GLGE_MYCTO
ID GLGE_MYCTO Reviewed; 701 AA.
AC P9WQ16; L0T7Y4; P63531; Q10638;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
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;
DE AltName: Full=(1->4)-alpha-D-glucan:phosphate alpha-D-maltosyltransferase;
GN Name=glgE; OrderedLocusNames=MT1369;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Essential maltosyltransferase that uses maltose 1-phosphate
CC (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-
CC glucans. Maltooligosaccharides with a degree of polymerization (DP)
CC superior or equal to 4 are efficient acceptors, with DP5 being optimal
CC in the GlgE-catalyzed polymerization with M1P. Is specific for the
CC alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no
CC activity. Exhibits an alpha-retaining catalytic mechanism. Is also able
CC to catalyze the reverse reaction in vitro, releasing M1P from glycogen
CC in the presence of inorganic phosphate. Also catalyzes
CC disproportionation reactions through maltosyl transfer between
CC maltooligosaccharides. Is involved in a branched alpha-glucan
CC biosynthetic pathway from trehalose, together with TreS, Mak and GlgB
CC (By similarity). {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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK45633.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK45633.1; ALT_INIT; Genomic_DNA.
DR PIR; C70770; C70770.
DR RefSeq; WP_003406897.1; NZ_KK341227.1.
DR PDB; 4U33; X-ray; 3.29 A; A/B/C/D/E/F=1-701.
DR PDB; 4U3C; X-ray; 3.98 A; A/B/C/D/E/F=1-701.
DR PDBsum; 4U33; -.
DR PDBsum; 4U3C; -.
DR AlphaFoldDB; P9WQ16; -.
DR SMR; P9WQ16; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAK45633; AAK45633; MT1369.
DR KEGG; mtc:MT1369; -.
DR PATRIC; fig|83331.31.peg.1476; -.
DR HOGENOM; CLU_015798_0_0_11; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001020; 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycogen biosynthesis;
KW Glycogen metabolism; Glycosyltransferase; Transferase.
FT CHAIN 1..701
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000426854"
FT REGION 286..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 447
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT BINDING 557..558
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000250"
FT SITE 503
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:4U33"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 212..225
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4U33"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4U33"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:4U33"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 476..486
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 507..511
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 513..527
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:4U33"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 576..588
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 590..593
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 599..604
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:4U33"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 621..628
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 634..639
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 642..645
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:4U33"
FT TURN 658..660
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 663..666
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:4U33"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:4U33"
FT STRAND 680..685
FT /evidence="ECO:0007829|PDB:4U33"
FT HELIX 694..697
FT /evidence="ECO:0007829|PDB:4U33"
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
