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Protein

Alpha-glucosidase

Gene

aglA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: -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.

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.

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

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism
LigandCobalt, Manganese, Metal-binding, NAD, Nickel

Enzyme and pathway databases

BRENDAi3.2.1.20 6331
SABIO-RKO33830

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

Chemistry databases

DrugBankiDB03323 Maltose

PTM / Processingi

Molecule processing

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

Proteomic databases

PRIDEiO33830

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
OMAiEMYSDVH

Family and domain databases

InterProiView 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
PANTHERiPTHR32092 PTHR32092, 1 hit
PfamiView protein in Pfam
PF02056 Glyco_hydro_4, 1 hit
PF11975 Glyco_hydro_4C, 1 hit
PRINTSiPR00732 GLHYDRLASE4
SUPFAMiSSF51735 SSF51735, 1 hit
SSF56327 SSF56327, 1 hit
PROSITEiView protein in PROSITE
PS01324 GLYCOSYL_HYDROL_F4, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiAGLA_THEMA
AccessioniPrimary (citable) accession number: O33830
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2000
Last modified: May 23, 2018
This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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