UniProtKB - O33830 (AGLA_THEMA)
Protein
Alpha-glucosidase
Gene
aglA
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
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.
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
Catalytic activityi
- Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose. EC:3.2.1.20
Cofactori
Protein has several cofactor binding sites:- NAD+1 PublicationNote: Binds 1 NAD+ per subunit.1 Publication
- Mn2+1 Publication, Co2+1 Publication, Ni2+1 PublicationNote: Binds 1 Mn2+ ion per subunit. Can also use Co2+ and Ni2+ ions, albeit less efficiently than manganese ion.1 Publication
Activity regulationi
Inhibited by Hg2+ ion and EDTA.
Kineticsi
- KM=0.23 mM for p-nitrophenyl-alpha-D-glucopyranoside2 Publications
- 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 119 | Substrate | 1 | |
Binding sitei | 153 | Substrate | 1 | |
Metal bindingi | 174 | ManganeseBy similarity | 1 | |
Active sitei | 175 | Proton donorCurated | 1 | |
Metal bindingi | 203 | ManganeseBy similarity | 1 | |
Active sitei | 260 | Proton acceptorCurated | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 4 – 70 | NADAdd BLAST | 67 |
GO - Molecular functioni
- maltose alpha-glucosidase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Biological process | Carbohydrate metabolism |
Ligand | Cobalt, Manganese, Metal-binding, NAD, Nickel |
Enzyme and pathway databases
BRENDAi | 3.2.1.20, 6331 |
SABIO-RKi | O33830 |
Protein family/group databases
CAZyi | GH4, Glycoside Hydrolase Family 4 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:aglA Ordered Locus Names:TM_1834 |
Organismi | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
Taxonomic identifieri | 243274 [NCBI] |
Taxonomic lineagei | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 10 | G → A: Reduced activity. 300-fold reduction of the binding affinity for NAD(+). No change in substrate affinity. 1 Publication | 1 | |
Mutagenesisi | 12 | G → A: No change in activity and substrate affinity. 5-fold reduction of the binding affinity for NAD(+). 1 Publication | 1 | |
Mutagenesisi | 13 | S → A: Highly reduced activity. 10-fold reduction of the binding affinity for NAD(+). No change in substrate affinity. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB03323, Maltose |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000169855 | 1 – 480 | Alpha-glucosidaseAdd BLAST | 480 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
STRINGi | 243274.THEMA_05030 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | O33830 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O33830 |
Family & Domainsi
Sequence similaritiesi
Belongs to the glycosyl hydrolase 4 family.Curated
Phylogenomic databases
eggNOGi | COG1486, Bacteria |
InParanoidi | O33830 |
OMAi | YYSTESN |
OrthoDBi | 277080at2 |
Family and domain databases
InterProi | View protein in InterPro IPR019802, GlycHydrolase_4_CS IPR001088, Glyco_hydro_4 IPR022616, Glyco_hydro_4_C IPR015955, Lactate_DH/Glyco_Ohase_4_C IPR036291, NAD(P)-bd_dom_sf |
PANTHERi | PTHR32092, PTHR32092, 1 hit |
Pfami | View protein in Pfam PF02056, Glyco_hydro_4, 1 hit PF11975, Glyco_hydro_4C, 1 hit |
PRINTSi | PR00732, GLHYDRLASE4 |
SUPFAMi | SSF51735, SSF51735, 1 hit SSF56327, SSF56327, 1 hit |
PROSITEi | View protein in PROSITE PS01324, GLYCOSYL_HYDROL_F4, 1 hit |
i Sequence
Sequence statusi: Complete.
O33830-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 459 – 479 | Missing (PubMed:9453151).CuratedAdd BLAST | 21 |
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, NZ_CP011107.1 |
Genome annotation databases
EnsemblBacteriai | AAD36897; AAD36897; TM_1834 |
KEGGi | tma:TM1834 |
Similar proteinsi
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, NZ_CP011107.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1OBB | X-ray | 1.90 | A/B | 1-480 | [»] | |
SMRi | O33830 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 243274.THEMA_05030 |
Chemistry databases
DrugBanki | DB03323, Maltose |
Protein family/group databases
CAZyi | GH4, Glycoside Hydrolase Family 4 |
Genome annotation databases
EnsemblBacteriai | AAD36897; AAD36897; TM_1834 |
KEGGi | tma:TM1834 |
Phylogenomic databases
eggNOGi | COG1486, Bacteria |
InParanoidi | O33830 |
OMAi | YYSTESN |
OrthoDBi | 277080at2 |
Enzyme and pathway databases
BRENDAi | 3.2.1.20, 6331 |
SABIO-RKi | O33830 |
Miscellaneous databases
EvolutionaryTracei | O33830 |
Family and domain databases
InterProi | View protein in InterPro IPR019802, GlycHydrolase_4_CS IPR001088, Glyco_hydro_4 IPR022616, Glyco_hydro_4_C IPR015955, Lactate_DH/Glyco_Ohase_4_C IPR036291, NAD(P)-bd_dom_sf |
PANTHERi | PTHR32092, PTHR32092, 1 hit |
Pfami | View protein in Pfam PF02056, Glyco_hydro_4, 1 hit PF11975, Glyco_hydro_4C, 1 hit |
PRINTSi | PR00732, GLHYDRLASE4 |
SUPFAMi | SSF51735, SSF51735, 1 hit SSF56327, SSF56327, 1 hit |
PROSITEi | View protein in PROSITE PS01324, GLYCOSYL_HYDROL_F4, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | AGLA_THEMA | |
Accessioni | O33830Primary (citable) accession number: O33830 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 15, 1998 |
Last sequence update: | May 30, 2000 | |
Last modified: | April 7, 2021 | |
This is version 151 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families