ID Q8R839_CALS4 Unreviewed; 201 AA.
AC Q8R839;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:AAM25349.1};
GN Name=PlsC2 {ECO:0000313|EMBL:AAM25349.1};
GN OrderedLocusNames=TTE2192 {ECO:0000313|EMBL:AAM25349.1};
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068 {ECO:0000313|EMBL:AAM25349.1, ECO:0000313|Proteomes:UP000000555};
RN [1] {ECO:0000313|EMBL:AAM25349.1, ECO:0000313|Proteomes:UP000000555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4
RC {ECO:0000313|Proteomes:UP000000555};
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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; AE008691; AAM25349.1; -; Genomic_DNA.
DR RefSeq; WP_009611242.1; NZ_JANUCV010000001.1.
DR AlphaFoldDB; Q8R839; -.
DR STRING; 273068.TTE2192; -.
DR KEGG; tte:TTE2192; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_5_9; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000000555; 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:AAM25349.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000555};
KW Transferase {ECO:0000313|EMBL:AAM25349.1}.
FT DOMAIN 35..147
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 201 AA; 22430 MW; 0CA618FF616B1444 CRC64;
MFLLYRVLRL IGIALLKIFY SFKVERDGNL SKGPYIFVSN HQSLLDPVAV ACAIKTPIIF
LASSELFNIY LLKPFLLIDK AIPIKKESAD LKAIKKALER LKEGYSIGIF PEGGISPKGV
IEKIYEGAMY LAYKSGKPLV PVVVQGTKEV LPLGKYVPKL RGKIKVRVGE PISPDLNKDI
KAEIAELKEK IKARMKEMLA E
//
