ID A0A0D5VDD0_9BURK Unreviewed; 264 AA.
AC A0A0D5VDD0; A0A2T1B1I9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:PRZ54711.1};
GN ORFNames=BX589_106250 {ECO:0000313|EMBL:PRZ54711.1};
OS Paraburkholderia fungorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=134537 {ECO:0000313|EMBL:PRZ54711.1, ECO:0000313|Proteomes:UP000238376};
RN [1] {ECO:0000313|EMBL:PRZ54711.1, ECO:0000313|Proteomes:UP000238376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28183 {ECO:0000313|EMBL:PRZ54711.1,
RC ECO:0000313|Proteomes:UP000238376};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PRZ54711.1}.
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DR EMBL; PVZM01000006; PRZ54711.1; -; Genomic_DNA.
DR RefSeq; WP_028200134.1; NZ_QFRC01000089.1.
DR STRING; 134537.OI25_2361; -.
DR GeneID; 66516325; -.
DR KEGG; bfn:OI25_2361; -.
DR OrthoDB; 9812274at2; -.
DR Proteomes; UP000238376; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:PRZ54711.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:PRZ54711.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..195
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 264 AA; 29216 MW; 7C38D59B794368A9 CRC64;
MNRRLDYVWR FCATGMAFVV FGVCGLLFSV LVFPLAWLWP HRASRQLAVT TVIHWFFRAL
VAVLRCIGVM ELEVSGAQAL RAGAPAIVVA NHPTYLDVMV LLSLTPRACC VVKNAHWGNP
CFWGIVRSAE YVSNADPSEL VEAGARQLAA GYTMIIFPEG TRSPAPNRLH AFSRGFAHMA
LKVGAPIVPV LMDCDPPAFT KQMRWYDVPA RAFRIRVNVL EPFGVEQLAD HDTSPSLAAR
SVTSAIEAHI TQHLFDYGFF KTGN
//