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
//