GLGM_MYCS2
ID GLGM_MYCS2 Reviewed; 387 AA.
AC A0R2E2;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Alpha-maltose-1-phosphate synthase {ECO:0000303|PubMed:27513637};
DE Short=M1P synthase {ECO:0000303|PubMed:27513637};
DE EC=2.4.1.342 {ECO:0000305|PubMed:27513637};
DE AltName: Full=ADP-alpha-D-glucose:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase {ECO:0000305|PubMed:27513637};
DE AltName: Full=M1P-producing glucosyltransferase {ECO:0000303|PubMed:27513637};
GN Name=glgM {ECO:0000303|PubMed:27513637}; Synonyms=glgA;
GN OrderedLocusNames=MSMEG_5080 {ECO:0000312|EMBL:ABK70457.1},
GN MSMEI_4954 {ECO:0000312|EMBL:AFP41398.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=27513637; DOI=10.1371/journal.ppat.1005768;
RA Koliwer-Brandl H., Syson K., van de Weerd R., Chandra G., Appelmelk B.,
RA Alber M., Ioerger T.R., Jacobs W.R. Jr., Geurtsen J., Bornemann S.,
RA Kalscheuer R.;
RT "Metabolic network for the biosynthesis of intra- and extracellular alpha-
RT glucans required for virulence of Mycobacterium tuberculosis.";
RL PLoS Pathog. 12:E1005768-E1005768(2016).
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:0000269|PubMed:27513637}.
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:0000305|PubMed:27513637};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:27513637}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show a discernible
CC effect on alpha-glucan content and do not accumulate ADP-glucose.
CC Combined inactivation of both glgM and glgB completely blocks alpha-
CC glucan production. Combined inactivation of both glgM and ostA
CC accumulates ADP-glucose. In the double mutant treS-glgE, inactivation
CC of the glgM gene fully abolishes maltose 1-phosphate (M1P) production.
CC {ECO:0000269|PubMed:27513637}.
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 the GlgC-GlgM branch provides most of M1P for the
CC GlgE pathway in M.smegmatis. {ECO:0000269|PubMed:27513637}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK70457.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41398.1; -; Genomic_DNA.
DR RefSeq; WP_011730300.1; NZ_SIJM01000019.1.
DR RefSeq; YP_889330.1; NC_008596.1.
DR PDB; 6TVP; X-ray; 1.90 A; A/B=1-387.
DR PDBsum; 6TVP; -.
DR AlphaFoldDB; A0R2E2; -.
DR SMR; A0R2E2; -.
DR STRING; 246196.MSMEI_4954; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; ABK70457; ABK70457; MSMEG_5080.
DR EnsemblBacteria; AFP41398; AFP41398; MSMEI_4954.
DR GeneID; 66736400; -.
DR KEGG; msg:MSMEI_4954; -.
DR KEGG; msm:MSMEG_5080; -.
DR PATRIC; fig|246196.19.peg.4958; -.
DR eggNOG; COG0297; Bacteria.
DR OMA; TREYPPD; -.
DR OrthoDB; 694191at2; -.
DR BRENDA; 2.4.1.342; 3512.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="Alpha-maltose-1-phosphate synthase"
FT /id="PRO_0000438836"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:6TVP"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:6TVP"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6TVP"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 240..256
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:6TVP"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:6TVP"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 333..349
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:6TVP"
FT HELIX 371..386
FT /evidence="ECO:0007829|PDB:6TVP"
SQ SEQUENCE 387 AA; 41679 MW; AD6F94AA26306BA2 CRC64;
MRVAMMTREY PPEVYGGAGV HVTELVAQLR KLCDVDVHCM GAPRDGAYVA HPDPTLRGAN
AALTMLSADL NMVNNAEAAT VVHSHTWYTG LAGHLASLLY GVPHVLTAHS LEPLRPWKAE
QLGGGYQVSS WVERTAVEAA DAVIAVSSGM RDDVLRTYPA LDPDRVHVVR NGIDTTVWYP
AEPGPDESVL AELGVDLNRP IVAFVGRITR QKGVAHLVAA AHRFAPDVQL VLCAGAPDTP
QIAEEVSSAV QQLAQARTGV FWVREMLPTH KIREILSAAT VFVCPSVYEP LGIVNLEAMA
CATAVVASDV GGIPEVVADG RTGLLVHYDA NDTEAYEARL AEAVNSLVAD PDRAREYGVA
GRERCIEEFS WAHIAEQTLE IYRKVSA
