ID A0A101APD3_9MYCO Unreviewed; 319 AA.
AC A0A101APD3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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=AU194_05640 {ECO:0000313|EMBL:KUI26535.1};
OS Mycobacterium sp. GA-2829.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1772283 {ECO:0000313|EMBL:KUI26535.1, ECO:0000313|Proteomes:UP000053444};
RN [1] {ECO:0000313|EMBL:KUI26535.1, ECO:0000313|Proteomes:UP000053444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA-2829 {ECO:0000313|EMBL:KUI26535.1,
RC ECO:0000313|Proteomes:UP000053444};
RG TB Trials Study Group;
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA Grewal H.M.S.;
RL Submitted (JAN-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}.
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:KUI26535.1}.
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DR EMBL; LQIT01000048; KUI26535.1; -; Genomic_DNA.
DR RefSeq; WP_059091901.1; NZ_LQIT01000048.1.
DR AlphaFoldDB; A0A101APD3; -.
DR STRING; 1772283.AU194_05640; -.
DR OrthoDB; 4366784at2; -.
DR Proteomes; UP000053444; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:KUI26535.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053444};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:KUI26535.1}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..319
FT /note="Acyl-CoA:diacylglycerol acyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007093033"
SQ SEQUENCE 319 AA; 33430 MW; 14FA77D9442CC4DD CRC64;
MRFLQSFRRK LLAGTAAALL LPGLIAVAGT SATANAYSRP GLPVETLMVP SPAMGRDIPV
KFQGGGPKAV YLLDGLRARD DNSGWDIETA AFENYFESGL SVVMPVGGMS SFYTNWQGPA
VGNGQTYTYQ WETFLTSELP AYLAANKGIS PSGNAVVGLS MSGSSALILA ANYPGQFSYA
ASLSGYLNLS DGLWPTLVGF AMRDAGGFNA NAMWGPGGGP AWKRNDPTVN VGKLVANGTR
IWVYCGTGRP GELGGGGDIA GQLLEGITLD SNRNFQRQYT AAGGSNGTFN FPPNGTHGWG
YWGAQLNAMK GDIQRTLGA
//
