ID A0A2K8X6J4_9FLAO Unreviewed; 249 AA.
AC A0A2K8X6J4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:AUC78523.1};
GN ORFNames=CW736_03505 {ECO:0000313|EMBL:AUC78523.1};
OS Nonlabens sp. MB-3u-79.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=2058134 {ECO:0000313|EMBL:AUC78523.1, ECO:0000313|Proteomes:UP000232401};
RN [1] {ECO:0000313|EMBL:AUC78523.1, ECO:0000313|Proteomes:UP000232401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB-3u-79 {ECO:0000313|EMBL:AUC78523.1,
RC ECO:0000313|Proteomes:UP000232401};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-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};
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DR EMBL; CP025116; AUC78523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8X6J4; -.
DR KEGG; nob:CW736_03505; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000232401; Chromosome.
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:AUC78523.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000232401};
KW Transferase {ECO:0000313|EMBL:AUC78523.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
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 249 AA; 28684 MW; 21EA51778451B519 CRC64;
MQKIISYPLT VIHIIVFFLL LIIFHPIQMI CYKLGGYNAH RKSVYILNWF LMQSQLPLLN
TFSINYKTDL PPGPSYIFVC NHQSMFDIPP LIYYLRHYHA KFIAKKELAK GIPSISLNLR
IGENCSIDRK DRKQAITALI KFAKNVYEKK RSVVIFAEGT RSRTGVPKSF QTNGLKTIFK
YVPDAVVVPV TINNSWKINR YGKFPYGIGN KIKLTIHEPI PIQGRDHEEL ILETQEVIHN
SITSTAFKS
//