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Protein

Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1

Gene

glgE1

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.1 Publication

Catalytic activityi

Alpha-maltose 1-phosphate + ((1->4)-alpha-D-glucosyl)(n) = phosphate + ((1->4)-alpha-D-glucosyl)(n+2).1 Publication

Enzyme regulationi

Is competitively inhibited by alpha-, beta- and gamma-cyclodextrins (cyclic maltooligosaccharides), unlike GlgE from M.tuberculosis.1 Publication

Kineticsi

  1. KM=1.5 mM for maltohexaose (in the presence of 5 mM M1P)1 Publication
  2. KM=0.30 mM for alpha-maltose 1-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.0 with maltohexaose as acceptor substrate.1 Publication

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius with maltohexaose as acceptor substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei264 – 2641Maltose 1-phosphate1 Publication
    Binding sitei324 – 3241Maltose 1-phosphate1 Publication
    Binding sitei359 – 3591Maltose 1-phosphate1 Publication
    Active sitei394 – 3941Nucleophile1 Publication
    Binding sitei395 – 3951Maltose 1-phosphate1 Publication
    Active sitei423 – 4231Proton donor1 Publication
    Sitei480 – 4801Transition state stabilizer1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 (EC:2.4.99.161 Publication)
    Short name:
    GMPMT 1
    Alternative name(s):
    (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase 1
    Gene namesi
    Name:glgE1
    Synonyms:pep1, pep1A, pep1I
    Ordered Locus Names:SCO5443
    ORF Names:SC6A11.19c
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    Proteomesi
    • UP000001973 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 675675Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1PRO_0000054349Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi100226.SCO5443.

    Structurei

    Secondary structure

    1
    675
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 286Combined sources
    Helixi31 – 333Combined sources
    Beta strandi37 – 404Combined sources
    Beta strandi44 – 518Combined sources
    Beta strandi54 – 563Combined sources
    Beta strandi59 – 668Combined sources
    Beta strandi79 – 824Combined sources
    Beta strandi87 – 937Combined sources
    Beta strandi96 – 10813Combined sources
    Helixi110 – 12415Combined sources
    Helixi128 – 14518Combined sources
    Helixi149 – 16214Combined sources
    Helixi169 – 1746Combined sources
    Helixi179 – 1879Combined sources
    Beta strandi192 – 1965Combined sources
    Beta strandi200 – 2056Combined sources
    Helixi207 – 2104Combined sources
    Beta strandi212 – 2165Combined sources
    Helixi219 – 2213Combined sources
    Helixi232 – 2354Combined sources
    Helixi236 – 2383Combined sources
    Helixi239 – 2446Combined sources
    Beta strandi249 – 2524Combined sources
    Helixi266 – 2683Combined sources
    Beta strandi269 – 2713Combined sources
    Turni295 – 2973Combined sources
    Helixi300 – 31213Combined sources
    Beta strandi316 – 3216Combined sources
    Helixi331 – 3344Combined sources
    Helixi336 – 3383Combined sources
    Beta strandi350 – 3523Combined sources
    Beta strandi355 – 3573Combined sources
    Helixi369 – 38517Combined sources
    Beta strandi390 – 3956Combined sources
    Helixi396 – 3983Combined sources
    Helixi401 – 41414Combined sources
    Beta strandi419 – 4224Combined sources
    Helixi428 – 4369Combined sources
    Beta strandi440 – 4434Combined sources
    Helixi446 – 4483Combined sources
    Helixi452 – 46211Combined sources
    Helixi465 – 4684Combined sources
    Beta strandi472 – 4765Combined sources
    Helixi484 – 4896Combined sources
    Helixi491 – 50414Combined sources
    Beta strandi506 – 5116Combined sources
    Helixi514 – 5163Combined sources
    Beta strandi521 – 5233Combined sources
    Turni533 – 5353Combined sources
    Helixi542 – 5487Combined sources
    Helixi553 – 56513Combined sources
    Helixi567 – 5704Combined sources
    Beta strandi576 – 5783Combined sources
    Beta strandi580 – 5823Combined sources
    Beta strandi585 – 5928Combined sources
    Beta strandi595 – 6028Combined sources
    Beta strandi605 – 6073Combined sources
    Beta strandi609 – 6146Combined sources
    Helixi617 – 6204Combined sources
    Beta strandi627 – 6326Combined sources
    Turni633 – 6353Combined sources
    Beta strandi638 – 64912Combined sources
    Turni651 – 6533Combined sources
    Beta strandi655 – 6617Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZSSX-ray1.80A/B/C/D1-675[»]
    3ZSTX-ray2.30A/B1-675[»]
    3ZT5X-ray2.09A/B/C/D1-675[»]
    3ZT6X-ray2.19A/B/C/D1-675[»]
    3ZT7X-ray2.50A/B/C/D1-675[»]
    4CN1X-ray2.55A/B1-675[»]
    4CN4X-ray2.40A/B1-675[»]
    4CN6X-ray2.29A/B1-675[»]
    4U2YX-ray2.48A/B1-675[»]
    4U2ZX-ray2.26A/B1-675[»]
    4U31X-ray1.85A/B1-675[»]
    ProteinModelPortaliQ9L1K2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9L1K2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni534 – 5352Maltose 1-phosphate binding1 Publication

