIDRK
NAESAIAAMK PLVDVMQNEG KSVVLAPEGT RSTTRKLGAF KKGAFHLAMQ AGVPIVPIVI
HNASDIAPKG DFVFRPGKVR VEVLEPIETK HWRLEDIDQH VNDVRQLYLE ALGQAEPSAA
KNNTPATQSK ARKPRATKTR NSLAKSSARG VKTRNESNH
//
