TGS1_MYCTU
ID TGS1_MYCTU Reviewed; 463 AA.
AC P9WKC9; E0YJK4; F2GJ38; O07035; P0A650;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Probable diacyglycerol O-acyltransferase tgs1;
DE Short=TGS1;
DE EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE AltName: Full=Probable triacylglycerol synthase tgs1;
GN Name=tgs1; OrderedLocusNames=Rv3130c; ORFNames=MTCY03A2.28, MTCY164.41c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G4B1.2;
RX PubMed=20639330; DOI=10.1128/jb.00536-10;
RA Domenech P., Kolly G.S., Leon-Solis L., Fallow A., Reed M.B.;
RT "Massive gene duplication event among clinical isolates of the
RT Mycobacterium tuberculosis W/Beijing family.";
RL J. Bacteriol. 192:4562-4570(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP INDUCTION BY HYPOXIA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11416222; DOI=10.1073/pnas.121172498;
RA Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA Schoolnik G.K.;
RT "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT encoding alpha -crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
RN [4]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
RN [5]
RP FUNCTION IN E.COLI, CATALYTIC ACTIVITY, PH DEPENDENCE, INDUCTION BY
RP HYPOXIA, AND BY NITRIC OXIDE (NO).
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15262939; DOI=10.1128/jb.186.15.5017-5030.2004;
RA Daniel J., Deb C., Dubey V.S., Sirakova T.D., Abomoelak B., Morbidoni H.R.,
RA Kolattukudy P.E.;
RT "Induction of a novel class of diacylglycerol acyltransferases and
RT triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into
RT a dormancy-like state in culture.";
RL J. Bacteriol. 186:5017-5030(2004).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES IN E.COLI, INDUCTION BY ACID, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16946266; DOI=10.1099/mic.0.28993-0;
RA Sirakova T.D., Dubey V.S., Deb C., Daniel J., Korotkova T.A., Abomoelak B.,
RA Kolattukudy P.E.;
RT "Identification of a diacylglycerol acyltransferase gene involved in
RT accumulation of triacylglycerol in Mycobacterium tuberculosis under
RT stress.";
RL Microbiology 152:2717-2725(2006).
RN [7]
RP INDUCTION BY CARBON MONOXIDE (CO).
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA Shiloh M.U., Manzanillo P., Cox J.S.;
RT "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT macrophage infection.";
RL Cell Host Microbe 3:323-330(2008).
RN [8]
RP INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18400743; DOI=10.1074/jbc.m802274200;
RA Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I.,
RA Agarwal A., Steyn A.J.;
RT "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
RT tuberculosis dormancy regulon.";
RL J. Biol. Chem. 283:18032-18039(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 (Probable).
CC {ECO:0000305|PubMed:15262939}.
CC -!- FUNCTION: Upon expression in E.coli functions as a triacylglycerol
CC synthase, making triacylglycerol (TG) from diolein and long-chain fatty
CC acyl-CoA. Prefers C(26:0)-CoA over C(18:1)-CoA. TG synthesis activity
CC increases in M.tuberculosis upon oxygen depletion and NO treatment,
CC with concomitant accumulation of TG in inclusion bodies. As disruption
CC of the gene encoding this protein obviates TG synthesis this seems to
CC be the major enzyme involved in production of TG. Has no wax synthase
CC activity to produce wax esters. {ECO:0000269|PubMed:15262939}.
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:0000269|PubMed:15262939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + di-(9Z)-octadecenoylglycerol = 1,2,3-
CC tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:45780,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:15262939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45781;
CC Evidence={ECO:0000269|PubMed:15262939};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=306 uM for C(26:0) {ECO:0000269|PubMed:16946266};
CC KM=540 uM for C(18:1) {ECO:0000269|PubMed:16946266};
CC Vmax=2.4 nmol/min/mg enzyme (for C(26:0))
CC {ECO:0000269|PubMed:16946266};
CC Vmax=1.1 nmol/min/mg enzyme (for C(18:1))
CC {ECO:0000269|PubMed:16946266};
CC Note=Upon expression in E.coli.;
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:15262939,
CC ECO:0000269|PubMed:16946266};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia), low levels of nitric oxide (NO) and
CC carbon monoxide (CO). It is hoped that this regulon will give insight
CC into the latent, or dormant phase of infection. Also induced when grown
CC at pH 5.0 for 3 weeks. {ECO:0000269|PubMed:11416222,
CC ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:15262939,
CC ECO:0000269|PubMed:16946266, ECO:0000269|PubMed:18400743,
CC ECO:0000269|PubMed:18474359}.
CC -!- DISRUPTION PHENOTYPE: No detectable TG under hypoxic growth conditions,
CC or when grown at pH 5.0. However, about 30% of normal levels of TG
CC accumulated when grown in the presence of NO but there was virtually no
CC C(26:0) TG produced. {ECO:0000269|PubMed:16946266}.
CC -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; HM053705; ADM62323.1; -; Genomic_DNA.
DR EMBL; HM053706; ADM62327.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45940.1; -; Genomic_DNA.
DR PIR; H70922; H70922.
DR RefSeq; NP_217646.1; NC_000962.3.
DR RefSeq; WP_003899932.1; NZ_NVQJ01000019.1.
DR AlphaFoldDB; P9WKC9; -.
DR SMR; P9WKC9; -.
DR STRING; 83332.Rv3130c; -.
DR SwissLipids; SLP:000001146; -.
DR iPTMnet; P9WKC9; -.
DR PaxDb; P9WKC9; -.
DR DNASU; 888841; -.
DR GeneID; 888841; -.
DR KEGG; mtu:Rv3130c; -.
DR TubercuList; Rv3130c; -.
DR eggNOG; COG1020; Bacteria.
DR OMA; RWAMLTK; -.
DR PhylomeDB; P9WKC9; -.
DR BRENDA; 2.3.1.20; 3445.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:MTBBASE.
DR GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IDA:MTBBASE.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045017; P:glycerolipid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IEP:MTBBASE.
DR GO; GO:0071731; P:response to nitric oxide; IEP:MTBBASE.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:MTBBASE.
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 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Glycerol metabolism; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..463
FT /note="Probable diacyglycerol O-acyltransferase tgs1"
FT /id="PRO_0000222916"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:21969609"
SQ SEQUENCE 463 AA; 50721 MW; 48CC60A8670F1D6B CRC64;
MNHLTTLDAG FLKAEDVDRH VSLAIGALAV IEGPAPDQEA FLSSLAQRLR PCTRFGQRLR
LRPFDLGAPK WVDDPDFDLG RHVWRIALPR PGNEDQLFEL IADLMARRLD RGRPLWEVWV
IEGLADSKWA ILTKLHHCMA DGIAATHLLA GLSDESMSDS FASNIHTTMQ SQSASVRRGG
FRVNPSEALT ASTAVMAGIV RAAKGASEIA AGVLSPAASS LNGPISDLRR YSAAKVPLAD
VEQVCRKFDV TINDVALAAI TESYRNVLIQ RGERPRFDSL RTLVPVSTRS NSALSKTDNR
VSLMLPNLPV DQENPLQRLR IVHSRLTRAK AGGQRQFGNT LMAIANRLPF PMTAWAVGLL
MRLPQRGVVT VATNVPGPRR PLQIMGRRVL DLYPVSPIAM QLRTSVAMLS YADDLYFGIL
ADYDVVADAG QLARGIEDAV ARLVAISKRR KVTRRRGALS LVV
