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Database: UniProt
Entry: A0A2S8Y9R2_9PSED
LinkDB: A0A2S8Y9R2_9PSED
Original site: A0A2S8Y9R2_9PSED 
ID   A0A2S8Y9R2_9PSED        Unreviewed;       240 AA.
AC   A0A2S8Y9R2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00016139, ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN   ORFNames=CQZ98_12335 {ECO:0000313|EMBL:PRA54301.1};
OS   Pseudomonas sp. MYb115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1848717 {ECO:0000313|EMBL:PRA54301.1, ECO:0000313|Proteomes:UP000239970};
RN   [1] {ECO:0000313|EMBL:PRA54301.1, ECO:0000313|Proteomes:UP000239970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb115 {ECO:0000313|EMBL:PRA54301.1,
RC   ECO:0000313|Proteomes:UP000239970};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU361267};
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:0000256|RuleBase:RU361267}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC       ECO:0000256|RuleBase:RU361267}.
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:PRA54301.1}.
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DR   EMBL; PCQM01000007; PRA54301.1; -; Genomic_DNA.
DR   RefSeq; WP_027618069.1; NZ_PCQM01000007.1.
DR   AlphaFoldDB; A0A2S8Y9R2; -.
DR   UniPathway; UPA00557; UER00613.
DR   Proteomes; UP000239970; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
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:SF11; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE ALPHA; 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 {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:PRA54301.1};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:PRA54301.1}.
FT   DOMAIN          68..183
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   240 AA;  26832 MW;  C05ACAF2744EA9FC CRC64;
     MLFVFRMLLM GLHFVLAGVL GVVLGLVRPF NPDNSRLCAR LYAWPAMCIL RLRVSADVDS
     LTHKQQSCVV IANHQSNYDL FVLGNVVPHR TVCIGKKSLK WVPLFGQLFW LAGNVLIDRG
     NAHKARQAML TTTDTLQHKD TSIWVFPEGT RNLGKELLPF KKGAFHMAIA AGVPIVQVCV
     SNYINHMRLN RWNSGRILIR SLPPIPTAGL TLDDIPALIE QCQAQMRECI DGLDRQLQAA
//
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