ID V7L9Z4_MYCAV Unreviewed; 347 AA.
AC V7L9Z4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=O973_19775 {ECO:0000313|EMBL:ETB18338.1};
OS Mycobacterium avium subsp. avium 11-4751.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1391992 {ECO:0000313|EMBL:ETB18338.1, ECO:0000313|Proteomes:UP000035007};
RN [1] {ECO:0000313|EMBL:ETB18338.1, ECO:0000313|Proteomes:UP000035007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-4751 {ECO:0000313|EMBL:ETB18338.1,
RC ECO:0000313|Proteomes:UP000035007};
RA Bannantine J.P., Robbe-Austerman S., O'Connell C.;
RT "Genome sequence of MAC strains.";
RL Submitted (OCT-2013) 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:ETB18338.1}.
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DR EMBL; AYOB01000388; ETB18338.1; -; Genomic_DNA.
DR AlphaFoldDB; V7L9Z4; -.
DR SMR; V7L9Z4; -.
DR PATRIC; fig|1391992.3.peg.4066; -.
DR Proteomes; UP000035007; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT REGION 326..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 36096 MW; DFAFF3DE504C208E CRC64;
MTLVDRLRGA VAGMPRRLVV GAAGAALLSG LIGAVGGSAT AGAFSRPGLP VEYLQVPSAA
MGRDIKVQFQ SGGANSPALY LLDGMRAQDD FNGWDINTPA FEWYNQSGIS VAMPVGGQSS
FYSDWYKPAC GKAGCTTYKW ETFLTSELPQ YLSAQKQVKP TGSGVVGLSM AGSSALILAA
YHPDQFVYAG SLSALLDPSQ GMGPSLIGLA MGDAGGYKAA DMWGPKEDPA WARNDPSLQV
GKLVANNTRI WVYCGNGKPS DLGGDNLPAK FLEGFVRTSN LKFQDAYNGA GGHNAVWNFD
ANGTHDWPYW GAQLQAMKPD LQSVLGATPG AGPATAAATN AGNGQGT
//
