GLGE_MYCBO
ID GLGE_MYCBO Reviewed; 701 AA.
AC P63532; A0A1R3XY21; Q10638; X2BHK7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase {ECO:0000255|HAMAP-Rule:MF_02124};
DE Short=GMPMT {ECO:0000255|HAMAP-Rule:MF_02124};
DE EC=2.4.99.16 {ECO:0000255|HAMAP-Rule:MF_02124};
DE AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase {ECO:0000255|HAMAP-Rule:MF_02124};
GN Name=glgE {ECO:0000255|HAMAP-Rule:MF_02124};
GN OrderedLocusNames=BQ2027_MB1362C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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:0000255|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:0000255|HAMAP-Rule:MF_02124};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02124}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02124}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02124}.
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DR EMBL; LT708304; SIT99965.1; -; Genomic_DNA.
DR RefSeq; NP_855016.1; NC_002945.3.
DR RefSeq; WP_003406897.1; NC_002945.4.
DR AlphaFoldDB; P63532; -.
DR SMR; P63532; -.
DR EnsemblBacteria; SIT99965; SIT99965; BQ2027_MB1362C.
DR PATRIC; fig|233413.5.peg.1494; -.
DR OMA; RPNFWPN; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001419; 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-UniRule.
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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11896; DUF3416; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..701
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000054348"
FT REGION 286..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT ACT_SITE 447
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 288
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 348
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 383
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 419
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 557..558
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT SITE 503
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
SQ SEQUENCE 701 AA; 78640 MW; EE637BA1DA7D694F CRC64;
MSGRAIGTET EWWVPGRVEI DDVAPVVSCG VYPAKAVVGE VVPVSAAVWR EGHEAVAATL
VVRYLGVRYP HLTDRPRARV LPTPSEPQQR VKPLLIPMTS GQEPFVFHGQ FTPDRVGLWT
FRVDGWGDPI HTWRHGLIAK LDAGQGETEL SNDLLVGAVL LERAATGVPR GLRDPLLAAA
AALRTPGDPV TRTALALTPE IEELLADYPL RDLVTRGEQF GVWVDRPLAR FGAWYEMFPR
STGGWDDDGN PVHGTFATAA AELPRIAGMG FDVVYLPPIH PIGKVHRKGR NNSPTAAPTD
VGSPWAIGSD EGGHDTVHPS LGTIDDFDDF VSAARDLGME VALDLALQCA PDHPWAREHR
QWFTELPDGT IAYAENPPKK YQDIYPLNFD NDPEGLYDEV LRVVQHWVNH GVKFFRVDNP
HTKPPNFWAW LIAQVKTVDP DVLFLSEAFT PPARQYGLAK LGFTQSYSYF TWRTTKWELT
EFGNQIAELA DYRRPNLFVN TPDILHAVLQ HNGPGMFAIR AVLAATMSPA WGMYCGYELF
EHRAVREGSE EYLDSEKYEL RPRDFASALD QGRSLQPFIT RLNIIRRLHP AFQQLRTIHF
HHVDNDALLA YSKFDPATGD CVLVVVTLNA FGPEEATLWL DMAALGMEDY DRFWVRDEIT
GEEYQWGQAN YIRIDPARAV AHIINMPAVP YESRNTLLRR R
