ID   GLGM_MYCTO              Reviewed;         387 AA.
AC   P9WMZ0; L0T8Z4; O05313; Q7D8L6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Alpha-maltose-1-phosphate synthase {ECO:0000250|UniProtKB:P9WMZ1};
DE            Short=M1P synthase {ECO:0000250|UniProtKB:P9WMZ1};
DE            EC=2.4.1.342 {ECO:0000250|UniProtKB:P9WMZ1};
DE   AltName: Full=ADP-alpha-D-glucose:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase {ECO:0000250|UniProtKB:P9WMZ1};
DE   AltName: Full=M1P-producing glucosyltransferase {ECO:0000250|UniProtKB:P9WMZ1};
GN   Name=glgM {ECO:0000250|UniProtKB:P9WMZ1}; Synonyms=glgA;
GN   OrderedLocusNames=MT1250;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Involved in the biosynthesis of the maltose-1-phosphate (M1P)
CC       building block required for alpha-glucan production by the key enzyme
CC       GlgE. Catalyzes the formation of an alpha-1,4 linkage between glucose
CC       from ADP-glucose and glucose 1-phosphate (G1P) to yield maltose-1-
CC       phosphate (M1P). {ECO:0000250|UniProtKB:P9WMZ1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-alpha-D-glucose + alpha-D-glucose 1-phosphate = ADP +
CC         alpha-maltose 1-phosphate + H(+); Xref=Rhea:RHEA:50692,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:63576, ChEBI:CHEBI:456216; EC=2.4.1.342;
CC         Evidence={ECO:0000250|UniProtKB:P9WMZ1};
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WMZ1}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WMZ1}.
CC   -!- MISCELLANEOUS: Maltose-1-phosphate (M1P) is generated by two
CC       alternative routes: the TreS-Pep2 branch and the GlgC-GlgM branch,
CC       however it seems that TreS-Pep2 branch provides most of M1P for the
CC       GlgE pathway in M.tuberculosis. {ECO:0000250|UniProtKB:P9WMZ1}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45507.1; -; Genomic_DNA.
DR   PIR; B70610; B70610.
DR   RefSeq; WP_003898773.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMZ0; -.
DR   SMR; P9WMZ0; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; AAK45507; AAK45507; MT1250.
DR   KEGG; mtc:MT1250; -.
DR   PATRIC; fig|83331.31.peg.1351; -.
DR   HOGENOM; CLU_009583_2_3_11; -.
DR   UniPathway; UPA00164; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   InterPro; IPR011875; M1P_synthase.
DR   Pfam; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   TIGRFAMs; TIGR02149; glgA_Coryne; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Carbohydrate metabolism;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..387
FT                   /note="Alpha-maltose-1-phosphate synthase"
FT                   /id="PRO_0000427218"
SQ   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