ID PLSC_BORBU Reviewed; 250 AA.
AC Q59188;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE Short=1-AGP acyltransferase;
DE Short=1-AGPAT;
DE EC=2.3.1.51;
DE AltName: Full=Lysophosphatidic acid acyltransferase;
DE Short=LPAAT;
GN Name=plsC; OrderedLocusNames=BB_0037;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-250.
RC STRAIN=212;
RX PubMed=7812434; DOI=10.1099/13500872-140-11-2931;
RA Ojaimi C., Davidson B.E., Saint-Girons I., Old I.G.;
RT "Conservation of gene arrangement and an unusual organization of rRNA genes
RT in the linear chromosomes of the Lyme disease spirochaetes Borrelia
RT burgdorferi, B. garinii and B. afzelii.";
RL Microbiology 140:2931-2940(1994).
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
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 -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
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:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AE000783; AAC66417.1; -; Genomic_DNA.
DR EMBL; L32861; AAC41407.1; -; Genomic_DNA.
DR PIR; E70104; E70104.
DR RefSeq; NP_212171.1; NC_001318.1.
DR RefSeq; WP_002665505.1; NC_001318.1.
DR AlphaFoldDB; Q59188; -.
DR SMR; Q59188; -.
DR STRING; 224326.BB_0037; -.
DR PaxDb; 224326-BB_0037; -.
DR EnsemblBacteria; AAC66417; AAC66417; BB_0037.
DR KEGG; bbu:BB_0037; -.
DR PATRIC; fig|224326.49.peg.436; -.
DR HOGENOM; CLU_027938_6_1_12; -.
DR OrthoDB; 9803035at2; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
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; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..250
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000208167"
FT MOTIF 88..93
FT /note="HXXXXD motif"
SQ SEQUENCE 250 AA; 28581 MW; A730BED7058AD999 CRC64;
MIIVFMKILR SIITYFNVLL FFLILIFFLF PFYLVCKIFL IERYVVRLSF IMMRACIKIS
LWLAGIKIIV TGSENIPKKS NVIIMGNHIA AMDPLIFIYT FACPFVILAK HSLLRIPFVN
IVLIVMGVIF VNRRSIRSAA AAEVKAIKVM REGRSIGIFP EGTRNRGGDT RVFKKGSIKM
ALKTGTSILP VTLYNTNNFF IKNIIFNSGL SVYIHVHPLI DVLKLSEYEK ENLTSIIRDQ
IVKKLETIKI
//
