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Database: UniProt
Entry: A0A095XY29_9ACTO
LinkDB: A0A095XY29_9ACTO
Original site: A0A095XY29_9ACTO 
ID   A0A095XY29_9ACTO        Unreviewed;       265 AA.
AC   A0A095XY29;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:KGE99331.1};
GN   ORFNames=HMPREF1627_09280 {ECO:0000313|EMBL:KGE99331.1};
OS   Actinomyces sp. S6-Spd3.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=1284680 {ECO:0000313|EMBL:KGE99331.1, ECO:0000313|Proteomes:UP000029604};
RN   [1] {ECO:0000313|EMBL:KGE99331.1, ECO:0000313|Proteomes:UP000029604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S6-Spd3 {ECO:0000313|EMBL:KGE99331.1,
RC   ECO:0000313|Proteomes:UP000029604};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) 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};
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:KGE99331.1}.
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DR   EMBL; JRMV01000281; KGE99331.1; -; Genomic_DNA.
DR   RefSeq; WP_034503048.1; NZ_JRMV01000281.1.
DR   AlphaFoldDB; A0A095XY29; -.
DR   PATRIC; fig|1284680.3.peg.1562; -.
DR   eggNOG; COG0204; Bacteria.
DR   Proteomes; UP000029604; 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:KGE99331.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029604};
KW   Transferase {ECO:0000313|EMBL:KGE99331.1}.
FT   DOMAIN          35..154
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          229..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  28615 MW;  473A400B66DBE6D3 CRC64;
     MGLYQALKLT GTPILKAAYR PWIRGKENIP ETGPAILASN HNAVWDSVFL PMMIDREVVF
     MGKADYFTGT GLKGWATKEF MRAVGTIPVD RSGGRASEAA LKAGLKRLGE GELFGIYPEG
     TRSPDGRLYR GKTGVARLAL LSGAPVIPVA MIGTHAAQPI GQKIPSRTNI GMVIGEPLDF
     SRYKGLDRDR FVLRAITDEI MYNLMLLSGQ EYVDLYAADV KAQLAAEGAF DGPVPSNGKT
     APGGRVAPDV EVPTPTEEEL HEEEN
//
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