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O33830 (AGLA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:TM_1834
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

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

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 NAD per subunit. Ref.3

Binds 1 manganese ion per subunit. Can also use cobalt and nickel ions, albeit less efficiently than manganese ion. Ref.3

Enzyme regulation

Inhibited by Hg2+ ion and EDTA.

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 4 family.

Caution

In the crystal structure (Ref.5), 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.

Biophysicochemical properties

Kinetic parameters:

KM=0.23 mM for p-nitrophenyl-alpha-D-glucopyranoside Ref.3 Ref.4

KM=0.53 mM for p-nitrophenyl-alpha-D-galactopyranoside

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

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

pH dependence:

Optimum pH is 7.5. Active from pH 6.5 to 9.

Temperature dependence:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Alpha-glucosidase
PRO_0000169855

Regions

Nucleotide binding4 – 7067NAD

Sites

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

Experimental info

Mutagenesis101G → A: Reduced activity. 300-fold reduction of the binding affinity for NAD(+). No change in substrate affinity. Ref.4
Mutagenesis121G → A: No change in activity and substrate affinity. 5-fold reduction of the binding affinity for NAD(+). Ref.4
Mutagenesis131S → A: Highly reduced activity. 10-fold reduction of the binding affinity for NAD(+). No change in substrate affinity. Ref.4
Sequence conflict459 – 47921Missing Ref.1

Secondary structure

............................................................................... 480
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O33830 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 4CA5DB3B155CE5A1

FASTA48055,047
        10         20         30         40         50         60 
MPSVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAILT IAKKYVEEVG 

        70         80         90        100        110        120 
ADLKFEKTMN LDDVIIDADF VINTAMVGGH TYLEKVRQIG EKYGYYRGID AQEFNMVSDY 

       130        140        150        160        170        180 
YTFSNYNQLK YFVDIARKIE KLSPKAWYLQ AANPIFEGTT LVTRTVPIKA VGFCHGHYGV 

       190        200        210        220        230        240 
MEIVEKLGLE EEKVDWQVAG VNHGIWLNRF RYNGGNAYPL LDKWIEEKSK DWKPENPFND 

       250        260        270        280        290        300 
QLSPAAIDMY RFYGVMPIGD TVRNSSWRYH RDLETKKKWY GEPWGGADSE IGWKWYQDTL 

       310        320        330        340        350        360 
GKVTEITKKV AKFIKENPSV RLSDLGSVLG KDLSEKQFVL EVEKILDPER KSGEQHIPFI 

       370        380        390        400        410        420 
DALLNDNKAR FVVNIPNKGI IHGIDDDVVV EVPALVDKNG IHPEKIEPPL PDRVVKYYLR 

       430        440        450        460        470        480 
PRIMRMEMAL EAFLTGDIRI IKELLYRDPR TKSDEQVEKV IEEILALPEN EEMRKHYLKR 

« Hide

References

« Hide 'large scale' references
[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]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001089 Genomic DNA. Translation: CAA04524.1.
AE000512 Genomic DNA. Translation: AAD36897.1.
PIRF72205.
RefSeqNP_229631.1. NC_000853.1.
YP_007978192.1. NC_021214.1.
YP_008991069.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OBBX-ray1.90A/B1-480[»]
ProteinModelPortalO33830.
SMRO33830. Positions 2-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1834.

Protein family/group databases

CAZyGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36897; AAD36897; TM_1834.
GeneID897356.
KEGGtma:TM1834.
tmi:THEMA_05030.
tmm:Tmari_1843.
PATRIC23938655. VBITheMar51294_1854.

Phylogenomic databases

eggNOGCOG1486.
KOK07406.
OMAINCWAIK.
OrthoDBEOG6TJ7TJ.

Enzyme and pathway databases

BioCycTMAR243274:GC6P-1885-MONOMER.
BRENDA3.2.1.20. 6331.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 2 hits.
InterProIPR019802. 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]
PfamPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSPR00732. GLHYDRLASE4.
SUPFAMSSF56327. SSF56327. 1 hit.
PROSITEPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO33830.

Entry information

Entry nameAGLA_THEMA
AccessionPrimary (citable) accession number: O33830
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 113 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries