ID   TGS2_MYCTO              Reviewed;         454 AA.
AC   P9WKC6; L0TGD2; O69701; P67210;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Probable diacyglycerol O-acyltransferase tgs2;
DE            Short=TGS2;
DE   AltName: Full=Diacylglycerol O-acyltransferase;
DE            Short=DGAT;
DE            EC=2.3.1.20 {ECO:0000250|UniProtKB:P9WKC7};
DE   AltName: Full=Long-chain-alcohol O-fatty-acyltransferase;
DE            EC=2.3.1.75 {ECO:0000250|UniProtKB:P9WKC7};
DE   AltName: Full=Probable triacylglycerol synthase tgs2;
DE   AltName: Full=Wax ester synthase/acyl-CoA:diacylglycerol acyltransferase;
DE   AltName: Full=Wax synthase;
DE            Short=WS;
GN   Name=tgs2; OrderedLocusNames=MT3839;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the terminal and only committed step in
CC       triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as
CC       substrates. Required for storage lipid synthesis.
CC       {ECO:0000250|UniProtKB:P9WKC9}.
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:0000250|UniProtKB:P9WKC7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester +
CC         CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75;
CC         Evidence={ECO:0000250|UniProtKB:P9WKC7};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK48206.1; -; Genomic_DNA.
DR   PIR; G70797; G70797.
DR   RefSeq; WP_003420440.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKC6; -.
DR   SMR; P9WKC6; -.
DR   EnsemblBacteria; AAK48206; AAK48206; MT3839.
DR   KEGG; mtc:MT3839; -.
DR   PATRIC; fig|83331.31.peg.4134; -.
DR   HOGENOM; CLU_024186_4_1_11; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0102966; F:arachidoyl-CoA:1-dodecanol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR014292; Acyl_transf_WS/DGAT.
DR   InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR   InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR   InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR   PANTHER; PTHR31650; PTHR31650; 1.
DR   Pfam; PF03007; WES_acyltransf; 1.
DR   Pfam; PF06974; WS_DGAT_C; 1.
DR   TIGRFAMs; TIGR02946; acyl_WS_DGAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Glycerol metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Transferase.
FT   CHAIN           1..454
FT                   /note="Probable diacyglycerol O-acyltransferase tgs2"
FT                   /id="PRO_0000427677"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   454 AA;  49304 MW;  11CD02FA1BEB6ACB CRC64;
     MDLMMPNDSM FLFIESREHP MHVGGLSLFE PPQGAGPEFV REFTERLVAN DEFQPMFRKH
     PATIGGGIAR VAWAYDDDID IDYHVRRSAL PSPGRVRDLL ELTSRLHTSL LDRHRPLWEL
     HVVEGLNDGR FAMYTKMHHA LIDGVSAMKL AQRTLSADPD DAEVRAIWNL PPRPRTRPPS
     DGSSLLDALF KMAGSVVGLA PSTLKLARAA LLEQQLTLPF AAPHSMFNVK VGGARRCAAQ
     SWSLDRIKSV KQAAGVTVND AVLAMCAGAL RYYLIERNAL PDRPLIAMVP VSLRSKEDAD
     AGGNLVGSVL CNLATHVDDP AQRIQTISAS MDGNKKVLSE LPQLQVLALS ALNMAPLTLA
     GVPGFLSAVP PPFNIVISNV PGPVDPLYYG TARLDGSYPL SNIPDGQALN ITLVNNAGNL
     DFGLVGCRRS VPHLQRLLAH LESSLKDLEQ AVGI