ID V9XK97_9NOCA Unreviewed; 476 AA.
AC V9XK97;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN ORFNames=Y013_20190 {ECO:0000313|EMBL:AHD22783.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD22783.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD22783.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD22783.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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}.
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DR EMBL; CP006996; AHD22783.1; -; Genomic_DNA.
DR RefSeq; WP_024103038.1; NC_023150.1.
DR AlphaFoldDB; V9XK97; -.
DR GeneID; 29938575; -.
DR KEGG; rpy:Y013_20190; -.
DR PATRIC; fig|1435356.3.peg.4065; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_027938_11_1_11; -.
DR Proteomes; UP000018781; 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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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 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 Transferase {ECO:0000256|RuleBase:RU361267}.
FT DOMAIN 307..421
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 476 AA; 51739 MW; A4D62AD817AC6FB9 CRC64;
MNLEQALERV RTGPQGPEVA AFFDFDGTIV HGFSGVHFFR DRVLAGKVSA SELAATMING
IRGTETEEDF ERFVAIAFKA WRGHTEDELY EIGHRLFMTT IAGHLYPEAW QLIGAHQNAG
HTVVIASSAS RYQIQAAGDA LGVEHILFTP LEVENGVLTG RVDGKSLWRS GKAEAARNFV
ETHGIDAEAS YTYSNGGEDV EFLAVAGNPT ATNPDRTLTR FAIERDWPIM RFRPRGTPGA
RELVRTAAAY GGMFGSVWTG LGLGLINRSR KTALDSIISI GTEVSLALAG VNVRIVGEAN
AWAARPAVFI FNHQSQLDPV VLAKVLRQDF TGVTKKEMAN DPLFGPLLRF VGATFVDRTN
TERAVAALGP VVDTLREGTS IVIAPEGTRS LTPAIGRFKK GAFHIAMQAG VPIVPVVIRN
AGEILWKHST LLRSGTVDVA VLEPIDVSGW SRENLGEHIA EVEDLYRRTL SSWPTD
//
