Y2285_MYCTU
ID Y2285_MYCTU Reviewed; 445 AA.
AC P9WKB5; L0TBU7; P67206; Q50680;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Putative diacyglycerol O-acyltransferase Rv2285;
DE EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE AltName: Full=Putative triacylglycerol synthase Rv2285;
GN OrderedLocusNames=Rv2285; ORFNames=MTCY339.25c;
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, 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; CCP45067.1; -; Genomic_DNA.
DR PIR; A70732; A70732.
DR RefSeq; NP_216801.1; NC_000962.3.
DR RefSeq; WP_003411704.1; NZ_NVQJ01000012.1.
DR AlphaFoldDB; P9WKB5; -.
DR SMR; P9WKB5; -.
DR STRING; 83332.Rv2285; -.
DR SwissLipids; SLP:000001151; -.
DR PaxDb; P9WKB5; -.
DR GeneID; 45426264; -.
DR GeneID; 888632; -.
DR KEGG; mtu:Rv2285; -.
DR TubercuList; Rv2285; -.
DR eggNOG; COG1020; Bacteria.
DR OMA; TPFNTRI; -.
DR PhylomeDB; P9WKB5; -.
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 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..445
FT /note="Putative diacyglycerol O-acyltransferase Rv2285"
FT /id="PRO_0000222910"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 47707 MW; 0AF79D2A7EC103EB CRC64;
MKLLSPLDQM FARMEAPRTP MHIGAFAVFD LPKGAPRRFI RDLYEAISQL AFLPFPFDSV
IAGGASMAYW RQVQPDPSYH VRLSALPYPG TGRDLGALVE RLHSTPLDMA KPLWELHLIE
GLTGRQFAMY FKAHHCAVDG LGGVNLIKSW LTTDPEAPPG SGKPEPFGDD YDLASVLAAA
TTKRAVEGVS AVSELAGRLS SMVLGANSSV RAALTTPRTP FNTRVNRHRR LAVQVLKLPR
LKAVAHATDC TVNDVILASV GGACRRYLQE LGDLPTNTLT ASVPVGFERD ADTVNAASGF
VAPLGTSIED PVARLTTISA STTRGKAELL AMSPNALQHY SVFGLLPIAV GQKTGALGVI
PPLFNFTVSN VVLSKDPLYL SGAKLDVIVP MSFLCDGYGL NVTLVGYTDK VVLGFLGCRD
TLPHLQRLAQ YTGAAFEELE TAALP
