ID Q53W57_THET8 Unreviewed; 225 AA.
AC Q53W57;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:BAD71901.1};
GN OrderedLocusNames=TTHB105 {ECO:0000313|EMBL:BAD71901.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27 {ECO:0000313|EMBL:BAD71901.1,
OG ECO:0000313|Proteomes:UP000000532}.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD71901.1, ECO:0000313|Proteomes:UP000000532};
RN [1] {ECO:0000313|EMBL:BAD71901.1, ECO:0000313|Proteomes:UP000000532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RC PLASMID=pTT27 {ECO:0000313|EMBL:BAD71901.1,
RC ECO:0000313|Proteomes:UP000000532};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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; AP008227; BAD71901.1; -; Genomic_DNA.
DR RefSeq; WP_011174498.1; NC_006462.1.
DR RefSeq; YP_145344.1; NC_006462.1.
DR AlphaFoldDB; Q53W57; -.
DR EnsemblBacteria; BAD71901; BAD71901; BAD71901.
DR GeneID; 3169304; -.
DR KEGG; ttj:TTHB105; -.
DR PATRIC; fig|300852.9.peg.2048; -.
DR HOGENOM; CLU_097817_0_0_0; -.
DR Proteomes; UP000000532; Plasmid pTT27.
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:BAD71901.1};
KW Plasmid {ECO:0000313|EMBL:BAD71901.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000532};
KW Transferase {ECO:0000313|EMBL:BAD71901.1}.
FT DOMAIN 47..152
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 225 AA; 25118 MW; BF072710A10B235E CRC64;
MADLWETLKE RPTGKALRLL VEALVLRSLK ESLRGVYLRG EAPEGPLVLA LNHHGFFDGH
LAWLLGKLCR RPLSLLVAEE NLRAYPVLKL AGALEAGRVR EALRRLRRGE WVALFPEGEM
RYPGPLGPLR EGANWLARKA GVPLLPVALR VVLRGYEHPE AFLWVGRPLP PGGDLGRALG
GLLQALDALL AKTHPREVPE GFREVLRGRR SLEERVLPLV RLLRP
//
