ID A0A0G1FBL2_9BACT Unreviewed; 239 AA.
AC A0A0G1FBL2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:KKT19483.1};
GN ORFNames=UW04_C0044G0003 {ECO:0000313|EMBL:KKT19483.1};
OS Parcubacteria group bacterium GW2011_GWB1_43_8.
OC Bacteria.
OX NCBI_TaxID=1618874 {ECO:0000313|EMBL:KKT19483.1, ECO:0000313|Proteomes:UP000033953};
RN [1] {ECO:0000313|EMBL:KKT19483.1, ECO:0000313|Proteomes:UP000033953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- 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:KKT19483.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCGU01000044; KKT19483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1FBL2; -.
DR Proteomes; UP000033953; 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:KKT19483.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:KKT19483.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..175
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 239 AA; 27407 MW; 02AE95A25BE38D99 CRC64;
MIKKTAIPIF VQVTLYWVAL IVFKIFLHFK VEGQENLKEI ENDSIIFASN HNSYLDGVFA
AISLPRSSLW PKNFFPIRFL AIDRFFQWNF FPINIIYKLG GAVKITRAKD KKSDNSHLHE
VLAEPIKLLK QREKIWIYPE GGFNDDSTPK KPRNGVTFLH QQTKTPIAPV AIIGNGKILS
TEIFSLKTLA DILKSLLMMN KIKVVFGKPI YSTGDADLDE STDLIMNEIY KLKKQHEII
//
