ID   Y3480_MYCTU             Reviewed;         497 AA.
AC   P9WKA7; L0TE90; O06343;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Putative diacyglycerol O-acyltransferase Rv3480c;
DE            EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE   AltName: Full=Putative triacylglycerol synthase Rv3480c;
GN   OrderedLocusNames=Rv3480c; ORFNames=MTCY13E12.33c;
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.
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: Upon expression in E.coli has a weak triacylglycerol synthase
CC       function, making triacylglycerol (TG) from diolein and long-chain fatty
CC       acyl-CoA. Also functions weakly as a wax synthase, as it incorporates
CC       palmityl alcohol into wax esters in the presence of palmitoyl-CoA.
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   -!- 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   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- INDUCTION: Constitutively expressed at a low level, it is not further
CC       induced by hypoxia or nitric oxide exposure.
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; CCP46302.1; -; Genomic_DNA.
DR   PIR; E70568; E70568.
DR   RefSeq; NP_217997.1; NC_000962.3.
DR   RefSeq; WP_003418921.1; NZ_NVQJ01000042.1.
DR   AlphaFoldDB; P9WKA7; -.
DR   SMR; P9WKA7; -.
DR   STRING; 83332.Rv3480c; -.
DR   SwissLipids; SLP:000001153; -.
DR   PaxDb; P9WKA7; -.
DR   GeneID; 888473; -.
DR   KEGG; mtu:Rv3480c; -.
DR   TubercuList; Rv3480c; -.
DR   eggNOG; COG1020; Bacteria.
DR   OMA; PWELHVI; -.
DR   PhylomeDB; P9WKA7; -.
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; IBA:GO_Central.
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; 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..497
FT                   /note="Putative diacyglycerol O-acyltransferase Rv3480c"
FT                   /id="PRO_0000222920"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  53315 MW;  90D661E32B5658C2 CRC64;
     MSQTARRLGP QDMFFLYSES STTMMHVGAL MPFTPPSGAP PDLLRQLVDE SKASEVVEPW
     SLRLSHPELL YHPTQSWVVD DNFDLDYHVR RSALASPGDE RELGIPVSRL HSHALDLRRP
     PWEVHFIEGL EGGRFAIYIK MHHSLIDGYT GQKMLARSLS TDPHDTTHPL FFNIPTPGRS
     PADTQDSVGG GLIAGAGNVL DGLGDVVRGL GGLVSGVGSV LGSVAGAGRS TFELTKALVN
     AQLRSDHEYR NLVGSVQAPH CILNTRISRN RRFATQQYPL DRLKAIGAQY DATINDVALA
     IIGGGLRRFL DELGELPNKS LIVVLPVNVR PKDDEGGGNA VATILATLGT DVADPVQRLA
     AVTASTRAAK AQLRSMDKDA ILAYSAALMA PYGVQLASTL SGVKPPWPYT FNLCVSNVPG
     PEDVLYLRGS RMEASYPVSL VAHSQALNVT LQSYAGTLNF GFIGCRDTLP HLQRLAVYTG
     EALDQLAAAD GAAGLGS