TGS3_MYCTU
ID TGS3_MYCTU Reviewed; 271 AA.
AC P9WKC5; L0TC77; O05879;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Probable diacyglycerol O-acyltransferase tgs3;
DE Short=TGS3;
DE EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE AltName: Full=Probable triacylglycerol synthase tgs3;
GN Name=tgs3; OrderedLocusNames=Rv3234c; ORFNames=MTCY20B11.09c;
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, AND INDUCTION BY
RP HYPOXIA.
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. Has no wax synthase activity to produce wax esters.
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=(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 pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:15262939};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- INDUCTION: A possible member of the dormancy regulon. Induced in
CC response to reduced oxygen tension (hypoxia), it is not induced by
CC nitric oxide exposure. {ECO:0000269|PubMed:15262939}.
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, however this protein still
CC has diacyglycerol O-acyltransferase activity in E.coli. {ECO:0000305}.
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DR EMBL; AL123456; CCP46053.1; -; Genomic_DNA.
DR PIR; D70591; D70591.
DR RefSeq; NP_217751.1; NC_000962.3.
DR RefSeq; WP_003899981.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; P9WKC5; -.
DR SMR; P9WKC5; -.
DR STRING; 83332.Rv3234c; -.
DR SwissLipids; SLP:000001148; -.
DR PaxDb; P9WKC5; -.
DR DNASU; 888767; -.
DR GeneID; 888767; -.
DR KEGG; mtu:Rv3234c; -.
DR PATRIC; fig|83332.111.peg.3612; -.
DR TubercuList; Rv3234c; -.
DR eggNOG; COG1020; Bacteria.
DR PhylomeDB; P9WKC5; -.
DR BRENDA; 2.3.1.20; 3445.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:MTBBASE.
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 1: Evidence at protein level;
KW Acyltransferase; Glycerol metabolism; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..271
FT /note="Probable diacyglycerol O-acyltransferase tgs3"
FT /id="PRO_0000222918"
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
