Y3371_MYCTU
ID Y3371_MYCTU Reviewed; 446 AA.
AC P9WKA9; L0TDY3; O50400;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Putative diacyglycerol O-acyltransferase Rv3371;
DE EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE AltName: Full=Putative triacylglycerol synthase Rv3371;
GN OrderedLocusNames=Rv3371; ORFNames=MTV004.29;
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 no wax synthase activity to produce wax
CC esters. {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; CCP46192.1; -; Genomic_DNA.
DR PIR; B70972; B70972.
DR RefSeq; NP_217888.1; NC_000962.3.
DR RefSeq; WP_003900036.1; NZ_NVQJ01000052.1.
DR AlphaFoldDB; P9WKA9; -.
DR SMR; P9WKA9; -.
DR STRING; 83332.Rv3371; -.
DR SwissLipids; SLP:000001177; -.
DR PaxDb; P9WKA9; -.
DR DNASU; 888053; -.
DR GeneID; 888053; -.
DR KEGG; mtu:Rv3371; -.
DR TubercuList; Rv3371; -.
DR eggNOG; COG1020; Bacteria.
DR OMA; FHAITHA; -.
DR PhylomeDB; P9WKA9; -.
DR BRENDA; 2.3.1.20; 3445.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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 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..446
FT /note="Putative diacyglycerol O-acyltransferase Rv3371"
FT /id="PRO_0000222919"
FT REGION 425..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 446 AA; 48847 MW; 0E7CC07E93CC15AD CRC64;
MAQLTALDAG FLKSRDPERH PGLAIGAVAV VNGAAPSYDQ LKTVLTERIK SIPRCTQVLA
TEWIDYPGFD LTQHVRRVAL PRPGDEAELF RAIALALERP LDPDRPLWEC WIIEGLNGNR
WAILIKIHHC MAGAMSAAHL LARLCDDADG SAFANNVDIK QIPPYGDARS WAETLWRMSV
SIAGAVCTAA ARAVSWPAVT SPAGPVTTRR RYQAVRVPRD AVDAVCHKFG VTANDVALAA
ITEGFRTVLL HRGQQPRADS LRTLEKTDGS SAMLPYLPVE YDDPVRRLRT VHNRSQQSGR
RQPDSLSDYT PLMLCAKMIH ALARLPQQGI VTLATSAPRP RHQLRLMGQK MDQVLPIPPT
ALQLSTGIAV LSYGDELVFG ITADYDAASE MQQLVNGIEL GVARLVALSD DSVLLFTKDR
RKRSSRALPS AARRGRPSVP TARARH
