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Database: UniProt
Entry: H6RST7_BLASD
LinkDB: H6RST7_BLASD
Original site: H6RST7_BLASD 
ID   H6RST7_BLASD            Unreviewed;       252 AA.
AC   H6RST7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:CCG03040.1};
DE            EC=2.3.1.51 {ECO:0000313|EMBL:CCG03040.1};
GN   OrderedLocusNames=BLASA_2131 {ECO:0000313|EMBL:CCG03040.1};
OS   Blastococcus saxobsidens (strain DD2).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG03040.1, ECO:0000313|Proteomes:UP000007517};
RN   [1] {ECO:0000313|EMBL:CCG03040.1, ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|EMBL:CCG03040.1,
RC   ECO:0000313|Proteomes:UP000007517};
RX   PubMed=22535935; DOI=10.1128/JB.00320-12;
RA   Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA   Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA   Gury J., Pujic P., Normand P.;
RT   "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT   Bacterium.";
RL   J. Bacteriol. 194:2752-2753(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA   Genoscope.;
RT   "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; FO117623; CCG03040.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6RST7; -.
DR   STRING; 1146883.BLASA_2131; -.
DR   KEGG; bsd:BLASA_2131; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_4_0_11; -.
DR   OrthoDB; 9808424at2; -.
DR   Proteomes; UP000007517; Chromosome.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
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:CCG03040.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007517};
KW   Transferase {ECO:0000313|EMBL:CCG03040.1}.
FT   DOMAIN          35..154
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   252 AA;  27235 MW;  27AEE5E67224F9AF CRC64;
     MFYWFLKFVA IGPLARVVFR PKAEGAENVP ATGAAILASN HLSATDWIFL PLQLRRRVTF
     LAKAEYFTGT GVKGFLQRAF FTGAGQVPID RSSASAAEGA IQTGLRILRE GKLLGIYPEG
     TRSPDGRLYR GKIGVARMAL EIGVPVVPVA VVYSSRPLPF GKKITRVRVR FGEPLDFSRY
     EGLAGDRFVE RSVTDEIMYE IMTLSGQEYV DVYGAAVKKS MDATGASANE VVATLQPPAG
     EAADRAPTTL AG
//
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