ID A1UJW8_MYCSK Unreviewed; 695 AA.
AC A1UJW8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
DE Short=GMPMT {ECO:0000256|HAMAP-Rule:MF_02124};
DE EC=2.4.99.16 {ECO:0000256|HAMAP-Rule:MF_02124};
DE AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
GN Name=glgE {ECO:0000256|HAMAP-Rule:MF_02124};
GN OrderedLocusNames=Mkms_3934 {ECO:0000313|EMBL:ABL93126.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL93126.1};
RN [1] {ECO:0000313|EMBL:ABL93126.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL93126.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 involved in a branched alpha-glucan biosynthetic pathway from
CC trehalose, together with TreS, Mak and GlgB. {ECO:0000256|HAMAP-
CC Rule:MF_02124}.
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:0000256|ARBA:ARBA00000575, ECO:0000256|HAMAP-
CC Rule:MF_02124};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02124}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_02124}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02124}.
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DR EMBL; CP000518; ABL93126.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UJW8; -.
DR STRING; 189918.Mkms_3934; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; mkm:Mkms_3934; -.
DR HOGENOM; CLU_015798_0_0_11; -.
DR OrthoDB; 9805159at2; -.
DR UniPathway; UPA00164; -.
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-UniRule.
DR CDD; cd11344; AmyAc_GlgE_like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR HAMAP; MF_02124; GlgE; 1.
DR InterPro; IPR026585; GlgE.
DR InterPro; IPR049171; GLGE_C.
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; PTHR47786:SF2; AAMY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47786; ALPHA-1,4-GLUCAN:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF21702; GLGE_C; 1.
DR Pfam; PF11896; GlgE_dom_N_S; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_02124}; Glycogen biosynthesis {ECO:0000256|HAMAP-Rule:MF_02124};
KW Glycogen metabolism {ECO:0000256|HAMAP-Rule:MF_02124};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_02124};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02124}.
FT DOMAIN 226..580
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 441
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 282
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 342
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 377
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 413
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 551..552
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 497
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 695 AA; 77687 MW; F341F99D38C3B152 CRC64;
MAGRIGIDDV APVVSGGRYP AKAVVGEVVP VSATVWREGH EAVSATLVVR YHGTSYPELA
DAPVGRVSTT EAVPIDEVVS PSPRKKPQAL PMSLGRTPDV FHGHFVPDAV GLWTYRVDGW
GDPIASWRHN VIAKLDAGQS ESELDNDLLV GARLLERAAT GVPRQDRYPL AQAVERLREP
GDPFYRAGAA LAADVTALLD QYPLRELVTR GEQYGVWVDR PLARFGSWYE FFPRSTGGWD
SQGHPVHGTF ATATKALPRV ARMGFDVVYL PPIHPIGKVH RKGPNNSVTA GPNDVGSPWA
IGSDEGGHDA VHPELGTIED FDDFVAAARD EGLEVALDLA LQCAPDHPWA REHPEWFTVL
PDGTIAYAEN PPKKYQDIYP LNFDNDPTGL YMEVLRVVRF WISHGVKVFR VDNPHTKPPN
FWAWLIGEIK NEDPDVLFLA EAFTRPARLY GLAKLGYTQS YTYFTWRTSK HELTEFGRQI
AEHADYARPN LFVNTPDILH ESLQHGGPGM FAIRAVLAST MSSVWGVYSG YELFEHRPVR
EGSEEYLNSE KYELRPRDFD AALADGESLE PFITRLNEIR RVHPALHELR TITFHYPDND
AVLAYSKFDP ATGDQVLVVV TLNPFGPEEA TVWLDMPALG MEPYDRFWVR DEITGEEYQW
GQSNYVRIEP AKAVAHVLNM PQVPADQRLN LLRRE
//
