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Y221_MYCTU
ID   Y221_MYCTU              Reviewed;         469 AA.
AC   P9WKB7; L0T2V6; P96403;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Putative diacyglycerol O-acyltransferase Rv0221;
DE            EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE   AltName: Full=Putative triacylglycerol synthase Rv0221;
GN   OrderedLocusNames=Rv0221; ORFNames=MTCY08D5.16;
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 NITRIC OXIDE
RP   (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: Induced in response to low levels of nitric oxide (NO).
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; CCP42949.1; -; Genomic_DNA.
DR   PIR; C70961; C70961.
DR   RefSeq; NP_214735.1; NC_000962.3.
DR   RefSeq; WP_003900834.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; P9WKB7; -.
DR   SMR; P9WKB7; -.
DR   STRING; 83332.Rv0221; -.
DR   SwissLipids; SLP:000001175; -.
DR   PaxDb; P9WKB7; -.
DR   DNASU; 886719; -.
DR   GeneID; 886719; -.
DR   KEGG; mtu:Rv0221; -.
DR   TubercuList; Rv0221; -.
DR   eggNOG; COG1020; Bacteria.
DR   OMA; VVGKIHH; -.
DR   PhylomeDB; P9WKB7; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IBA:GO_Central.
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: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   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..469
FT                   /note="Putative diacyglycerol O-acyltransferase Rv0221"
FT                   /id="PRO_0000222905"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   469 AA;  51862 MW;  8569D83717BA946B CRC64;
     MKRLSGWDAV LLYSETPNVH MHTLKVAVIE LDSDRQEFGV DAFREVIAGR LHKLEPLGYQ
     LVDVPLKFHH PMWREHCQVD LNYHIRPWRL RAPGGRRELD EAVGEIASTP LNRDHPLWEM
     YFVEGLANHR IAVVAKIHHA LADGVASANM MARGMDLLPG PEVGRYVPDP APTKRQLLSA
     AFIDHLRHLG RIPATIRYTT QGLGRVRRSS RKLSPALTMP FTPPPTFMNH RLTPERRFAT
     ATLALIDVKA TAKLLGATIN DMVLAMSTGA LRTLLLRYDG KAEPLLASVP VSYDFSPERI
     SGNRFTGMLV ALPADSDDPL QRVRVCHENA VSAKESHQLL GPELISRWAA YWPPAGAEAL
     FRWLSERDGQ NKVLNLNISN VPGPRERGRV GAALVTEIYS VGPLTAGSGL NITVWSYVDQ
     LNISVLTDGS TVQDPHEVTA GMIADFIEIR RAAGLSVELT VVESAMAQA
 
 
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