ID V2GUT5_9BURK Unreviewed; 208 AA.
AC V2GUT5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:ESH93881.1};
GN ORFNames=B551_0220670 {ECO:0000313|EMBL:ESH93881.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESH93881.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESH93881.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) 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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:ESH93881.1}.
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DR EMBL; AMPR02000429; ESH93881.1; -; Genomic_DNA.
DR RefSeq; WP_023264868.1; NZ_AMPR02000429.1.
DR AlphaFoldDB; V2GUT5; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000053474; Unassembled WGS sequence.
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:ESH93881.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053474};
KW Transferase {ECO:0000313|EMBL:ESH93881.1}.
FT DOMAIN 35..157
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 208 AA; 23089 MW; CD808F7C70D2A515 CRC64;
MWIARVTARA IIVFARLLTG MRANWQGCVP AAVQRVYFAN HSSHGDFVLI WGCLPPELRP
RTRPVAGADY WDRSALRRFI GRDVFRALLI DRTRSDPGSD PVALMRGALE GGDSLILFPE
GTRNTTEARL LPFKSGIFHL ARACPSVEFV PVWIDNLNRV MPKGEIVPVP LLCTVTFGQP
VLLVPDDDKD SFLARCRDGL LALAPVLD
//
