ID A0A2U1JJW5_9FLAO Unreviewed; 245 AA.
AC A0A2U1JJW5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:PWA05163.1};
GN ORFNames=DB895_07590 {ECO:0000313|EMBL:PWA05163.1};
OS Flavobacterium psychrotolerans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2169410 {ECO:0000313|EMBL:PWA05163.1, ECO:0000313|Proteomes:UP000245449};
RN [1] {ECO:0000313|EMBL:PWA05163.1, ECO:0000313|Proteomes:UP000245449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB1R5 {ECO:0000313|EMBL:PWA05163.1,
RC ECO:0000313|Proteomes:UP000245449};
RA Liu Q., Xin Y.-H.;
RT "Flavobacterium sp. nov., isolated from glacier ice.";
RL Submitted (APR-2018) 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:PWA05163.1}.
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DR EMBL; QCZI01000008; PWA05163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1JJW5; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000245449; 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:PWA05163.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245449};
KW Transferase {ECO:0000313|EMBL:PWA05163.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
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 245 AA; 27841 MW; 98D8064E1C3F2E0A CRC64;
MQKIISYPIS LIALLTFLLA LVFFHPIQWI CFNLFGYQAH KKSVDYLNFV LLRIGHLLGS
SYVFKNRESI PKGVPIIFVA NHQSLYDIIA MIWFLRKFHP KFVSKKELGK GVPSVSYNLR
HGGSVLIDRK DPKQAVPTIK ALSEYIELHK RSAVIFPEGT RSKTGAPKEF SQTGLKILCK
YAPSAYVVPI SINNSWKIFK YGFFPLGLGN RLTFTVHKAL SVKDLSFEEI MKQSEQAIVR
GIHVV
//
