ID A0A0Q5MBT3_9MICO Unreviewed; 228 AA.
AC A0A0Q5MBT3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=ASF88_06195 {ECO:0000313|EMBL:KQR54377.1};
OS Leifsonia sp. Leaf336.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736341 {ECO:0000313|EMBL:KQR54377.1, ECO:0000313|Proteomes:UP000050966};
RN [1] {ECO:0000313|EMBL:KQR54377.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR54377.1,
RC ECO:0000313|Proteomes:UP000050966};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR54377.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR54377.1,
RC ECO:0000313|Proteomes:UP000050966};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR54377.1}.
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DR EMBL; LMOZ01000001; KQR54377.1; -; Genomic_DNA.
DR RefSeq; WP_055915566.1; NZ_LMOZ01000001.1.
DR AlphaFoldDB; A0A0Q5MBT3; -.
DR STRING; 1736341.ASF88_06195; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000050966; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000050966}.
FT DOMAIN 35..154
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 228 AA; 24931 MW; 51EBF29627CAECE5 CRC64;
MFYWLMKNLI AGPILRGIFR PWVVGIENVP ADGAVILASN HLSFIDSIFL PLVVDRHVSF
LAKSDYFTRR GLKGWATKAF MNATGQLPID RSGGKASEAS LNTGLAVLAR GEILGIYPEG
TRSPDGKLYR GRTGVARMIL EAGVPVVPVA MVDTAEIMPI GKRLPHIGRI GIIIGEPLDF
SRFEGMEGDR FILRSVTDEI MYALHALGAQ EYVDVYASTV KEKRAALT
//