ID A0A0C1G416_9FLAO Unreviewed; 269 AA.
AC A0A0C1G416;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:KIA98783.1};
GN ORFNames=OA93_07800 {ECO:0000313|EMBL:KIA98783.1};
OS Flavobacterium sp. KMS.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA98783.1, ECO:0000313|Proteomes:UP000031466};
RN [1] {ECO:0000313|EMBL:KIA98783.1, ECO:0000313|Proteomes:UP000031466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:KIA98783.1,
RC ECO:0000313|Proteomes:UP000031466};
RA Smith A.K., Newman J.;
RT "Flavobacterium sp. KMS.";
RL Submitted (OCT-2014) 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 -!- 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:KIA98783.1}.
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; JSYP01000006; KIA98783.1; -; Genomic_DNA.
DR RefSeq; WP_039112589.1; NZ_JSYP01000006.1.
DR AlphaFoldDB; A0A0C1G416; -.
DR STRING; 1566023.OA93_07800; -.
DR OrthoDB; 1450572at2; -.
DR Proteomes; UP000031466; 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:KIA98783.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031466};
KW Transferase {ECO:0000313|EMBL:KIA98783.1}.
FT DOMAIN 53..194
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 269 AA; 31305 MW; CE224C9974BA555B CRC64;
MGLFKRNPFG HILFIKKWLI RVFGAVTHRR YRGFNELQID GSEIIRSLPD TNVLFISNHQ
TYFADVVAMF HVFNASLSGR EDNIKNVGYL WQPKMNIYYV AAKETMRAGL LPRILSYVGA
ITVERTWRAK GVDVTEKREV NPNDTENIKM ALNDGWVITF PQGTTKSFKP VRKGTAHIIK
EHRPIVVPIV IDGFRRSFDK KGLRLKKKGI LQSFIIKEPL VIDYDNETIE EIVEKVEFAI
EQHPSFLKVI PSEELKVQEE LNQMRRWDY
//
