ID E6SKL7_THEM7 Unreviewed; 203 AA.
AC E6SKL7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN OrderedLocusNames=Tmar_1112 {ECO:0000313|EMBL:ADU51225.1};
OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 /
OS 7p75a).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU51225.1, ECO:0000313|Proteomes:UP000008915};
RN [1] {ECO:0000313|EMBL:ADU51225.1, ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX PubMed=21304738;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75a).";
RL Stand. Genomic Sci. 3:337-345(2010).
RN [2] {ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX DOI=10.4056/sigs.1373474;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S.,
RA Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75aT).";
RL Stand. Genomic Sci. 3:337-345(2010).
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 ECO:0000256|RuleBase:RU361267};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004728}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC ECO:0000256|RuleBase:RU361267}.
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DR EMBL; CP002344; ADU51225.1; -; Genomic_DNA.
DR RefSeq; WP_013495530.1; NC_014831.1.
DR AlphaFoldDB; E6SKL7; -.
DR STRING; 644966.Tmar_1112; -.
DR KEGG; tmr:Tmar_1112; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_5_9; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000008915; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW ECO:0000313|EMBL:ADU51225.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Reference proteome {ECO:0000313|Proteomes:UP000008915};
KW Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:ADU51225.1}.
FT DOMAIN 34..145
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 203 AA; 22296 MW; 8E667379375193EF CRC64;
MLYRVGKVLF QLLFALGYRW DVRGVENVPA GGPLLVIANH FSWLDPPLVG TVLPRNVHFM
AKQELFRNPL AAWVLRRLGA FPVRRGQPDR WALRQALELL EQGRVVGLFP EGTRSRGPLR
PFEPGAALLA VKSGAPVLPV AIIGPYKLGR PVRVRIGTPF RVERGGGEGS IEAVADRMRK
AIAALLAEEP APGRQGRRRI PAG
//
