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O33830

- AGLA_THEMA

UniProt

O33830 - AGLA_THEMA

Protein

Alpha-glucosidase

Gene

aglA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Alpha-glycosidase with a very broad specificity. Hydrolyzes maltose and other small maltooligosaccharides but is inactive against the polymeric substrate starch. AglA is not specific with respect to the configuration at the C-4 position of its substrates because glycosidic derivatives of D-galactose are also hydrolyzed. Does not cleave beta-glycosidic bonds.

    Catalytic activityi

    Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

    Cofactori

    Binds 1 NAD per subunit.1 Publication
    Binds 1 manganese ion per subunit. Can also use cobalt and nickel ions, albeit less efficiently than manganese ion.1 Publication

    Enzyme regulationi

    Inhibited by Hg2+ ion and EDTA.

    Kineticsi

    1. KM=0.23 mM for p-nitrophenyl-alpha-D-glucopyranoside2 Publications
    2. KM=0.53 mM for p-nitrophenyl-alpha-D-galactopyranoside2 Publications

    Vmax=9.94 µmol/min/mg enzyme with p-nitrophenyl-alpha-D-glucopyranoside as substrate2 Publications

    Vmax=11.42 µmol/min/mg enzyme with p-nitrophenyl-alpha-D-galactopyranoside as substrate2 Publications

    pH dependencei

    Optimum pH is 7.5. Active from pH 6.5 to 9.1 Publication

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius. Active from 60 to 105 degrees Celsius. Highly thermostable.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei119 – 1191Substrate
    Binding sitei153 – 1531Substrate
    Metal bindingi174 – 1741ManganeseBy similarity
    Active sitei175 – 1751Proton donorCurated
    Metal bindingi203 – 2031ManganeseBy similarity
    Active sitei260 – 2601Proton acceptorCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 7067NADAdd
    BLAST

    GO - Molecular functioni

    1. maltose alpha-glucosidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Cobalt, Manganese, Metal-binding, NAD, Nickel

    Enzyme and pathway databases

    BioCyciTMAR243274:GC6P-1885-MONOMER.
    BRENDAi3.2.1.20. 6331.

    Protein family/group databases

    CAZyiGH4. Glycoside Hydrolase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-glucosidase (EC:3.2.1.20)
    Alternative name(s):
    Maltase
    Gene namesi
    Name:aglA
    Ordered Locus Names:TM_1834
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101G → A: Reduced activity. 300-fold reduction of the binding affinity for NAD(+). No change in substrate affinity. 1 Publication
    Mutagenesisi12 – 121G → A: No change in activity and substrate affinity. 5-fold reduction of the binding affinity for NAD(+). 1 Publication
    Mutagenesisi13 – 131S → A: Highly reduced activity. 10-fold reduction of the binding affinity for NAD(+). No change in substrate affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 480480Alpha-glucosidasePRO_0000169855Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi243274.TM1834.

    Structurei

    Secondary structure

    1
    480
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Turni10 – 123
    Helixi14 – 2512
    Helixi28 – 303
    Beta strandi34 – 385
    Helixi42 – 5817
    Beta strandi64 – 696
    Helixi71 – 755
    Beta strandi79 – 835
    Helixi89 – 10214
    Beta strandi122 – 1243
    Helixi126 – 14217
    Beta strandi147 – 1504
    Helixi155 – 16511
    Beta strandi168 – 1736
    Helixi176 – 1783
    Helixi179 – 1868
    Helixi191 – 1933
    Beta strandi194 – 2018
    Beta strandi204 – 2129
    Helixi218 – 22710
    Helixi229 – 2313
    Helixi244 – 25310
    Helixi259 – 2613
    Helixi267 – 2704
    Helixi273 – 2808
    Turni282 – 2854
    Helixi290 – 31627
    Helixi322 – 3243
    Beta strandi326 – 3294
    Helixi333 – 34614
    Helixi356 – 36510
    Beta strandi369 – 3768
    Beta strandi388 – 39710
    Beta strandi400 – 4034
    Helixi412 – 4176
    Helixi419 – 43517
    Helixi438 – 4469
    Helixi454 – 46512
    Helixi468 – 4703
    Helixi471 – 4777

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OBBX-ray1.90A/B1-480[»]
    ProteinModelPortaliO33830.
    SMRiO33830. Positions 2-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO33830.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 4 family.Curated

