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Database: UniProt/SWISS-PROT
Entry: GLGSY_MYCTU
LinkDB: GLGSY_MYCTU
Original site: GLGSY_MYCTU 
ID   GLGSY_MYCTU             Reviewed;         414 AA.
AC   P9WMY9; L0TCY4; O53279; Q7D693;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   23-MAY-2018, entry version 21.
DE   RecName: Full=Glycogen synthase;
DE            EC=2.4.1.11;
DE   AltName: Full=Alpha-1,4-glucosyltransferase Rv3032;
DE   AltName: Full=UDP-glucose--glycogen glucosyltransferase;
GN   OrderedLocusNames=Rv3032;
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.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION IN MGLP AND GLYCOGEN BIOSYNTHESIS, CATALYTIC ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=17640872; DOI=10.1074/jbc.M702676200;
RA   Stadthagen G., Sambou T., Guerin M., Barilone N., Boudou F.,
RA   Kordulakova J., Charles P., Alzari P.M., Lemassu A., Daffe M.,
RA   Puzo G., Gicquel B., Riviere M., Jackson M.;
RT   "Genetic basis for the biosynthesis of methylglucose
RT   lipopolysaccharides in Mycobacterium tuberculosis.";
RL   J. Biol. Chem. 282:27270-27276(2007).
RN   [3]
RP   FUNCTION IN GLYCOGEN BIOSYNTHESIS, DISRUPTION PHENOTYPE, AND PATHWAY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=18808383; DOI=10.1111/j.1365-2958.2008.06445.x;
RA   Sambou T., Dinadayala P., Stadthagen G., Barilone N., Bordat Y.,
RA   Constant P., Levillain F., Neyrolles O., Gicquel B., Lemassu A.,
RA   Daffe M., Jackson M.;
RT   "Capsular glucan and intracellular glycogen of Mycobacterium
RT   tuberculosis: biosynthesis and impact on the persistence in mice.";
RL   Mol. Microbiol. 70:762-774(2008).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND SYNTHETIC LETHALITY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=20305657; DOI=10.1038/nchembio.340;
RA   Kalscheuer R., Syson K., Veeraraghavan U., Weinrick B., Biermann K.E.,
RA   Liu Z., Sacchettini J.C., Besra G., Bornemann S., Jacobs W.R. Jr.;
RT   "Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an
RT   alpha-glucan pathway.";
RL   Nat. Chem. Biol. 6:376-384(2010).
RN   [5]
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.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Glucosyltransferase that uses UDP-glucose as the sugar
CC       donor to elongate alpha-(1->4)-glucans. Is involved in the
CC       biosynthesis of both 6-O-methylglucosyl lipopolysaccharides (MGLP)
CC       and glycogen. May also use ADP-glucose as substrate.
CC       {ECO:0000269|PubMed:17640872, ECO:0000269|PubMed:18808383}.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC       {ECO:0000269|PubMed:17640872}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000269|PubMed:18808383}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of Rv3032 affects the
CC       production of both glycogen (two-fold reduction) and 6-O-
CC       methylglucosyl lipopolysaccharides (MGLP), but not that of
CC       capsular alpha-D-glucan. Cells lacking this gene are not affected
CC       in their multiplication or persistence in the BALB/c mouse
CC       infection model. They also show a slightly slower growth than that
CC       of wild-type at 37 degrees Celsius and a completely abolished
CC       growth at 39 degrees Celsius. Moreover, in contrast to wild-type,
CC       they are exceptionally sensitive to the TreS inhibitor validamycin
CC       A; the sensitivity is abolished by overexpression of TreS.
CC       {ECO:0000269|PubMed:17640872, ECO:0000269|PubMed:18808383,
CC       ECO:0000269|PubMed:20305657}.
CC   -!- MISCELLANEOUS: Attempts to disrupt both the Rv3032 gene and glgA
CC       in order to create a mutant simultaneously deficient in both
CC       alpha-1,4-glucosyltransferases turned out to be unsuccessful.
CC       Thus, M.tuberculosis H37Rv requires a functional copy of at least
CC       one of these two genes for growth. Moreover, it is not possible to
CC       inactivate Rv3032 in a mutant lacking treS, suggesting the joint
CC       essentiality of the different alpha-(1->4)-glucans biosynthesis
CC       pathways involving these two genes.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
DR   EMBL; AL123456; CCP45840.1; -; Genomic_DNA.
DR   PIR; C70859; C70859.
DR   RefSeq; NP_217548.1; NC_000962.3.
DR   RefSeq; WP_003415928.1; NZ_KK339370.1.
DR   ProteinModelPortal; P9WMY9; -.
DR   SMR; P9WMY9; -.
DR   STRING; 83332.Rv3032; -.
DR   PaxDb; P9WMY9; -.
DR   PRIDE; P9WMY9; -.
DR   EnsemblBacteria; CCP45840; CCP45840; Rv3032.
DR   GeneID; 888185; -.
DR   KEGG; mtu:Rv3032; -.
DR   TubercuList; Rv3032; -.
DR   eggNOG; ENOG4107T3Q; Bacteria.
DR   eggNOG; COG0438; LUCA.
DR   KO; K16150; -.
DR   OMA; WEFPPRI; -.
DR   PhylomeDB; P9WMY9; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IMP:MTBBASE.
DR   GO; GO:0040007; P:growth; IMP:MTBBASE.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:MTBBASE.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   Pfam; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Glycogen biosynthesis;
KW   Glycogen metabolism; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN         1    414       Glycogen synthase.
FT                                /FTId=PRO_0000413905.
SQ   SEQUENCE   414 AA;  44805 MW;  64ADC7A4EA17A0DE CRC64;
     MRILMVSWEY PPVVIGGLGR HVHHLSTALA AAGHDVVVLS RCPSGTDPST HPSSDEVTEG
     VRVIAAAQDP HEFTFGNDMM AWTLAMGHAM IRAGLRLKKL GTDRSWRPDV VHAHDWLVAH
     PAIALAQFYD VPMVSTIHAT EAGRHSGWVS GALSRQVHAV ESWLVRESDS LITCSASMND
     EITELFGPGL AEITVIRNGI DAARWPFAAR RPRTGPAELL YVGRLEYEKG VHDAIAALPR
     LRRTHPGTTL TIAGEGTQQD WLIDQARKHR VLRATRFVGH LDHTELLALL HRADAAVLPS
     HYEPFGLVAL EAAAAGTPLV TSNIGGLGEA VINGQTGVSC APRDVAGLAA AVRSVLDDPA
     AAQRRARAAR QRLTSDFDWQ TVATATAQVY LAAKRGERQP QPRLPIVEHA LPDR
//
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