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family. GlgE subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105EP6. Bacteria.
    COG0366. LUCA.
    HOGENOMiHOG000239230.
    InParanoidiQ9L1K2.
    KOiK16147.
    OMAiRDLHFHH.
    OrthoDBiEOG6S52J5.
    PhylomeDBiQ9L1K2.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    HAMAPiMF_02124. GlgE.
    InterProiIPR026585. GlgE.
    IPR021828. GlgE_dom_N/S.
    IPR015902. Glyco_hydro_13.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR013780. Glyco_hydro_b.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 2 hits.
    PfamiPF11896. DUF3416. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9L1K2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPATHHSSAT SAERPTVVGR IPVLDVRPVV QRGRRPAKAV TGESFEVSAT
    60 70 80 90 100
    VFREGHDAVG ANVVLRDPRG RPGPWTPMRE LAPGTDRWGA TVTAGETGTW
    110 120 130 140 150
    SYTVEAWGDP VTTWRHHARI KIPAGLDTDL VLEEGARLYE RAAADVPGRE
    160 170 180 190 200
    DRRELLAAVD ALRDESRPAA SRLAAALTPQ VDAVLARHPL RDLVTSSDPL
    210 220 230 240 250
    PLLVERERAL YGAWYEFFPR SEGTPHTPHG TFRTAARRLP AIAAMGFDVV
    260 270 280 290 300
    YLPPIHPIGT THRKGRNNTL SATGDDVGVP WAIGSPEGGH DSIHPALGTL
    310 320 330 340 350
    DDFDHFVTEA GKLGLEIALD FALQCSPDHP WVHKHPEWFH HRPDGTIAHA
    360 370 380 390 400
    ENPPKKYQDI YPIAFDADPD GLATETVRIL RHWMDHGVRI FRVDNPHTKP
    410 420 430 440 450
    VAFWERVIAD INGTDPDVIF LAEAFTRPAM MATLAQIGFQ QSYTYFTWRN
    460 470 480 490 500
    TKQELTEYLT ELSGEAASYM RPNFFANTPD ILHAYLQHGG RPAFEVRAVL
    510 520 530 540 550
    AATLSPTWGI YSGYELCENT PLREGSEEYL DSEKYQLKPR DWTRAAREGT
    560 570 580 590 600
    TIAPLVTRLN TIRRENPALR QLRDLHFHPT DKEEVIAYSK RQGSNTVLVV
    610 620 630 640 650
    VNLDPRHTQE ATVSLDMPQL GLDWHESVPV RDELTGETYH WGRANYVRLE
    660 670
    PGRTPAHVCT VLRPSHPQIG GSHTT
    Length:675
    Mass (Da):75,290
    Last modified:October 1, 2000 - v1
    Checksum:iC23DBCFF23AD42D6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti218 – 2181F → W in CAA04600 (PubMed:10821190).Curated
    Sequence conflicti450 – 4512NT → LR in CAA04600 (PubMed:10821190).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ001205 Genomic DNA. Translation: CAA04600.1.
    AL939123 Genomic DNA. Translation: CAB72419.1.
    RefSeqiNP_629581.1. NC_003888.3.
    WP_011030248.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAB72419; CAB72419; CAB72419.
    GeneIDi1100883.
    KEGGisco:SCO5443.
    PATRICi23740736. VBIStrCoe124346_5524.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ001205 Genomic DNA. Translation: CAA04600.1.
    AL939123 Genomic DNA. Translation: CAB72419.1.
    RefSeqiNP_629581.1. NC_003888.3.
    WP_011030248.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZSSX-ray1.80A/B/C/D1-675[»]
    3ZSTX-ray2.30A/B1-675[»]
    3ZT5X-ray2.09A/B/C/D1-675[»]
    3ZT6X-ray2.19A/B/C/D1-675[»]
    3ZT7X-ray2.50A/B/C/D1-675[»]
    4CN1X-ray2.55A/B1-675[»]
    4CN4X-ray2.40A/B1-675[»]
    4CN6X-ray2.29A/B1-675[»]
    4U2YX-ray2.48A/B1-675[»]
    4U2ZX-ray2.26A/B1-675[»]
    4U31X-ray1.85A/B1-675[»]
    ProteinModelPortaliQ9L1K2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO5443.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB72419; CAB72419; CAB72419.
    GeneIDi1100883.
    KEGGisco:SCO5443.
    PATRICi23740736. VBIStrCoe124346_5524.

