TGS2_MYCTU
ID TGS2_MYCTU Reviewed; 454 AA.
AC P9WKC7; 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 44.
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:0000269|PubMed:15262939};
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase;
DE EC=2.3.1.75 {ECO:0000269|PubMed:15262939};
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=Rv3734c; ORFNames=MTV025.082c;
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 [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 [2]
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 [3]
RP IDENTIFICATION BY MASS 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.
CC {ECO:0000250|UniProtKB:P9WKC9}.
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. Also functions as a wax synthase, incorporating palmityl
CC alcohol into wax esters in the presence of palmitoyl-CoA.
CC {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=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: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 -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl
CC hexadecanoate; Xref=Rhea:RHEA:38167, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75584;
CC Evidence={ECO:0000269|PubMed:15262939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168;
CC Evidence={ECO:0000269|PubMed:15262939};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.2. {ECO:0000269|PubMed:15262939};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- INDUCTION: A possible member of the dormancy regulon. Slightly induced
CC in response to reduced oxygen tension (hypoxia) and by low levels of
CC nitric oxide (NO). It is hoped that this regulon will give insight into
CC the latent, or dormant phase of infection.
CC {ECO:0000269|PubMed:15262939}.
CC -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46561.1; -; Genomic_DNA.
DR PIR; G70797; G70797.
DR RefSeq; NP_218251.1; NC_000962.3.
DR RefSeq; WP_003420440.1; NZ_NVQJ01000009.1.
DR AlphaFoldDB; P9WKC7; -.
DR SMR; P9WKC7; -.
DR STRING; 83332.Rv3734c; -.
DR SwissLipids; SLP:000001147; -.
DR PaxDb; P9WKC7; -.
DR DNASU; 885335; -.
DR GeneID; 885335; -.
DR KEGG; mtu:Rv3734c; -.
DR TubercuList; Rv3734c; -.
DR eggNOG; COG1020; Bacteria.
DR OMA; FQPTFRK; -.
DR PhylomeDB; P9WKC7; -.
DR BRENDA; 2.3.1.20; 3445.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0102966; F:arachidoyl-CoA:1-dodecanol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:MTBBASE.
DR GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IBA:GO_Central.
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 Acyltransferase; Glycerol metabolism; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..454
FT /note="Probable diacyglycerol O-acyltransferase tgs2"
FT /id="PRO_0000222921"
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
