ID A0A1L7CVM5_9CORY Unreviewed; 368 AA.
AC A0A1L7CVM5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CSPHI_00970 {ECO:0000313|EMBL:APT89893.1};
OS Corynebacterium sphenisci DSM 44792.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1437874 {ECO:0000313|EMBL:APT89893.1, ECO:0000313|Proteomes:UP000185469};
RN [1] {ECO:0000313|EMBL:APT89893.1, ECO:0000313|Proteomes:UP000185469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44792 {ECO:0000313|EMBL:APT89893.1,
RC ECO:0000313|Proteomes:UP000185469};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium sphenisci CECT 5990(T) (=DSM
RT 44792(T)), isolated from healthy wild penguins.";
RL Submitted (AUG-2014) 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; CP009248; APT89893.1; -; Genomic_DNA.
DR RefSeq; WP_075691090.1; NZ_CP009248.1.
DR AlphaFoldDB; A0A1L7CVM5; -.
DR STRING; 1437874.CSPHI_00970; -.
DR KEGG; csph:CSPHI_00970; -.
DR OrthoDB; 4510758at2; -.
DR Proteomes; UP000185469; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000185469};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..368
FT /note="Acyl-CoA:diacylglycerol acyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012792512"
SQ SEQUENCE 368 AA; 39431 MW; C7D23C5DEF6DA521 CRC64;
MRLRRTRITA AALAVAAMAA PTAAGASPLP APALSEVPTA AVAATEHTVP TREAVVGVKE
NPNANPEWRG LIAGRDNVHE VWAHSPSMRR NVPMVWIHPA GAEPTAPRPT LYVLNGADGG
EGKASWLYQS DILDFFSDKD VNVIVIQAGK YSYYTDWVNQ GTELGAQYWE TFLTRELPGP
LERRIGAAGR DRGLIGMSMS GTSSLLFAEH HPGLYAAVGS FSGCASTSDD VSASFIDLVL
DRANATGEDM WGPRPSELWT ANDALLGVES LGDTPAYISN GSGLWGAAEF PGQPDLNAEI
ALTAQRTAGS VIEAATNLCT RNLKARMDAA GVGGNVIWDF GNVGTHSWSY WQEDLHQSWE
QLFSRVLR
//
