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O86960 (AGLA_THENE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-glucosidase

EC=3.2.1.20
Alternative name(s):
Maltase
Gene names
Name:aglA
OrganismThermotoga neapolitana
Taxonomic identifier2337 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose. Ref.2

Cofactor

Binds 1 NAD per subunit. Ref.2

Binds 1 manganese ion per subunit. Ref.2

Enzyme regulation

Inhibited by EDTA in vitro. Ref.2

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 4 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5. Ref.2

Temperature dependence:

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

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Alpha-glucosidase
PRO_0000415284

Regions

Nucleotide binding4 – 7067NAD By similarity

Sites

Active site1751Proton donor By similarity
Active site2601Proton acceptor By similarity
Metal binding1741Manganese By similarity
Metal binding2031Manganese By similarity
Binding site1191Substrate By similarity
Binding site1531Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O86960 [UniParc].

Last modified January 25, 2012. Version 2.
Checksum: 93A471746B46B21B

FASTA48054,901
        10         20         30         40         50         60 
MPAVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAVLT IAKKYVEEVG 

        70         80         90        100        110        120 
ADLKFEKTTS VDEAIADADF VINTAMVGGH TYLEKVRRIS EKYGYYRGID AQEFNMVSDY 

       130        140        150        160        170        180 
YTFSNYNQLK YFVDIARKIE RLSPKAWYSA AANPVFEGTT LVTRTVPIKA VGFCHGHYGV 

       190        200        210        220        230        240 
MEIIEKLGLE RKQVDWQVAG VNHGIWLNRF RYNGEDAYPL LPRWISEKSK DWKPENPFND 

       250        260        270        280        290        300 
QLSPAAIDMY KFYGVMPIGD TVRNASWRYH RDLETKKRWY GEPWGGADSE IGWKWYQDTL 

       310        320        330        340        350        360 
GKVTDITKKV AKFIKENPAL KLSDLGSVLG KDLSEKQFVL EVEKILDPEK KSGEQHISFH 

       370        380        390        400        410        420 
DALLNDNRSR FVINIPNKGI IQGIDDDVVV EVPAVVDRDG IHPEKIDPPL PERVVKYYLR 

       430        440        450        460        470        480 
PRIMRMEMAL EAFLTGDIRI IKEVLYRDPR TKSDEQVEKV IEEILSLPEN EEMRKNYLKK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ009832 Genomic DNA. Translation: CAA08868.1. Frameshift.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 2 hits.
InterProIPR001088. Glyco_hydro_4.
IPR022616. Glyco_hydro_4_C.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSPR00732. GLHYDRLASE4.
SUPFAMSSF56327. SSF56327. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAGLA_THENE
AccessionPrimary (citable) accession number: O86960
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries