GLGE1_STRCO
ID GLGE1_STRCO Reviewed; 675 AA.
AC Q9L1K2; O54202;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1;
DE Short=GMPMT 1;
DE EC=2.4.99.16 {ECO:0000269|PubMed:21914799};
DE AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase 1;
GN Name=glgE1; Synonyms=pep1, pep1A, pep1I; OrderedLocusNames=SCO5443;
GN ORFNames=SC6A11.19c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=10821190; DOI=10.1007/s004380051200;
RA Schneider D., Bruton C.J., Chater K.F.;
RT "Duplicated gene clusters suggest an interplay of glycogen and trehalose
RT metabolism during sequential stages of aerial mycelium development in
RT Streptomyces coelicolor A3(2).";
RL Mol. Gen. Genet. 263:543-553(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APOENZYME AND COMPLEXES WITH
RP MALTOSE AND ALPHA- OR BETA-CYCLODEXTRIN, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
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.
CC Maltooligosaccharides with a degree of polymerization (DP) superior or
CC equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-
CC catalyzed polymerization with M1P. Is specific for the alpha-anomer of
CC M1P as substrate, since the beta-anomer of M1P gives no activity.
CC Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but
CC alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an
CC alpha-retaining catalytic mechanism, with evidence that
CC maltooligosaccharide acceptors are extended at their non-reducing ends.
CC Is also able to catalyze the reverse reaction in vitro, releasing M1P
CC from glycogen or maltoheptaose in the presence of inorganic phosphate.
CC Also catalyzes disproportionation reactions through maltosyl transfer
CC between maltooligosaccharides. Is probably involved in a branched
CC alpha-glucan biosynthetic pathway from trehalose, together with TreS,
CC Mak and GlgB. {ECO:0000269|PubMed:21914799}.
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:21914799};
CC -!- ACTIVITY REGULATION: Is competitively inhibited by alpha-, beta- and
CC gamma-cyclodextrins (cyclic maltooligosaccharides), unlike GlgE from
CC M.tuberculosis. {ECO:0000269|PubMed:21914799}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for maltohexaose (in the presence of 5 mM M1P)
CC {ECO:0000269|PubMed:21914799};
CC KM=0.30 mM for alpha-maltose 1-phosphate
CC {ECO:0000269|PubMed:21914799};
CC pH dependence:
CC Optimum pH is 7.0 with maltohexaose as acceptor substrate.
CC {ECO:0000269|PubMed:21914799};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius with maltohexaose as
CC acceptor substrate. {ECO:0000269|PubMed:21914799};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21914799}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02124}.
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; AJ001205; CAA04600.1; -; Genomic_DNA.
DR EMBL; AL939123; CAB72419.1; -; Genomic_DNA.
DR RefSeq; NP_629581.1; NC_003888.3.
DR RefSeq; WP_011030248.1; NZ_VNID01000011.1.
DR PDB; 3ZSS; X-ray; 1.80 A; A/B/C/D=1-675.
DR PDB; 3ZST; X-ray; 2.30 A; A/B=1-675.
DR PDB; 3ZT5; X-ray; 2.09 A; A/B/C/D=1-675.
DR PDB; 3ZT6; X-ray; 2.19 A; A/B/C/D=1-675.
DR PDB; 3ZT7; X-ray; 2.50 A; A/B/C/D=1-675.
DR PDB; 4CN1; X-ray; 2.55 A; A/B=1-675.
DR PDB; 4CN4; X-ray; 2.40 A; A/B=1-675.
DR PDB; 4CN6; X-ray; 2.29 A; A/B=1-675.
DR PDB; 4U2Y; X-ray; 2.48 A; A/B=1-675.
DR PDB; 4U2Z; X-ray; 2.26 A; A/B=1-675.
DR PDB; 4U31; X-ray; 1.85 A; A/B=1-675.
DR PDB; 5CVS; X-ray; 2.30 A; A/B=1-675.
DR PDB; 5LGV; X-ray; 2.50 A; A/B=1-675.
DR PDB; 5LGW; X-ray; 1.95 A; A/B=1-675.
DR PDB; 5VSJ; X-ray; 2.46 A; A/B=1-663.
DR PDB; 5VT4; X-ray; 3.21 A; A/B/C/D=1-663.
DR PDB; 7MEL; X-ray; 1.75 A; A/B=1-675.
DR PDB; 7MGY; X-ray; 1.83 A; A/B=1-675.
DR PDBsum; 3ZSS; -.
DR PDBsum; 3ZST; -.
DR PDBsum; 3ZT5; -.
DR PDBsum; 3ZT6; -.
DR PDBsum; 3ZT7; -.
DR PDBsum; 4CN1; -.
DR PDBsum; 4CN4; -.
DR PDBsum; 4CN6; -.
DR PDBsum; 4U2Y; -.
DR PDBsum; 4U2Z; -.
DR PDBsum; 4U31; -.
DR PDBsum; 5CVS; -.
DR PDBsum; 5LGV; -.
DR PDBsum; 5LGW; -.
DR PDBsum; 5VSJ; -.
DR PDBsum; 5VT4; -.
DR PDBsum; 7MEL; -.
DR PDBsum; 7MGY; -.
DR AlphaFoldDB; Q9L1K2; -.
DR SMR; Q9L1K2; -.
DR STRING; 100226.SCO5443; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 1100883; -.
DR KEGG; sco:SCO5443; -.
DR PATRIC; fig|100226.15.peg.5524; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_015798_0_0_11; -.
DR InParanoid; Q9L1K2; -.
DR OMA; RPNFWPN; -.
DR PhylomeDB; Q9L1K2; -.
DR BRENDA; 2.4.99.16; 5998.
DR EvolutionaryTrace; Q9L1K2; -.
DR Proteomes; UP000001973; 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 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; PF11896; DUF3416; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..675
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase 1"
FT /id="PRO_0000054349"
FT ACT_SITE 394
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:21914799"
FT ACT_SITE 423
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:21914799"
FT BINDING 264
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000305|PubMed:21914799"
FT BINDING 324
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000305|PubMed:21914799"
FT BINDING 359
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000305|PubMed:21914799"
FT BINDING 395
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000305|PubMed:21914799"
FT BINDING 534..535
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000305|PubMed:21914799"
FT SITE 480
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:21914799"
FT CONFLICT 218
FT /note="F -> W (in Ref. 1; CAA04600)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..451
FT /note="NT -> LR (in Ref. 1; CAA04600)"
FT /evidence="ECO:0000305"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:7MEL"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4U31"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 300..312
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5VT4"
FT HELIX 369..385
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 428..436
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 452..463
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 484..504
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:7MEL"
FT TURN 512..517
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:7MEL"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:4U2Y"
FT HELIX 542..547
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 553..565
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:5LGW"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 595..602
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:7MEL"
FT HELIX 617..620
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:7MEL"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 643..649
FT /evidence="ECO:0007829|PDB:7MEL"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:7MEL"
FT STRAND 655..661
FT /evidence="ECO:0007829|PDB:7MEL"
SQ SEQUENCE 675 AA; 75290 MW; C23DBCFF23AD42D6 CRC64;
MPATHHSSAT SAERPTVVGR IPVLDVRPVV QRGRRPAKAV TGESFEVSAT VFREGHDAVG
ANVVLRDPRG RPGPWTPMRE LAPGTDRWGA TVTAGETGTW SYTVEAWGDP VTTWRHHARI
KIPAGLDTDL VLEEGARLYE RAAADVPGRE DRRELLAAVD ALRDESRPAA SRLAAALTPQ
VDAVLARHPL RDLVTSSDPL PLLVERERAL YGAWYEFFPR SEGTPHTPHG TFRTAARRLP
AIAAMGFDVV YLPPIHPIGT THRKGRNNTL SATGDDVGVP WAIGSPEGGH DSIHPALGTL
DDFDHFVTEA GKLGLEIALD FALQCSPDHP WVHKHPEWFH HRPDGTIAHA ENPPKKYQDI
YPIAFDADPD GLATETVRIL RHWMDHGVRI FRVDNPHTKP VAFWERVIAD INGTDPDVIF
LAEAFTRPAM MATLAQIGFQ QSYTYFTWRN TKQELTEYLT ELSGEAASYM RPNFFANTPD
ILHAYLQHGG RPAFEVRAVL AATLSPTWGI YSGYELCENT PLREGSEEYL DSEKYQLKPR
DWTRAAREGT TIAPLVTRLN TIRRENPALR QLRDLHFHPT DKEEVIAYSK RQGSNTVLVV
VNLDPRHTQE ATVSLDMPQL GLDWHESVPV RDELTGETYH WGRANYVRLE PGRTPAHVCT
VLRPSHPQIG GSHTT
