ID A0A1H6ZI34_9DEIO Unreviewed; 230 AA.
AC A0A1H6ZI34;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:SEJ49220.1};
GN ORFNames=SAMN04488058_10950 {ECO:0000313|EMBL:SEJ49220.1};
OS Deinococcus reticulitermitis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=856736 {ECO:0000313|EMBL:SEJ49220.1, ECO:0000313|Proteomes:UP000199223};
RN [1] {ECO:0000313|Proteomes:UP000199223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10218 {ECO:0000313|Proteomes:UP000199223};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNZA01000009; SEJ49220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6ZI34; -.
DR STRING; 856736.SAMN04488058_10950; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000199223; 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:SEJ49220.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:SEJ49220.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..176
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 230 AA; 25089 MW; 5F32E4C9B0FE4A4F CRC64;
MSGAPPPDEQ RPDEQRLHFP GLRTAFFLGV VRPLLLLGFG VGVRHRERLP ARGPALVVAN
HNSHLDTLLL LSLFSSRTLP LVRPVAAGDY FGRSRALRWL TREIVGGLLI DRAPSGGRRD
PLAPVMAALG RGEIVLLFPE GTRGEPEVRA EFKSGVAHLA RRRPDVPVVP VGLRGLGYAL
PKGEWLPVPL NLYVAVGEAL TPGADRRAFM AQLEAAMEAL DAELPRLHWD
//
