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 25-MAY-2022, entry version 37.
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., 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 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., Puzo G.,
RA Gicquel B., Riviere M., Jackson M.;
RT "Genetic basis for the biosynthesis of methylglucose lipopolysaccharides in
RT 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., Daffe M.,
RA Jackson M.;
RT "Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis:
RT 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., 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: Glucosyltransferase that uses UDP-glucose as the sugar donor
CC to elongate alpha-(1->4)-glucans. Is involved in the biosynthesis of
CC both 6-O-methylglucosyl lipopolysaccharides (MGLP) and glycogen. May
CC also use ADP-glucose as substrate. {ECO:0000269|PubMed:17640872,
CC ECO:0000269|PubMed:18808383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11;
CC Evidence={ECO:0000269|PubMed:17640872};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:18808383}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of Rv3032 affects the production of
CC both glycogen (two-fold reduction) and 6-O-methylglucosyl
CC lipopolysaccharides (MGLP), but not that of capsular alpha-D-glucan.
CC Cells lacking this gene are not affected in their multiplication or
CC persistence in the BALB/c mouse infection model. They also show a
CC slightly slower growth than that of wild-type at 37 degrees Celsius and
CC a completely abolished growth at 39 degrees Celsius. Moreover, in
CC contrast to wild-type, they are exceptionally sensitive to the TreS
CC inhibitor validamycin A; the sensitivity is abolished by overexpression
CC of TreS. {ECO:0000269|PubMed:17640872, ECO:0000269|PubMed:18808383,
CC ECO:0000269|PubMed:20305657}.
CC -!- MISCELLANEOUS: Attempts to disrupt both the Rv3032 gene and glgA in
CC order to create a mutant simultaneously deficient in both alpha-1,4-
CC glucosyltransferases turned out to be unsuccessful. Thus,
CC M.tuberculosis H37Rv requires a functional copy of at least one of
CC these two genes for growth. Moreover, it is not possible to inactivate
CC Rv3032 in a mutant lacking treS, suggesting the joint essentiality of
CC the different alpha-(1->4)-glucans biosynthesis pathways involving
CC these two genes.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000305}.
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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_NVQJ01000011.1.
DR AlphaFoldDB; P9WMY9; -.
DR SMR; P9WMY9; -.
DR STRING; 83332.Rv3032; -.
DR PaxDb; P9WMY9; -.
DR DNASU; 888185; -.
DR GeneID; 888185; -.
DR KEGG; mtu:Rv3032; -.
DR TubercuList; Rv3032; -.
DR eggNOG; COG0297; Bacteria.
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:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; 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; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..414
FT /note="Glycogen synthase"
FT /id="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
