Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O33830

- AGLA_THEMA

UniProt

O33830 - AGLA_THEMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

Protein has several cofactor binding sites:

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. alpha-1,4-glucosidase activity Source: UniProtKB-EC
  2. maltose alpha-glucosidase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. 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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiO33830.
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

        10         20         30         40         50
MPSVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAILT
60 70 80 90 100
IAKKYVEEVG ADLKFEKTMN LDDVIIDADF VINTAMVGGH TYLEKVRQIG
110 120 130 140 150
EKYGYYRGID AQEFNMVSDY YTFSNYNQLK YFVDIARKIE KLSPKAWYLQ
160 170 180 190 200
AANPIFEGTT LVTRTVPIKA VGFCHGHYGV MEIVEKLGLE EEKVDWQVAG
210 220 230 240 250
VNHGIWLNRF RYNGGNAYPL LDKWIEEKSK DWKPENPFND QLSPAAIDMY
260 270 280 290 300
RFYGVMPIGD TVRNSSWRYH RDLETKKKWY GEPWGGADSE IGWKWYQDTL
310 320 330 340 350
GKVTEITKKV AKFIKENPSV RLSDLGSVLG KDLSEKQFVL EVEKILDPER
360 370 380 390 400
KSGEQHIPFI DALLNDNKAR FVVNIPNKGI IHGIDDDVVV EVPALVDKNG
410 420 430 440 450
IHPEKIEPPL PDRVVKYYLR PRIMRMEMAL EAFLTGDIRI IKELLYRDPR
460 470 480
TKSDEQVEKV IEEILALPEN EEMRKHYLKR
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:
EMBLi
GenBanki
DDBJi
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.
GeneIDi18092856.
897356.
KEGGitma:TM1834.
PATRICi23938655. VBITheMar51294_1854.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 18092856.
897356.
KEGGi tma:TM1834.
PATRICi 23938655. VBITheMar51294_1854.

Phylogenomic databases

eggNOGi COG1486.
InParanoidi O33830.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 117 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