ID   Y1760_MYCTU             Reviewed;         502 AA.
AC   P9WKB9; L0T7L6; O06795;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Putative diacyglycerol O-acyltransferase Rv1760;
DE            EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE   AltName: Full=Putative triacylglycerol synthase Rv1760;
GN   OrderedLocusNames=Rv1760; ORFNames=MTCY28.26;
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   EXPRESSION IN E.COLI, CATALYTIC ACTIVITY, AND INDUCTION BY HYPOXIA AND BY
RP   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 weakly as a
CC       triacylglycerol synthase, making triacylglycerol (TG) from diolein and
CC       long-chain fatty acyl-CoA. Has very weak wax synthase activity,
CC       incorporating palmityl alcohol into wax esters in the presence of
CC       palmitoyl-CoA. {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   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- INDUCTION: A possible member of the dormancy regulon. Induced in
CC       response to reduced oxygen tension (hypoxia) and low levels of nitric
CC       oxide (NO). It is hoped that this regulon will give insight into the
CC       latent, or dormant phase of infection. {ECO:0000269|PubMed:15262939}.
CC   -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP44526.1; -; Genomic_DNA.
DR   PIR; A70988; A70988.
DR   RefSeq; NP_216276.1; NC_000962.3.
DR   RefSeq; WP_010886129.1; NC_000962.3.
DR   AlphaFoldDB; P9WKB9; -.
DR   SMR; P9WKB9; -.
DR   STRING; 83332.Rv1760; -.
DR   SwissLipids; SLP:000001150; -.
DR   PaxDb; P9WKB9; -.
DR   DNASU; 885556; -.
DR   GeneID; 885556; -.
DR   KEGG; mtu:Rv1760; -.
DR   PATRIC; fig|83332.111.peg.1959; -.
DR   TubercuList; Rv1760; -.
DR   eggNOG; COG1020; Bacteria.
DR   OMA; RNQTTWM; -.
DR   PhylomeDB; P9WKB9; -.
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; IBA:GO_Central.
DR   GO; GO:0071731; P:response to nitric oxide; IBA:GO_Central.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR014292; Acyl_transf_WS/DGAT.
DR   InterPro; IPR023213; CAT-like_dom_sf.
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..502
FT                   /note="Putative diacyglycerol O-acyltransferase Rv1760"
FT                   /id="PRO_0000222909"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   502 AA;  54092 MW;  833B9D3F900A43F2 CRC64;
     MPRGCAGARF ACNACLNFLA GLGISEPISP GWAAMERLSG LDAFFLYMET PSQPLNVCCV
     LELDTSTMPG GYTYGRFHAA LEKYVKAAPE FRMKLADTEL NLDHPVWVDD DNFQIRHHLR
     RVAMPAPGGR RELAEICGYI AGLPLDRDRP LWEMWVIEGG ARSDTVAVML KVHHAVVDGV
     AGANLLSHLC SLQPDAPAPQ PVRGTGGGNV LQIAASGLEG FASRPVRLAT VVPATVLTLV
     RTLLRAREGR TMAAPFSAPP TPFNGPLGRL RNIAYTQLDM RDVKRVKDRF GVTINDVVVA
     LCAGALRRFL LEHGVLPEAP LVATVPVSVH DKSDRPGRNQ ATWMFCRVPS QISDPAQRIR
     TIAAGNTVAK DHAAAIGPTL LHDWIQFGGS TMFGAAMRIL PHISITHSPA YNLILSNVPG
     PQAQLYFLGC RMDSMFPLGP LLGNAGLNIT VMSLNGELGV GIVSCPDLLP DLWGVADGFP
     EALKELLECS DDQPEGSNHQ DS