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O86960

- AGLA_THENE

UniProt

O86960 - AGLA_THENE

Protein

Alpha-glucosidase

Gene

aglA

Organism
Thermotoga neapolitana
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 2 (25 Jan 2012)
      Previous versions | rss
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    Functioni

    Is able to hydrolyze diverse types of alpha-glycoside bonds in di- and trisaccharides: alpha-1,4 bonds of maltose and maltotriose, alpha-1,1 bonds of trehalose, alpha-1,2 bonds of sucrose, alpha-1,3 bonds of turanose and melizitose, alpha-1,6 bonds of isomaltose and melibiose. AglA is not specific with respect to the configuration at the C-4 position of its substrates because it also possesses alpha-galactosidase activity. Acts on the substrate from the non-reducing end of the chain. The activity of AglA drops with increasing length of the saccharide chain. Does not hydrolyze alpha-, beta-, and gamma-cyclodextrins or polysaccharides (starch, pullulan, amylose, amylopectin, glycogen). Does not cleave beta-glycosidic bonds in di-, oligo-, or polysaccharides.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 NAD per subunit.1 Publication
    Binds 1 manganese ion per subunit.1 Publication

    Enzyme regulationi

    Inhibited by EDTA in vitro.1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 85 degrees Celsius. Retains 80% activity after incubation at 85 degrees Celsius for 3 hours.1 Publication

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 7067NADBy similarityAdd
    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

    Manganese, Metal-binding, NAD

    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
    OrganismiThermotoga neapolitana
    Taxonomic identifieri2337 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 480480Alpha-glucosidasePRO_0000415284Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 4 family.Curated

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 2 hits.
    InterProiIPR001088. 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.

    Sequencei

    Sequence statusi: Complete.

    O86960-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAVLT    50
    IAKKYVEEVG ADLKFEKTTS VDEAIADADF VINTAMVGGH TYLEKVRRIS 100
    EKYGYYRGID AQEFNMVSDY YTFSNYNQLK YFVDIARKIE RLSPKAWYSA 150
    AANPVFEGTT LVTRTVPIKA VGFCHGHYGV MEIIEKLGLE RKQVDWQVAG 200
    VNHGIWLNRF RYNGEDAYPL LPRWISEKSK DWKPENPFND QLSPAAIDMY 250
    KFYGVMPIGD TVRNASWRYH RDLETKKRWY GEPWGGADSE IGWKWYQDTL 300
    GKVTDITKKV AKFIKENPAL KLSDLGSVLG KDLSEKQFVL EVEKILDPEK 350
    KSGEQHISFH DALLNDNRSR FVINIPNKGI IQGIDDDVVV EVPAVVDRDG 400
    IHPEKIDPPL PERVVKYYLR PRIMRMEMAL EAFLTGDIRI IKEVLYRDPR 450
    TKSDEQVEKV IEEILSLPEN EEMRKNYLKK 480
    Length:480
    Mass (Da):54,901
    Last modified:January 25, 2012 - v2
    Checksum:i93A471746B46B21B
    GO

    Sequence cautioni

    The sequence CAA08868.1 differs from that shown. Reason: Frameshift at position 459.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ009832 Genomic DNA. Translation: CAA08868.1. Frameshift.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ009832 Genomic DNA. Translation: CAA08868.1 . Frameshift.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH4. Glycoside Hydrolase Family 4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 2 hits.
    InterProi 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.
    ProtoNeti Search...

    Publicationsi

    1. "Thermotoga neapolitana gene clusters participating in degradation of starch and maltodextins: molecular structure of the locus."
      Berezina O.V., Lunina N.A., Zverlov V.V., Naumoff D.G., Liebl W., Velikodvorskaya G.A.
      Mol. Biol. (Mosk.) 37:801-809(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Z2706-MC24.
    2. "Thermotoga neopolitina gene cluster, participating in degradation of starch and maltodextrins: expression of aglB and aglA gene in Escherichia coli, properties of recombinant enzymes."
      Lunina N.A., Berezina O.V., Veith B., Zverlov V.V., Vorob'eva I.P., Chekanovskaia L.A., Khromov I.S., Raash G., Libel W., Velikodvorskaia G.A.
      Mol. Biol. (Mosk.) 37:810-819(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
      Strain: Z2706-MC24.

    Entry informationi

    Entry nameiAGLA_THENE
    AccessioniPrimary (citable) accession number: O86960
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: January 25, 2012
    Last modified: October 1, 2014
    This is version 52 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3