    Phylogenomic databases

    eggNOGiCOG1486.
    KOiK07406.
    OMAiINCWAIK.
    OrthoDBiEOG6TJ7TJ.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 2 hits.
    InterProiIPR019802. GlycHydrolase_4_CS.
    IPR001088. Glyco_hydro_4.
    IPR022616. Glyco_hydro_4_C.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view]
    PRINTSiPR00732. GLHYDRLASE4.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O33830-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAILT    50
    IAKKYVEEVG ADLKFEKTMN LDDVIIDADF VINTAMVGGH TYLEKVRQIG 100
    EKYGYYRGID AQEFNMVSDY YTFSNYNQLK YFVDIARKIE KLSPKAWYLQ 150
    AANPIFEGTT LVTRTVPIKA VGFCHGHYGV MEIVEKLGLE EEKVDWQVAG 200
    VNHGIWLNRF RYNGGNAYPL LDKWIEEKSK DWKPENPFND QLSPAAIDMY 250
    RFYGVMPIGD TVRNSSWRYH RDLETKKKWY GEPWGGADSE IGWKWYQDTL 300
    GKVTEITKKV AKFIKENPSV RLSDLGSVLG KDLSEKQFVL EVEKILDPER 350
    KSGEQHIPFI DALLNDNKAR FVVNIPNKGI IHGIDDDVVV EVPALVDKNG 400
    IHPEKIEPPL PDRVVKYYLR PRIMRMEMAL EAFLTGDIRI IKELLYRDPR 450
    TKSDEQVEKV IEEILALPEN EEMRKHYLKR 480
    Length:480
    Mass (Da):55,047
    Last modified:May 30, 2000 - v2
    Checksum:i4CA5DB3B155CE5A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti459 – 47921Missing(PubMed:9453151)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001089 Genomic DNA. Translation: CAA04524.1.
    AE000512 Genomic DNA. Translation: AAD36897.1.
    PIRiF72205.
    RefSeqiNP_229631.1. NC_000853.1.
    WP_010865414.1. NC_023151.1.
    YP_007978192.1. NC_021214.1.
    YP_008991069.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36897; AAD36897; TM_1834.
    GeneIDi897356.
    KEGGitma:TM1834.
    tmi:THEMA_05030.
    tmm:Tmari_1843.
    PATRICi23938655. VBITheMar51294_1854.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001089 Genomic DNA. Translation: CAA04524.1 .
    AE000512 Genomic DNA. Translation: AAD36897.1 .
    PIRi F72205.
    RefSeqi NP_229631.1. NC_000853.1.
    WP_010865414.1. NC_023151.1.
    YP_007978192.1. NC_021214.1.
    YP_008991069.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OBB X-ray 1.90 A/B 1-480 [» ]
    ProteinModelPortali O33830.
    SMRi O33830. Positions 2-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM1834.

    Protein family/group databases

    CAZyi GH4. Glycoside Hydrolase Family 4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD36897 ; AAD36897 ; TM_1834 .
    GeneIDi 897356.
    KEGGi tma:TM1834.
    tmi:THEMA_05030.
    tmm:Tmari_1843.
    PATRICi 23938655. VBITheMar51294_1854.

    Phylogenomic databases

    eggNOGi COG1486.
    KOi K07406.
    OMAi INCWAIK.
    OrthoDBi EOG6TJ7TJ.

    Enzyme and pathway databases

    BioCyci TMAR243274:GC6P-1885-MONOMER.
    BRENDAi 3.2.1.20. 6331.

    Miscellaneous databases

    EvolutionaryTracei O33830.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 2 hits.
    InterProi IPR019802. GlycHydrolase_4_CS.
    IPR001088. Glyco_hydro_4.
    IPR022616. Glyco_hydro_4_C.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view ]
    PRINTSi PR00732. GLHYDRLASE4.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    PROSITEi PS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima."
      Bibel M., Brettl C., Gosslar U., Kriegshaeuser G., Liebl W.
      FEMS Microbiol. Lett. 158:9-15(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    3. "Thermotoga maritima AglA, an extremely thermostable NAD+-, Mn2+-, and thiol-dependent alpha-glucosidase."
      Raasch C., Streit W., Schanzer J., Bibel M., Gosslar U., Liebl W.
      Extremophiles 4:189-200(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    4. "Identification of residues important for NAD+ binding by the Thermotoga maritima alpha-glucosidase AglA, a member of glycoside hydrolase family 4."
      Raasch C., Armbrecht M., Streit W., Hoecker B., Straeter N., Liebl W.
      FEBS Lett. 517:267-271(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-10; GLY-12 AND SER-13, KINETIC PARAMETERS.
    5. "Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases."
      Lodge J.A., Maier T., Liebl W., Hoffmann V., Straeter N.
      J. Biol. Chem. 278:19151-19158(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH NAD(+) AND MALTOSE.

    Entry informationi

    Entry nameiAGLA_THEMA
    AccessioniPrimary (citable) accession number: O33830
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    In the crystal structure (PubMed:12588867), the metal ion is absent, probably due to the oxidation of the active site Cys-174 to sulfinic acid. In the absence of metal, positions of the coenzyme and the substrate and their interactions are all significantly altered, presumably accounting for the inactivity of this form.1 Publication

    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

    External Data

    Dasty 3