ID C6X0P2_FLAB3 Unreviewed; 266 AA.
AC C6X0P2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN OrderedLocusNames=FIC_00466 {ECO:0000313|EMBL:ACU06928.1};
OS Flavobacteriaceae bacterium (strain 3519-10).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU06928.1, ECO:0000313|Proteomes:UP000001512};
RN [1] {ECO:0000313|EMBL:ACU06928.1, ECO:0000313|Proteomes:UP000001512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3519-10 {ECO:0000313|EMBL:ACU06928.1,
RC ECO:0000313|Proteomes:UP000001512};
RX PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA Raymond J.A., Christner B.C., Schuster S.C.;
RT "A bacterial ice-binding protein from the Vostok ice core.";
RL Extremophiles 12:713-717(2008).
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; CP001673; ACU06928.1; -; Genomic_DNA.
DR AlphaFoldDB; C6X0P2; -.
DR STRING; 531844.FIC_00466; -.
DR KEGG; fba:FIC_00466; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_1022137_0_0_10; -.
DR OrthoDB; 1450572at2; -.
DR Proteomes; UP000001512; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001512};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..194
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 266 AA; 30110 MW; F1041A380BD7E2F9 CRC64;
MAKKNIFTDA FGNLYFLKRL IIIILGVVSY RRFNGFNKLK ITGTENLQDL PGSNVLFVSN
HQTYFADVAA MYHAFCAVNN GYLNTIKNPV YLLNPKVDFY YVAAEETMNK GLMTKIFKLA
GAVTVKRTWR AEGSNVNRMV DLTEVENIMK ALDNGWVITF PQGTTSAFAQ GRKGTAKLVK
NQRPIVIPIK INGFRRAFDK KGLRVKVTGV KPTMEFKAPL DIDYDKDDAQ CILNKIMVAI
EQTEDFNLLH DYDLELKAQK SEETLS
//
