ID A0A0G3GUH4_9CORY Unreviewed; 651 AA.
AC A0A0G3GUH4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Name=csp1 {ECO:0000313|EMBL:AKK04155.1};
GN ORFNames=CEPID_11635 {ECO:0000313|EMBL:AKK04155.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK04155.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK04155.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK04155.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-2015) 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; CP011541; AKK04155.1; -; Genomic_DNA.
DR RefSeq; WP_047241040.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GUH4; -.
DR STRING; 1050174.CEPID_11635; -.
DR KEGG; cei:CEPID_11635; -.
DR PATRIC; fig|1050174.4.peg.2349; -.
DR OrthoDB; 4527292at2; -.
DR Proteomes; UP000035368; 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; IPR013207; LGFP.
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 Pfam; PF08310; LGFP; 4.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000035368};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT REGION 58..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 70883 MW; FBB5CE342394EDE5 CRC64;
MRETRSARRR SLQLALAAVP VAIAIGLSPL NAPLVAQAQS SGSSDLLGGV KKQTGISDYL
DPGEVPQRTP IKTDHPKLEG LPAGVSIDRV EWLTDRRVAV FINSAAMPEH PIQVQILLAR
DWHSNPKAKF PEVWALDGLR AVDTENGWTI HTNIEQFYAD KNVNVILPVG GEASFYTDWE
GPAKDKNYKW ESFLLNELPA VLQNGYRSNG QRAITGLSMG GTAAMNLAQH RPDMFNFVGS
FSGYLDTTST GMPDMLRGAL VEGGGYNVDN MWGRPINQRW IDNDPKLGIE ALKGKTIYVS
AGNGVDDFGK PGSVATGPSN EAGKGLEVIS RMTTQTFVER ANRAGVPVVA QFRPSGIHNW
PYWQFEMSQA WPYIADSLAL KKEDRGADCT TIGAIAEATK GAQWGACLNN EYQVKGGVSQ
DFSTGRAFWS AETGAHVLQG RISARYAEMG ATDSWLGFPT SNEIATPDGK GRFVTFQHGV
IYWTHETNAQ EIPADMFNAW GRQGWETGVL GYPTAAPQTI DGAIVQKFQG GWVVRNKANE
SFYVRGKIAE KYGELNTVKS ALGAPTSDEF LIPGGALQNF ENGSIYWNAA TGAHVVMNGA
IRDTWGANGW ENGRYGWPTS DLTKVPAGGD QQTFQHGTIK QLNGRIVEEP R
//
