GLGE_BURPS
ID GLGE_BURPS Reviewed; 1136 AA.
AC Q63T93;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=BPSL2074;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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 (By similarity).
CC {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 13 family. GlgE subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH36075.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX571965; CAH36075.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_108673.1; NC_006350.1.
DR AlphaFoldDB; Q63T93; -.
DR SMR; Q63T93; -.
DR STRING; 272560.BPSL2074; -.
DR PRIDE; Q63T93; -.
DR EnsemblBacteria; CAH36075; CAH36075; BPSL2074.
DR KEGG; bps:BPSL2074; -.
DR PATRIC; fig|272560.6.peg.2349; -.
DR eggNOG; COG0366; Bacteria.
DR Proteomes; UP000000605; Chromosome 1.
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 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; 2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11896; DUF3416; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..1136
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000413893"
FT REGION 1..439
FT /note="Unknown"
FT REGION 440..1136
FT /note="Maltosyltransferase"
FT ACT_SITE 842
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 871
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 710
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 770
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 805
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 843
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 982..983
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT SITE 929
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1136 AA; 125438 MW; A4D161F433027D1F CRC64;
METRPSFAPN LYFCDARLVG PLHAWPPLFE RVAAWGFDHV LIGGLWAASR RGYPRHVADP
DRPAESFATS LDATSALARL SDSAREHGLR IAVEVVVDRV AREHPLHDAH RAWYVVDERD
DALIDPRTAA LAHDVAHANV GSAAALDALA DWWRARLGAL ADAGAAAFLV DAPQRMPAHW
WAALLRALRQ ARADLPVIAG VPGREREALA QLACAGFDAA FSSLRWWDLR APWFVEEHRL
LRRVGAPIAF PDAFDGPRLA HDWRQAAPET IERAHRRALW TAAALGTGWL VPMGFERGVA
VELMAREPRA DAYRAALDSA PFDLSGAIAE ANALRRATPA LRGNGEIAQL TGADAPATVL
LRGARTALEY DDEAALIAVN PDLAHPAAIA PCAALAGVPG GFTRFAPFAD GRRPRMGALE
PFALAAGACT LLRAQRARPV TTAPAEDRRG NRPGTRASVT AALAGERIAI ERIEPVVDDG
RFAVKRVIGE RLAVRAAIFA DGHARLAAAV QWRAADENGW HEARCAAEGN DAWRADIPLE
RLGRHLFRVI AWRDDWATLV DEIGKKHAAG QAVALELEEA RRLAADVLTR APEANPAALA
VLREFAAALD AAPPDQRLAL IGAPHVADAF AALRERAFAT RDAPVFPVDV ERRAARFASW
YEMFPRSASD DVRRHGTFDD VVAHLPRIRD MGFDVLYFPP IHPIGTTARK GRNNSLQAAP
DDVGSPYAIG SPAGGHTAVH PQLGSLDAFR RLVAAARAHD LEIALDFAVQ CSPDHPWLTE
HPGWFAWRPD GSLRYAENPP KRYQDIVNPD FYARDAMPAL WIALRDVVLF WIDAGVRIFR
VDNPHTKPLP FWAWMIADVR ARHPDTVFLS EAFTRPSMMY RLAKLGFSQS YTYFTWRESK
REFIDYLTEL ADGPAREYFR PNFFVNTPDI NPRHLQQAPR TQFVIRAALA ATLSGLWGMY
SGFELCESDA LPDSEEYRDA EKYELRARDW RRPGHIGDEI ARLNRARRDN PALQTHLGIR
FAHAPNDAVL VFSKATPAHD NVVVVAISLD PWHPQATDFT LDAALYRGWG IADGERLVAV
DQTADHVETW HGRRHYVALD PHVRPFAIWR VAPAAGVARG ARDDARDVPA QEVHER
