ID A0A1M5F048_9FLAO Unreviewed; 278 AA.
AC A0A1M5F048;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:SHF84581.1};
GN ORFNames=SAMN05444344_1666 {ECO:0000313|EMBL:SHF84581.1};
OS Tenacibaculum mesophilum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=104268 {ECO:0000313|EMBL:SHF84581.1, ECO:0000313|Proteomes:UP000183998};
RN [1] {ECO:0000313|EMBL:SHF84581.1, ECO:0000313|Proteomes:UP000183998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13764 {ECO:0000313|EMBL:SHF84581.1,
RC ECO:0000313|Proteomes:UP000183998};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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};
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DR EMBL; FQVV01000002; SHF84581.1; -; Genomic_DNA.
DR RefSeq; WP_047789545.1; NZ_LDOD01000006.1.
DR AlphaFoldDB; A0A1M5F048; -.
DR STRING; 104268.SAMN05444344_1666; -.
DR OrthoDB; 1450572at2; -.
DR Proteomes; UP000183998; 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:SHF84581.1};
KW Transferase {ECO:0000313|EMBL:SHF84581.1}.
FT DOMAIN 53..192
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 278 AA; 32188 MW; DB3DC9084C606598 CRC64;
MPLFKRNPFG HILFIKRFLI QVLGVISHGR YRKFNDLQIE GMDVLRSLPD QKVLFISNHQ
TYFADVAAMF HVFNAALKGR DDNIRNVGYL WKPKLNIYYV AAGETMRSGL LPKIFAYVGS
VSVERTWRSA GKDVNRQVKM SDISNIGKAL DDGWVITFPQ GTTTPFKPIR RGTAHIIKTY
KPIVVPIVID GFRRSFDKKG LMIKKRNVLQ SMVIKEPLEI DYENEDVASI VEKIEYAIEQ
HPSFLKVLTP KQLQEQEEFI EKRRFWGADK PKEKEKKD
//