GLGE_MYCS2
ID GLGE_MYCS2 Reviewed; 697 AA.
AC Q9RP48; A0R1Y3; I7G6B6;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase;
DE Short=GMPMT;
DE EC=2.4.99.16;
DE AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase;
GN Name=glgE; OrderedLocusNames=MSMEG_4916, MSMEI_4789;
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 [GENOMIC DNA], AND MUTAGENESIS OF HIS-349.
RX PubMed=10542168; DOI=10.1128/jb.181.21.6670-6678.1999;
RA Belanger A.E., Hatfull G.F.;
RT "Exponential-phase glycogen recycling is essential for growth of
RT Mycobacterium smegmatis.";
RL J. Bacteriol. 181:6670-6678(1999).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP KINETIC PARAMETERS, AND PATHWAY.
RC STRAIN=ATCC 14468 / DSM 43277 / NCIB 9953 / NCTC 10265 / W-113;
RX PubMed=20118231; DOI=10.1074/jbc.m109.033944;
RA Elbein A.D., Pastuszak I., Tackett A.J., Wilson T., Pan Y.T.;
RT "Last step in the conversion of trehalose to glycogen: a mycobacterial
RT enzyme that transfers maltose from maltose 1-phosphate to glycogen.";
RL J. Biol. Chem. 285:9803-9812(2010).
RN [6]
RP DISRUPTION PHENOTYPE, AND DISCUSSION OF MUTANT TYR-349 PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
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 [7]
RP SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=21914799; DOI=10.1074/jbc.m111.279315;
RA Syson K., Stevenson C.E., Rejzek M., Fairhurst S.A., Nair A., Bruton C.J.,
RA Field R.A., Chater K.F., Lawson D.M., Bornemann S.;
RT "Structure of a Streptomyces maltosyltransferase GlgE: a homologue of a
RT genetically validated anti-tuberculosis target.";
RL J. Biol. Chem. 286:38298-38310(2011).
CC -!- FUNCTION: Maltosyltransferase that uses maltose 1-phosphate (M1P) as
CC the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is
CC also able to catalyze the reverse reaction in vitro. Cannot use glucose
CC 1-phosphate as substrate. Is involved in a branched alpha-glucan
CC biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
CC {ECO:0000269|PubMed:20118231}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate =
CC [(1->4)-alpha-D-glucosyl](n+2) + phosphate; Xref=Rhea:RHEA:42692,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:10183, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:63576; EC=2.4.99.16;
CC Evidence={ECO:0000269|PubMed:20118231};
CC -!- ACTIVITY REGULATION: The transfer reaction from maltose-1-P to glycogen
CC is inhibited by micromolar amounts of inorganic phosphate or arsenate
CC but is only slightly inhibited by millimolar concentrations of glucose-
CC 1-P, glucose-6-P, or inorganic pyrophosphate. Is also inhibited by ATP,
CC by 1,4-dideoxy-1,4-imino-D-arabinitol (DIA), but not by isofagomine.
CC {ECO:0000269|PubMed:20118231}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=250 uM for maltose 1-phosphate {ECO:0000269|PubMed:20118231};
CC Vmax=25.2 nmol/min/mg enzyme {ECO:0000269|PubMed:20118231};
CC Note=The data are not very reliable because measures were done with a
CC partially purified enzyme.;
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:20118231}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21914799}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display M1P accumulation
CC and trehalose sensitivity. These phenotypes are suppressed in mutants
CC lacking both glgE and treS or both glgE and mak. Deletion of glgE does
CC not increase glycogen content. {ECO:0000269|PubMed:20305657}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK71468.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF172946; AAF07898.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK71468.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP41237.1; -; Genomic_DNA.
DR RefSeq; YP_889171.1; NC_008596.1.
DR AlphaFoldDB; Q9RP48; -.
DR SMR; Q9RP48; -.
DR STRING; 246196.MSMEI_4789; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABK71468; ABK71468; MSMEG_4916.
DR EnsemblBacteria; AFP41237; AFP41237; MSMEI_4789.
DR KEGG; msg:MSMEI_4789; -.
DR KEGG; msm:MSMEG_4916; -.
DR PATRIC; fig|246196.19.peg.4797; -.
DR eggNOG; COG0366; Bacteria.
DR BRENDA; 2.4.99.16; 3512.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_02124; GlgE; 1.
DR InterPro; IPR026585; GlgE.
DR InterPro; IPR021828; GlgE_dom_N/S.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR10357:SF203; PTHR10357:SF203; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11896; DUF3416; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..697
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000054346"
FT REGION 286..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 443
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 553..554
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT SITE 499
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MUTAGEN 349
FT /note="H->Y: In SMEG53; results in a temperature-dependent
FT accumulation of M1P during exponential growth."
FT /evidence="ECO:0000269|PubMed:10542168"
SQ SEQUENCE 697 AA; 78043 MW; E1B92754318A1E55 CRC64;
MRSGWVAGRI GIDDVAPVVS CGRYPAKAVV GEVVPVRATV WREGHDAVSA TLVVRYLGTE
FPRLASGPGT TPPAVPLGTV VQPGKRVKPQ ILQMSKGRTP DVFHGEFTPD AVGLWTFRVD
GWGDPIATWR HAVEAKLEAG QSETELNNDL LVGARLLMRA AEGVPRKLRD PLLEAAQQLR
TPGDPYQRAG GALSPEVADL LLQYPLREFV TRGEVHGVWV DRPLARFSSW YEMFPRSTGG
WDENGHPVHG TFATAAAALP RIARMGFNVV YLPPIHPIGK VHRKGRNNSV TAAPGDVGSP
WAIGSDEGGH DAVHPDLGTI DDFDAFVAAA RDAGLEVALD LALQCAPDHP WAKEHPEWFT
VLPDGTIAYA ENPPKKYQDI YPLNFDNDPD GLFHEVLRVV KFWISHGVKV FRVDNPHTKP
PNFWAWLIAE VKNEDPDILF LSEAFTRPAR LYGLAKLGFT QSYTYFTWRT AKWELTEFGE
EIAKYADHAR PNLWVNTPDI LHESLQHGGP GMFAIRAVLA STMSSSWGVY SGYELFEHRS
VREGSEEYLD SEKYELRPRD FDGALARGES LEPFLTRLNE IRRLHPALRQ LRTIKFHHLD
NDALLAYSKF DPVTGDTVLV VVTLNPFGPE ESTLWLDMEA LGMEPYDRFW VRDEITGEEY
QWGQSNYVRI EPAKAVAHVL NMPLIPYEKR LDLLRRE
