ID A0A1H5R2J2_9PSEU Unreviewed; 272 AA.
AC A0A1H5R2J2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Acyl-CoA:diacylglycerol acyltransferase {ECO:0000256|ARBA:ARBA00032572};
DE EC=2.3.1.122 {ECO:0000256|ARBA:ARBA00012820};
DE EC=2.3.1.20 {ECO:0000256|ARBA:ARBA00013244};
GN ORFNames=SAMN05421837_106321 {ECO:0000313|EMBL:SEF32555.1};
OS Amycolatopsis pretoriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=218821 {ECO:0000313|EMBL:SEF32555.1, ECO:0000313|Proteomes:UP000198878};
RN [1] {ECO:0000313|EMBL:SEF32555.1, ECO:0000313|Proteomes:UP000198878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44654 {ECO:0000313|EMBL:SEF32555.1,
RC ECO:0000313|Proteomes:UP000198878};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose
CC 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234;
CC EC=2.3.1.122; Evidence={ECO:0000256|ARBA:ARBA00000697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00001039};
CC -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC {ECO:0000256|ARBA:ARBA00005874}.
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DR EMBL; FNUJ01000006; SEF32555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5R2J2; -.
DR STRING; 218821.SAMN05421837_106321; -.
DR Proteomes; UP000198878; Unassembled WGS sequence.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0050348; F:trehalose O-mycolyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR48098:SF1; DIACYLGLYCEROL ACYLTRANSFERASE_MYCOLYLTRANSFERASE AG85A; 1.
DR PANTHER; PTHR48098; ENTEROCHELIN ESTERASE-RELATED; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:SEF32555.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..272
FT /note="Acyl-CoA:diacylglycerol acyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011462521"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 28705 MW; 8B59437039BA2571 CRC64;
MLSRRGLLAG STLALLAGCS SAEPAPGPPP VPAPTRPSAP SAPVTVQRMP SAARGTDVDL
VLITPEGVPS SGLPVCLALH GRGARARTFL DLGVPAALTR AVREGVPPFA VAAVDGDHYW
VGVGEDDDPQ RMLTDEVPAW LTARDLRPAS AVFGISMGGF GALRFARAHP DLKAVATASA
ALFVSWPDAR SRKVFSDEAN WRAEEPLLHT GELRPDAVGV WCGESDPFLS ADRKLVKAVS
PAVSRFSPGG HQDEYWRGIL PDVLKFVGQR LN
//
