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Database: UniProt
Entry: Q67NT9_SYMTH
LinkDB: Q67NT9_SYMTH
Original site: Q67NT9_SYMTH 
ID   Q67NT9_SYMTH            Unreviewed;       214 AA.
AC   Q67NT9;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:BAD40654.1};
GN   OrderedLocusNames=STH1669 {ECO:0000313|EMBL:BAD40654.1};
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD40654.1, ECO:0000313|Proteomes:UP000000417};
RN   [1] {ECO:0000313|EMBL:BAD40654.1, ECO:0000313|Proteomes:UP000000417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD40654.1; -; Genomic_DNA.
DR   RefSeq; WP_011195798.1; NC_006177.1.
DR   AlphaFoldDB; Q67NT9; -.
DR   STRING; 292459.STH1669; -.
DR   KEGG; sth:STH1669; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_4_5_9; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000000417; 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:BAD40654.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000417};
KW   Transferase {ECO:0000313|EMBL:BAD40654.1}.
FT   DOMAIN          35..147
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   214 AA;  22589 MW;  651FA1D963FF9966 CRC64;
     MWLYGFARIV VGLGYRLAYR VQAEGREHIP PTGGVILCGN HINAQDPIVI GLACPRPICF
     MAKEELFRSQ LLGFIIKGLG AFPVKRGSAD RAALKHALAL LEAGCCFGIF PEGTRSRTGE
     LQKPEPGTAY IALKSGVPVI PVGISGSYRL FSPIRVRFGP PVDLDRFRGE KLNGETLEAA
     SQAIADAIAA LLDPPSGLSN AGAGPPAGRA LSSL
//
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