ID B3R2E1_CUPTR Unreviewed; 208 AA.
AC B3R2E1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:CAQ69658.1};
GN OrderedLocusNames=RALTA_A1715 {ECO:0000313|EMBL:CAQ69658.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ69658.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ69658.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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DR EMBL; CU633749; CAQ69658.1; -; Genomic_DNA.
DR RefSeq; WP_012352978.1; NC_010528.1.
DR AlphaFoldDB; B3R2E1; -.
DR GeneID; 29761460; -.
DR KEGG; cti:RALTA_A1715; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_8_1_4; -.
DR BioCyc; CTAI977880:RALTA_RS08255-MONOMER; -.
DR Proteomes; UP000001692; Chromosome 1.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
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 SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:CAQ69658.1};
KW Transferase {ECO:0000313|EMBL:CAQ69658.1}.
FT DOMAIN 35..157
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 208 AA; 22967 MW; F37D8402BDB7FCAA CRC64;
MWLARATARA IIVFARLLTG MRANWQGCIP AAVQRVYFAN HSSHGDFVLI WGCLPPDLRA
VTRPVAGADY WQTSPLRRFI GRDVFRALLI DRTRSDPGCD PVALMQAGLA AGDSLILFPE
GTRNTTDARL LPFKSGIYHL ARACPEVEFV PVWIDNLNRV MPKGEVVPVP LLCTVTFGQP
LRLAADDSKE AFLARCREGL LALAPELE
//
