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Database: UniProt
Entry: S9QJT5_9RHOB
LinkDB: S9QJT5_9RHOB
Original site: S9QJT5_9RHOB 
ID   S9QJT5_9RHOB            Unreviewed;       212 AA.
AC   S9QJT5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:EPX81706.1};
DE            EC=2.3.1.51 {ECO:0000313|EMBL:EPX81706.1};
GN   ORFNames=thalar_00263 {ECO:0000313|EMBL:EPX81706.1};
OS   Litoreibacter arenae DSM 19593.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Litoreibacter.
OX   NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX81706.1, ECO:0000313|Proteomes:UP000015351};
RN   [1] {ECO:0000313|Proteomes:UP000015351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX   PubMed=24501650; DOI=10.4056/sigs.4258318;
RA   Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT   member of the Roseobacter clade isolated from sea sand.";
RL   Stand. Genomic Sci. 9:117-127(2013).
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   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPX81706.1}.
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DR   EMBL; AONI01000005; EPX81706.1; -; Genomic_DNA.
DR   RefSeq; WP_021101205.1; NZ_KE557310.1.
DR   AlphaFoldDB; S9QJT5; -.
DR   STRING; 1123360.thalar_00263; -.
DR   PATRIC; fig|1123360.3.peg.261; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_8_1_5; -.
DR   OrthoDB; 9808424at2; -.
DR   Proteomes; UP000015351; Unassembled WGS sequence.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   InterPro; IPR000872; Tafazzin.
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   PRINTS; PR00979; TAFAZZIN.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:EPX81706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015351};
KW   Transferase {ECO:0000313|EMBL:EPX81706.1}.
FT   DOMAIN          37..159
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   212 AA;  23835 MW;  6151A5A5F6B640A7 CRC64;
     MRRFAASVVG KLLIFFAQFI TAARAEWRGI EPVRRQRIYY ANHTSNADLP LIWTVLPAAL
     RRDTRAVAAA DYWLKNKLRA FVGRDVFRAV LIDRRPEHRT DDPIAKIVEA LDEGSSIIIF
     PEGGRNRSED PLMPFKAGLY NIATQRPEID LVPCWIDNIS HIMPSGEVIP VPLACTVVFG
     SAIHVEDGEP KDKFLTRASD ALLQLIPQRG HA
//
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