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Database: UniProt
Entry: A0A257K9V1_9FLAO
LinkDB: A0A257K9V1_9FLAO
Original site: A0A257K9V1_9FLAO 
ID   A0A257K9V1_9FLAO        Unreviewed;       244 AA.
AC   A0A257K9V1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:OYU84134.1};
GN   ORFNames=CFE24_08200 {ECO:0000313|EMBL:OYU84134.1};
OS   Flavobacterium sp. BFFFF2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2015558 {ECO:0000313|EMBL:OYU84134.1, ECO:0000313|Proteomes:UP000216176};
RN   [1] {ECO:0000313|EMBL:OYU84134.1, ECO:0000313|Proteomes:UP000216176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFFFF2 {ECO:0000313|EMBL:OYU84134.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-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   -!- 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:OYU84134.1}.
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DR   EMBL; NKJD01000020; OYU84134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257K9V1; -.
DR   Proteomes; UP000216176; 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:OYU84134.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216176};
KW   Transferase {ECO:0000313|EMBL:OYU84134.1};
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          76..195
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   244 AA;  27441 MW;  93F715DF5114C9D9 CRC64;
     MERLISYPIS VVYYLSFGLV LVIFHPIQWL CLHLSGYEAH KRSVDYMNFL LIGCSRMLFT
     RYTITGKEKI PFNVPLIIVS NHQSLYDIIG FIWFFRAYHI KYVSKKELGK GIPSVSFNLR
     HGGSALIDRK DPKQALPAIK ALGEYIEKNV RSASIFPEGT RSKNGKTRAF APNGLKILCK
     NAPSAYVVPI TINDSWKMTK FGVFPMGLGS ALQFIVHDPI KVGSCSFEEL LEKTESAVNS
     AIKS
//
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