    Phylogenomic databases

    eggNOGiENOG4105EP6. Bacteria.
    COG0366. LUCA.
    HOGENOMiHOG000239230.
    InParanoidiQ9L1K2.
    KOiK16147.
    OMAiRDLHFHH.
    OrthoDBiEOG6S52J5.
    PhylomeDBiQ9L1K2.

    Miscellaneous databases

    EvolutionaryTraceiQ9L1K2.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    HAMAPiMF_02124. GlgE.
    InterProiIPR026585. GlgE.
    IPR021828. GlgE_dom_N/S.
    IPR015902. Glyco_hydro_13.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR013780. Glyco_hydro_b.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 2 hits.
    PfamiPF11896. DUF3416. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Duplicated gene clusters suggest an interplay of glycogen and trehalose metabolism during sequential stages of aerial mycelium development in Streptomyces coelicolor A3(2)."
      Schneider D., Bruton C.J., Chater K.F.
      Mol. Gen. Genet. 263:543-553(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A3(2) / NRRL B-16638.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-471 / A3(2) / M145.
    3. "Structure of a Streptomyces maltosyltransferase GlgE: a homologue of a genetically validated anti-tuberculosis target."
      Syson K., Stevenson C.E., Rejzek M., Fairhurst S.A., Nair A., Bruton C.J., Field R.A., Chater K.F., Lawson D.M., Bornemann S.
      J. Biol. Chem. 286:38298-38310(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APOENZYME AND COMPLEXES WITH MALTOSE AND ALPHA- OR BETA-CYCLODEXTRIN, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC BAA-471 / A3(2) / M145.

    Entry informationi

    Entry nameiGLGE1_STRCO
    AccessioniPrimary (citable) accession number: Q9L1K2
    Secondary accession number(s): O54202
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 3, 2003
    Last sequence update: October 1, 2000
    Last modified: July 6, 2016
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.