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Protein

Alpha-glucosidase

Gene

aglA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: 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
  1. Vmax=9.94 µmol/min/mg enzyme with p-nitrophenyl-alpha-D-glucopyranoside as substrate2 Publications
  2. 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)DescriptionActionsGraphical viewLength
Binding sitei119Substrate1
Binding sitei153Substrate1
Metal bindingi174ManganeseBy similarity1
Active sitei175Proton donorCurated1
Metal bindingi203ManganeseBy similarity1
Active sitei260Proton acceptorCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi4 – 70NADAdd BLAST67

GO - Molecular functioni

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

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
Proteomesi
  • UP000008183 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10G → A: Reduced activity. 300-fold reduction of the binding affinity for NAD(+). No change in substrate affinity. 1 Publication1
Mutagenesisi12G → A: No change in activity and substrate affinity. 5-fold reduction of the binding affinity for NAD(+). 1 Publication1
Mutagenesisi13S → A: Highly reduced activity. 10-fold reduction of the binding affinity for NAD(+). No change in substrate affinity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001698551 – 480Alpha-glucosidaseAdd BLAST480

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi243274.TM1834.

Structurei

Secondary structure

1480
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Turni10 – 12Combined sources3
Helixi14 – 25Combined sources12
Helixi28 – 30Combined sources3
Beta strandi34 – 38Combined sources5
Helixi42 – 58Combined sources17
Beta strandi64 – 69Combined sources6
Helixi71 – 75Combined sources5
Beta strandi79 – 83Combined sources5
Helixi89 – 102Combined sources14
Beta strandi122 – 124Combined sources3
Helixi126 – 142Combined sources17
Beta strandi147 – 150Combined sources4
Helixi155 – 165Combined sources11
Beta strandi168 – 173Combined sources6
Helixi176 – 178Combined sources3
Helixi179 – 186Combined sources8
Helixi191 – 193Combined sources3
Beta strandi194 – 201Combined sources8
Beta strandi204 – 212Combined sources9
Helixi218 – 227Combined sources10
Helixi229 – 231Combined sources3
Helixi244 – 253Combined sources10
Helixi259 – 261Combined sources3
Helixi267 – 270Combined sources4
Helixi273 – 280Combined sources8
Turni282 – 285Combined sources4
Helixi290 – 316Combined sources27
Helixi322 – 324Combined sources3
Beta strandi326 – 329Combined sources4
Helixi333 – 346Combined sources14
Helixi356 – 365Combined sources10
Beta strandi369 – 376Combined sources8
Beta strandi388 – 397Combined sources10
Beta strandi400 – 403Combined sources4
Helixi412 – 417Combined sources6
Helixi419 – 435Combined sources17
Helixi438 – 446Combined sources9
Helixi454 – 465Combined sources12
Helixi468 – 470Combined sources3
Helixi471 – 477Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OBBX-ray1.90A/B1-480[»]
ProteinModelPortaliO33830.
SMRiO33830.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO33830.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 4 family.Curated

Phylogenomic databases

eggNOGiENOG4107V4V. Bacteria.
COG1486. LUCA.
InParanoidiO33830.
KOiK07406.
OMAiEMESDVH.

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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. 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)DescriptionActionsGraphical viewLength
Sequence conflicti459 – 479Missing (PubMed:9453151).CuratedAdd BLAST21

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. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36897; AAD36897; TM_1834.
GeneIDi897356.
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.
PIRiF72205.
RefSeqiNP_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 entryMethodResolution (Å)ChainPositionsPDBsum
1OBBX-ray1.90A/B1-480[»]
ProteinModelPortaliO33830.
SMRiO33830.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1834.

Protein family/group databases

CAZyiGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36897; AAD36897; TM_1834.
GeneIDi897356.
KEGGitma:TM1834.
PATRICi23938655. VBITheMar51294_1854.

Phylogenomic databases

eggNOGiENOG4107V4V. Bacteria.
COG1486. LUCA.
InParanoidiO33830.
KOiK07406.
OMAiEMESDVH.

Enzyme and pathway databases

BRENDAi3.2.1.20. 6331.

Miscellaneous databases

EvolutionaryTraceiO33830.

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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 134 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.