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Alpha-maltose-1-phosphate synthase (M1P synthase) (EC 2.4.1.342) (ADP-alpha-D-glucose:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase) (M1P-producing glucosyltransferase)

 GLGM_MYCTU              Reviewed;         387 AA.
P9WMZ1; L0T8Z4; O05313; Q7D8L6;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
13-FEB-2019, entry version 30.
RecName: Full=Alpha-maltose-1-phosphate synthase {ECO:0000303|PubMed:27513637};
Short=M1P synthase {ECO:0000303|PubMed:27513637};
EC=2.4.1.342 {ECO:0000269|PubMed:27513637};
AltName: Full=ADP-alpha-D-glucose:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase {ECO:0000305|PubMed:27513637};
AltName: Full=M1P-producing glucosyltransferase {ECO:0000303|PubMed:27513637};
Name=glgM {ECO:0000303|PubMed:27513637}; Synonyms=glgA;
OrderedLocusNames=Rv1212c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18808383; DOI=10.1111/j.1365-2958.2008.06445.x;
Sambou T., Dinadayala P., Stadthagen G., Barilone N., Bordat Y.,
Constant P., Levillain F., Neyrolles O., Gicquel B., Lemassu A.,
Daffe M., Jackson M.;
"Capsular glucan and intracellular glycogen of Mycobacterium
tuberculosis: biosynthesis and impact on the persistence in mice.";
Mol. Microbiol. 70:762-774(2008).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
DISRUPTION PHENOTYPE, ACTIVITY REGULATION, PATHWAY, AND SUBSTRATE
SPECIFICITY.
PubMed=27513637; DOI=10.1371/journal.ppat.1005768;
Koliwer-Brandl H., Syson K., van de Weerd R., Chandra G.,
Appelmelk B., Alber M., Ioerger T.R., Jacobs W.R. Jr., Geurtsen J.,
Bornemann S., Kalscheuer R.;
"Metabolic network for the biosynthesis of intra- and extracellular
alpha-glucans required for virulence of Mycobacterium tuberculosis.";
PLoS Pathog. 12:E1005768-E1005768(2016).
-!- FUNCTION: Involved in the biosynthesis of the maltose-1-phosphate
(M1P) building block required for alpha-glucan production by the
key enzyme GlgE (PubMed:18808383, PubMed:27513637). Catalyzes the
formation of an alpha-1,4 linkage between glucose from ADP-glucose
and glucose 1-phosphate (G1P) to yield maltose-1-phosphate (M1P)
(PubMed:27513637). Also able to catalyze the elongation of the
non-reducing ends of glycogen, maltodextrin and maltoheptaose
using ADP-glucose as sugar donor, however the rate of the reaction
appears to be too low to be physiologically relevant
(PubMed:27513637). GlgM is also able to use UDP-glucose as sugar
donor with G1P, however, it is less efficient than with ADP-
glucose (PubMed:27513637). UDP-glucose is not used as sugar donor
when glycogen is used as acceptor (PubMed:27513637).
{ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
-!- CATALYTIC ACTIVITY:
Reaction=ADP-alpha-D-glucose + alpha-D-glucose 1-phosphate = ADP +
alpha-maltose 1-phosphate + H(+); Xref=Rhea:RHEA:50692,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:58601,
ChEBI:CHEBI:63576, ChEBI:CHEBI:456216; EC=2.4.1.342;
Evidence={ECO:0000269|PubMed:27513637};
-!- ACTIVITY REGULATION: Inhibited at high G1P concentrations.
{ECO:0000269|PubMed:27513637}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.046 mM for ADP-glucose (with 4 mM of G1P)
{ECO:0000269|PubMed:27513637};
KM=0.063 mM for ADP-glucose (with 2.5 mM of G1P)
{ECO:0000269|PubMed:27513637};
KM=0.121 mM for ADP-glucose (with 1 mM of G1P)
{ECO:0000269|PubMed:27513637};
KM=0.145 mM for ADP-glucose (with 0.25 mM of G1P)
{ECO:0000269|PubMed:27513637};
KM=0.4 mM for alpha-glucan {ECO:0000269|PubMed:27513637};
KM=0.695 mM for G1P (with 4 mM of ADP-glucose)
{ECO:0000269|PubMed:27513637};
KM=0.816 mM for G1P (with 0.1 mM of ADP-glucose)
{ECO:0000269|PubMed:27513637};
KM=0.9 mM for rabbit liver glycogen
{ECO:0000269|PubMed:27513637};
KM=1.290 mM for G1P (with 0.5 mM of ADP-glucose)
{ECO:0000269|PubMed:27513637};
Vmax=136 umol/min/mg enzyme toward G1P (with 0.5 mM of ADP-
glucose) {ECO:0000269|PubMed:27513637};
Vmax=113 umol/min/mg enzyme toward G1P (with 4 mM of ADP-
glucose) {ECO:0000269|PubMed:27513637};
Vmax=54.2 umol/min/mg enzyme toward G1P (with 0.1 mM of ADP-
glucose) {ECO:0000269|PubMed:27513637};
Vmax=40.5 umol/min/mg enzyme toward ADP-glucose (with 1 mM of
G1P) {ECO:0000269|PubMed:27513637};
Vmax=27.7 umol/min/mg enzyme toward ADP-glucose (with 0.25 mM of
G1P) {ECO:0000269|PubMed:27513637};
Vmax=27.5 umol/min/mg enzyme toward ADP-glucose (with 2.5 mM of
G1P) {ECO:0000269|PubMed:27513637};
Vmax=21.4 umol/min/mg enzyme toward ADP-glucose (with 4 mM of
G1P) {ECO:0000269|PubMed:27513637};
Vmax=0.12 umol/min/mg enzyme with rabbit liver glycogen as
substrate {ECO:0000269|PubMed:27513637};
Vmax=0.02 umol/min/mg enzyme with alpha-glucan as substrate
{ECO:0000269|PubMed:27513637};
Note=Kcat is 97.9 sec(-1) for G1P as substrate (with 0.5 mM of
ADP-glucose). Kcat is 80.6 sec(-1) for G1P as substrate (with 4
mM of ADP-glucose). Kcat is 39 sec(-1) for G1P as substrate
(with 0.1 mM of ADP-glucose). Kcat is 29.2 sec(-1) for ADP-
glucose as substrate (with 1 mM of G1P). Kcat is 20 sec(-1) for
ADP-glucose as substrate (with 0.25 mM of G1P). Kcat is 19.8
sec(-1) for ADP-glucose as substrate (with 2.5 mM of G1P). Kcat
is 15.4 sec(-1) for ADP-glucose as substrate (with 4 mM of G1P).
