ID F4D155_PSEUX Unreviewed; 258 AA.
AC F4D155;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:AEA26843.1};
GN OrderedLocusNames=Psed_4696 {ECO:0000313|EMBL:AEA26843.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA26843.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA26843.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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};
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DR EMBL; CP002593; AEA26843.1; -; Genomic_DNA.
DR RefSeq; WP_013676755.1; NC_015312.1.
DR AlphaFoldDB; F4D155; -.
DR STRING; 675635.Psed_4696; -.
DR KEGG; pdx:Psed_4696; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_1_11; -.
DR OrthoDB; 9806008at2; -.
DR Proteomes; UP000007809; Chromosome.
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:AEA26843.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809};
KW Transferase {ECO:0000313|EMBL:AEA26843.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..178
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 258 AA; 28036 MW; E09E22B03E286DCC CRC64;
MADTDRPLTV REKLRLTLRR RRSGSGFWYG LGIELIWPFA MFLPKIVFRG GEHVPRSGGA
LLALNHVSFA DPIFDTAFVV ANGRMPRYLA KSELWKVPVV RSVLAGGRHI PVHRATSRAT
DAYRDAVEAL NRGEVVAFYP EGTYTADPDG WPMKAKNGIG RIAVVTGVPV IPVANWGTQE
ALPPGALPRL FPRRRVRVVA GPPVDLSAFV GKPRTRTNLD AATAAIMTDI TKLVADLRGE
QAPDAAYDPG PERPAAAS
//