ID C0QLN2_DESAH Unreviewed; 246 AA.
AC C0QLN2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 Name=plsC {ECO:0000313|EMBL:ACN16336.1};
GN OrderedLocusNames=HRM2_32570 {ECO:0000313|EMBL:ACN16336.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN16336.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN16336.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN16336.1; -; Genomic_DNA.
DR RefSeq; WP_015905098.1; NC_012108.1.
DR AlphaFoldDB; C0QLN2; -.
DR STRING; 177437.HRM2_32570; -.
DR KEGG; dat:HRM2_32570; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_6_3_7; -.
DR OrthoDB; 9809618at2; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
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:ACN16336.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:ACN16336.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..197
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 246 AA; 27270 MW; C7202E8E6AB4A8E5 CRC64;
MDAILKAVYQ PYKWLFVFPL MSLSTFFHGV LCMVVVLFFG ADAGNLVAVS WSRLACIVVP
IRVKIMGRHN YSRDKSYVVV ANHQSMVDIP VIHGWLGLRI KWVMKKELKK IPVFGPACQS
LGCIYVDRAD SGAALKSMDE AKNRLFFRGK ITGGAAVLFF PEGTRSRDGR LLAFKKGAFR
FAMDAGLPIL PITIRNSRQI LPSDSLNLSP GEVEIVVHPA VDLSCCTVEV LDETVSQVRC
TIEHAL
//
