ID A0A0A2M4M1_9FLAO Unreviewed; 244 AA.
AC A0A0A2M4M1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:KGO83270.1};
GN ORFNames=Q763_04470 {ECO:0000313|EMBL:KGO83270.1};
OS Flavobacterium beibuense F44-8.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1406840 {ECO:0000313|EMBL:KGO83270.1, ECO:0000313|Proteomes:UP000030129};
RN [1] {ECO:0000313|EMBL:KGO83270.1, ECO:0000313|Proteomes:UP000030129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F44-8 {ECO:0000313|EMBL:KGO83270.1,
RC ECO:0000313|Proteomes:UP000030129};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO83270.1}.
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DR EMBL; JRLV01000004; KGO83270.1; -; Genomic_DNA.
DR RefSeq; WP_035131613.1; NZ_JRLV01000004.1.
DR AlphaFoldDB; A0A0A2M4M1; -.
DR STRING; 1406840.Q763_04470; -.
DR eggNOG; COG0204; Bacteria.
DR Proteomes; UP000030129; 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:KGO83270.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030129};
KW Transferase {ECO:0000313|EMBL:KGO83270.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..195
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 244 AA; 27745 MW; BF9F93E73F2BE8FA CRC64;
MGKILSYPIS ILYYLVFLLF LLIFHPVQWV CLNVFGYQAH KKSVDILNFF LVRTTHILGT
SYKFEGIEKV PAGVPLIIVA NHQSMYDIPP IIWFMRKFHP KFISKKELGK GIPSVSYNLR
HGGSVLIDRK DPKQALPAIK QIATYIEKNT RSAVIFPEGT RSKNGKPKKF SENGLKILCK
FAPSAYIVPV SINNSWKLNR YGQYPLGLGA RVTFTVQEPF AIKNIPFEEV MERTENAVVQ
GIKN
//