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Database: UniProt
Entry: I0R033_9MICO
LinkDB: I0R033_9MICO
Original site: I0R033_9MICO 
ID   I0R033_9MICO            Unreviewed;       192 AA.
AC   I0R033;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:EIC91219.1};
GN   ORFNames=IMCC13023_07720 {ECO:0000313|EMBL:EIC91219.1};
OS   Candidatus Aquiluna sp. IMCC13023.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Aquiluna.
OX   NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC91219.1, ECO:0000313|Proteomes:UP000054510};
RN   [1] {ECO:0000313|Proteomes:UP000054510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX   PubMed=22689238; DOI=10.1128/JB.00586-12;
RA   Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT   "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT   member of the Actinobacteria isolated from an arctic fjord.";
RL   J. Bacteriol. 194:3550-3551(2012).
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   -!- 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:EIC91219.1}.
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DR   EMBL; AJKR01000003; EIC91219.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0R033; -.
DR   STRING; 1081644.IMCC13023_07720; -.
DR   PATRIC; fig|1081644.3.peg.779; -.
DR   eggNOG; COG0204; Bacteria.
DR   Proteomes; UP000054510; Unassembled WGS sequence.
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:EIC91219.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054510};
KW   Transferase {ECO:0000313|EMBL:EIC91219.1}.
FT   DOMAIN          1..118
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   192 AA;  21137 MW;  AA76AC9ECE7A1AF1 CRC64;
     MASNHLSFVD SIFLPLKLRR PVTFLAKSEY FTGKGFKGAL IRWFFISTGQ IPIDRSGGKA
     SEDSLNTGLG VLERGLLLGI YPEGTRSPNS DMHRGRTGIA RMALEAGVPV IPVAMIDTDK
     VQPLGAKYPK IHRVGVVIGE PLDFSRFAGM EGERAVLRSV TDQIVYSIHR LSNQKYEDVY
     ASTVKSRLAR AE
//
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