ID   TGS3_MYCTO              Reviewed;         271 AA.
AC   P9WKC4; L0TC77; O05879;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Probable diacyglycerol O-acyltransferase tgs3;
DE            Short=TGS3;
DE            EC=2.3.1.20 {ECO:0000250|UniProtKB:P9WKC5};
DE   AltName: Full=Probable triacylglycerol synthase tgs3;
GN   Name=tgs3; OrderedLocusNames=MT3331;
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:P9WKC5};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved His residue in position 138 suggested to
CC       serve as a proton acceptor for this family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47674.1; -; Genomic_DNA.
DR   PIR; D70591; D70591.
DR   RefSeq; WP_003899981.1; NC_002755.2.
DR   AlphaFoldDB; P9WKC4; -.
DR   SMR; P9WKC4; -.
DR   EnsemblBacteria; AAK47674; AAK47674; MT3331.
DR   KEGG; mtc:MT3331; -.
DR   PATRIC; fig|83331.31.peg.3587; -.
DR   HOGENOM; CLU_024186_4_0_11; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004144; F:diacylglycerol O-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; IPR045034; O-acyltransferase_WSD1-like.
DR   InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR   PANTHER; PTHR31650; PTHR31650; 1.
DR   Pfam; PF03007; WES_acyltransf; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Glycerol metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Transferase.
FT   CHAIN           1..271
FT                   /note="Probable diacyglycerol O-acyltransferase tgs3"
FT                   /id="PRO_0000427678"
SQ   SEQUENCE   271 AA;  30379 MW;  59D185254B1E9096 CRC64;
     MVTRLSASDA SFYQLENTAT PMYVGLLLIL RRPRAGLSYE ALLETVEQRL PQIPRYRQKV
     QEVKLGLARP VWIDDRDFDI TYHVRRSALP SPGSDEQLHE LIARLAARPL DKSRPLWEMY
     LVEGLEKNRI ALYTKSHQAL INGVTALAIG HVIADRTRRP PAFPEDIWVP ERDPGTTRLL
     LRAVGDWLVR PGAQLQAVGS AVAGLVTNSG QLVETGRKVL DIARTVARGT APSSPLNATV
     SRNRRFTVAR ASLDDYRTVR ARYDCDSTTW C