ID L0A300_DEIPD Unreviewed; 277 AA.
AC L0A300;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:AFZ68268.1};
GN OrderedLocusNames=Deipe_2804 {ECO:0000313|EMBL:AFZ68268.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ68268.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) 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; CP003382; AFZ68268.1; -; Genomic_DNA.
DR RefSeq; WP_015236570.1; NC_019793.1.
DR AlphaFoldDB; L0A300; -.
DR STRING; 937777.Deipe_2804; -.
DR KEGG; dpd:Deipe_2804; -.
DR PATRIC; fig|937777.3.peg.2817; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_1003713_0_0_0; -.
DR Proteomes; UP000010467; Chromosome.
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:AFZ68268.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010467};
KW Transferase {ECO:0000313|EMBL:AFZ68268.1}.
FT DOMAIN 66..178
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 277 AA; 31547 MW; C6AADC33392E8F72 CRC64;
MRGRLRHLLL GRTLLWQTAH CLKRLPETLS PAERDAAQKQ ASARLLRHLR VQLDTTGLEH
IMDGPYLVVP LHEGIADVLC LAQLPLPLRF VARDEIFNWP HVGPAIRRLG HVSINPESGA
RGYRELLRRA EGILKGGESL AMFPQGSLLG IETDFQRGAF VLARQLNVPL LPVVMTGAHR
VWEHPFTPRL RYGVRVGMRV LPPTPAPDGH RYTPDELRLT LRQLMKRHAL DGSMPAPRRY
RPERDGFWDG FRFDIDPDFP ELHHQIAERR RSHGPAA
//
