ID A0A2N4XME8_9RHOO Unreviewed; 253 AA.
AC A0A2N4XME8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:PLK48057.1};
GN ORFNames=C0V76_14030 {ECO:0000313|EMBL:PLK48057.1};
OS Uliginosibacterium sp. TH139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Uliginosibacterium.
OX NCBI_TaxID=2067453 {ECO:0000313|EMBL:PLK48057.1, ECO:0000313|Proteomes:UP000234247};
RN [1] {ECO:0000313|EMBL:PLK48057.1, ECO:0000313|Proteomes:UP000234247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH139 {ECO:0000313|EMBL:PLK48057.1,
RC ECO:0000313|Proteomes:UP000234247};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) 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:PLK48057.1}.
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; PKRR01000006; PLK48057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4XME8; -.
DR InParanoid; A0A2N4XME8; -.
DR OrthoDB; 9812274at2; -.
DR Proteomes; UP000234247; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:PLK48057.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000234247};
KW Transferase {ECO:0000313|EMBL:PLK48057.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..197
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 253 AA; 27952 MW; 5A24DEEFA588B4CC CRC64;
MKSLILLLRR AHAFLALHLG LGSLAAGCLL WTAVALPLNL LLPRQAGILL GRRIAMLGFR
LYLWWLRRLG IGHFDLRALD ALREAGPLII APNHPGLLDA LMVISRLPNV ACVLKAGLLD
NPLWGAGARL AGYVRNDWFI GSINLAVEQL RGGSQLLLFP EGTRTETPPV LNPFRAGTGY
VAHRAGVPIQ TVIIEQDTRF LGKGWPLFRP PVMPMNFRVR LGQRFAPPDD PVAFTAELQD
YFAREMRSPP LPD
//