Kcat is 0.09 sec(-1) for rabbit liver glycogen as substrate.
Kcat is 0.014 sec(-1) for alpha-glucan as substrate.
{ECO:0000269|PubMed:27513637};
-!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
{ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
-!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
{ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
-!- DISRUPTION PHENOTYPE: Inactivation of glgM affects the production
of extracellular alpha-glucan (two-fold reduction), but not that
of intracellular glycogen and 6-O-methylglucosyl
lipopolysaccharides (MGLP) (PubMed:18808383, PubMed:27513637).
Cells lacking this gene are also impaired in their ability to
persist in both the spleen and the lungs of mice
(PubMed:18808383). Combined inactivation of both glgM and ostA is
lethal, potentially due to accumulation of toxic levels of ADP-
glucose (PubMed:27513637). Combined inactivation of both glgM and
treS results in absence of alpha-glucan (PubMed:27513637).
{ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
-!- MISCELLANEOUS: Maltose-1-phosphate (M1P) is generated by two
alternative routes: the TreS-Pep2 branch and the GlgC-GlgM branch,
however it seems that TreS-Pep2 branch provides most of M1P for
the GlgE pathway in M.tuberculosis. {ECO:0000269|PubMed:27513637}.
-!- MISCELLANEOUS: Attempts to disrupt both the Rv3032 gene and glgA
in order to create a mutant simultaneously deficient in both
alpha-1,4-glucosyltransferases turned out to be unsuccessful.
Thus, M.tuberculosis H37Rv requires a functional copy of at least
one of these two genes for growth. {ECO:0000269|PubMed:18808383}.
-!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP43968.1; -; Genomic_DNA.
PIR; B70610; B70610.
RefSeq; NP_215728.1; NC_000962.3.
RefSeq; WP_003898773.1; NZ_NVQJ01000039.1.
ProteinModelPortal; P9WMZ1; -.
SMR; P9WMZ1; -.
STRING; 83332.Rv1212c; -.
PaxDb; P9WMZ1; -.
EnsemblBacteria; CCP43968; CCP43968; Rv1212c.
GeneID; 887805; -.
KEGG; mtu:Rv1212c; -.
TubercuList; Rv1212c; -.
eggNOG; ENOG4107QPH; Bacteria.
eggNOG; COG0438; LUCA.
KO; K16148; -.
OMA; LLHGIPH; -.
PhylomeDB; P9WMZ1; -.
BioCyc; MetaCyc:G185E-5382-MONOMER; -.
BioCyc; MTBH37RV:G185E-5382-MONOMER; -.
UniPathway; UPA00164; -.
UniPathway; UPA00934; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009250; P:glucan biosynthetic process; IMP:MTBBASE.
GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR001296; Glyco_trans_1.
InterPro; IPR028098; Glyco_trans_4-like_N.
InterPro; IPR011875; M1P_synthase.
Pfam; PF13439; Glyco_transf_4; 1.
Pfam; PF00534; Glycos_transf_1; 1.
TIGRFAMs; TIGR02149; glgA_Coryne; 1.
1: Evidence at protein level;
Capsule biogenesis/degradation; Carbohydrate metabolism;
Complete proteome; Glycosyltransferase; Reference proteome;
Transferase.
CHAIN 1 387 Alpha-maltose-1-phosphate synthase.
/FTId=PRO_0000413978.
SEQUENCE 387 AA; 41533 MW; BC4C4B66980BAAFF CRC64;
MRVAMLTREY PPEVYGGAGV HVTELVAYLR RLCAVDVHCM GAPRPGAFAY RPDPRLGSAN
AALSTLSADL VMANAASAAT VVHSHTWYTA LAGHLAAILY DIPHVLTAHS LEPLRPWKKE
QLGGGYQVST WVEQTAVLAA NAVIAVSSAM RNDMLRVYPS LDPNLVHVIR NGIDTETWYP
AGPARTGSVL AELGVDPNRP MAVFVGRITR QKGVVHLVTA AHRFRSDVQL VLCAGAADTP
EVADEVRVAV AELARNRTGV FWIQDRLTIG QLREILSAAT VFVCPSVYEP LGIVNLEAMA
CATAVVASDV GGIPEVVADG ITGSLVHYDA DDATGYQARL AEAVNALVAD PATAERYGHA
GRQRCIQEFS WAYIAEQTLD IYRKVCA


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