ID A0A0A0B5T0_9CELL Unreviewed; 256 AA.
AC A0A0A0B5T0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:KGM01179.1};
GN ORFNames=Q760_03380 {ECO:0000313|EMBL:KGM01179.1};
OS Cellulomonas cellasea DSM 20118.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM01179.1, ECO:0000313|Proteomes:UP000029833};
RN [1] {ECO:0000313|EMBL:KGM01179.1, ECO:0000313|Proteomes:UP000029833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM01179.1,
RC ECO:0000313|Proteomes:UP000029833};
RA Wang G., Zhuang W.;
RL Submitted (OCT-2013) 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:KGM01179.1}.
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DR EMBL; AXNT01000127; KGM01179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0B5T0; -.
DR STRING; 1408250.Q760_03380; -.
DR Proteomes; UP000029833; 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:KGM01179.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029833};
KW Transferase {ECO:0000313|EMBL:KGM01179.1}.
FT DOMAIN 26..145
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 220..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 256 AA; 26862 MW; 23D1F8A564346B71 CRC64;
MVGPLLHLVF RPWVRGAENV PSEGAAILAS NHLAVIDSFV LPLVLDREIV FIGKSEYFTG
TGVKGRLKAG FFRGVGTIPV DRSGGKASEA ALRTGLNRLR DGGLFGIYPE GTRSPDGRLY
RGKTGVARLA LESGAPVVPV VMVGTDVAQP LGRVIPKPVR LGVVIGEPLD FSRYRGMEND
RFILRSVTDE IMYALMSLSG QEYVDVYAAT QKARIATGHP AAAPVADAGP TAPGGRPAPD
VQVPGPPEGD AGPSVG
//
