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O86960

- AGLA_THENE

UniProt

O86960 - AGLA_THENE

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Protein

Alpha-glucosidase

Gene
aglA
Organism
Thermotoga neapolitana
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191Substrate By similarity
Binding sitei153 – 1531Substrate By similarity
Metal bindingi174 – 1741Manganese By similarity
Active sitei175 – 1751Proton donor By similarity
Metal bindingi203 – 2031Manganese By similarity
Active sitei260 – 2601Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi4 – 7067NAD By 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
Complete GO annotation...

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

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 16, 2013
This is version 51 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

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