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Entry version 109 (11 Dec 2019)
Sequence version 1 (01 Jun 2001)
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Protein

6-phospho-alpha-glucosidase

Gene

aglB

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Is involved in the catabolism of alpha-glycosides accumulated via a phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). Hydrolyzes a wide variety of 6-phospho-alpha-D-glucosides including maltose-6'-phosphate, isomaltose-6'-phosphate, maltitol-6-phosphate, trehalose-6-phosphate and the 6'-phosphorylated derivatives of the five linkage-isomeric alpha-D-glucosyl-D-fructoses: trehalulose-6'-phosphate, turanose-6'-phosphate, maltulose-6'-phosphate, leucrose-6'-phosphate, and palatinose-6'-phosphate. However, sucrose-6-phosphate is not a substrate for this enzyme.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.23 mM for trehalulose-6'-phosphate1 Publication
  2. KM=1.68 mM for turanose-6'-phosphate1 Publication
  3. KM=1.20 mM for maltulose-6'-phosphate1 Publication
  4. KM=5.63 mM for leucrose-6'-phosphate1 Publication
  5. KM=2.42 mM for palatinose-6'-phosphate1 Publication
  6. KM=3.08 mM for maltose-6'-phosphate1 Publication
  7. KM=4.48 mM for isomaltose-6'-phosphate1 Publication
  8. KM=0.82 mM for maltitol-6-phosphate1 Publication
  9. KM=1.16 mM for trehalose-6-phosphate1 Publication
  10. KM=0.05 mM for p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate1 Publication
  1. Vmax=0.89 µmol/min/mg enzyme with trehalulose-6'-phosphate as substrate1 Publication
  2. Vmax=2.41 µmol/min/mg enzyme with turanose-6'-phosphate as substrate1 Publication
  3. Vmax=1.15 µmol/min/mg enzyme with maltulose-6'-phosphate as substrate1 Publication
  4. Vmax=0.85 µmol/min/mg enzyme with leucrose-6'-phosphate as substrate1 Publication
  5. Vmax=0.90 µmol/min/mg enzyme with palatinose-6'-phosphate as substrate1 Publication
  6. Vmax=1.31 µmol/min/mg enzyme with maltose-6'-phosphate as substrate1 Publication
  7. Vmax=1.55 µmol/min/mg enzyme with isomaltose-6'-phosphate as substrate1 Publication
  8. Vmax=1.87 µmol/min/mg enzyme with maltitol-6-phosphate as substrate1 Publication
  9. Vmax=0.31 µmol/min/mg enzyme with trehalose-6-phosphate as substrate1 Publication
  10. Vmax=2.42 µmol/min/mg enzyme with p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate as substrate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: sucrose metabolism

This protein is involved in the pathway sucrose metabolism, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway sucrose metabolism and in Glycan biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei93SubstrateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei109Increases basicity of active site TyrBy similarity1
Binding sitei147SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi169ManganeseBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei170Proton donorBy similarity1
Metal bindingi200ManganeseBy similarity1
Active sitei263Proton acceptorBy similarity1
Binding sitei283SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi4 – 70NADBy similarityAdd BLAST67

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.122 2814

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q9AGA6

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00238

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH4 Glycoside Hydrolase Family 4

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
6-phospho-alpha-glucosidase (EC:3.2.1.122)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:aglB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiKlebsiella pneumoniae
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri573 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001698561 – 4406-phospho-alpha-glucosidaseAdd BLAST440

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By the five linkage-isomeric alpha-D-glucosyl-D-fructoses, or by maltose or maltitol.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9AGA6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 4 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105F8D Bacteria
COG1486 LUCA

Database of Orthologous Groups

More...
OrthoDBi
277080at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.110.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

The PANTHER Classification System

More...
PANTHERi
PTHR32092 PTHR32092, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02056 Glyco_hydro_4, 1 hit
PF11975 Glyco_hydro_4C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00732 GLHYDRLASE4

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit
SSF56327 SSF56327, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01324 GLYCOSYL_HYDROL_F4, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9AGA6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKFSVVIAG GGSTFTPGIV LMLLANQDRF PLRSLKFYDN DGARQETIAE
60 70 80 90 100
ACKVILKEQA PEIEFSYTTD PQAAFTDVDF VMAHIRVGKY PMREQDEKIP
110 120 130 140 150
LRHGVLGQET CGPGGIAYGM RSIGGVLELV DYMEKYSPNA WMLNYSNPAA
160 170 180 190 200
IVAEATRRLR PNAKILNICD MPIGIEGRMA QIVGLKDRKQ MRVRYYGLNH
210 220 230 240 250
FGWWTSIEDL DGNDLMPKLR EYVAKYGYVP PSNDPHTEAS WNDTFAKAKD
260 270 280 290 300
VQALDPQTMP NTYLKYYLFP DYVVAHSNPE RTRANEVMDH REKNVFSACR
310 320 330 340 350
AIIAAGKSTA GDLEIDEHAS YIVDLATAIA FNTQERMLLI VPNNGAIHNF
360 370 380 390 400
DADAMVEIPC LVGHNGPEPL TVGDIPHFQK GLMSQQVAVE KLVVDAWEQR
410 420 430 440
SYHKLWQAIT LSKTVPSASV AKAILDDLIA ANKDYWPELH
Length:440
Mass (Da):49,255
Last modified:June 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5D7287435E4DDC45
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 49254 Da. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF337811 Genomic DNA Translation: AAK01457.1

NCBI Reference Sequences

More...
RefSeqi
WP_002923306.1, NZ_VSSY01000020.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF337811 Genomic DNA Translation: AAK01457.1
RefSeqiWP_002923306.1, NZ_VSSY01000020.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6DUXX-ray2.25A/B2-440[»]
6DVVX-ray2.25A/B2-440[»]
SMRiQ9AGA6
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiGH4 Glycoside Hydrolase Family 4

Phylogenomic databases

eggNOGiENOG4105F8D Bacteria
COG1486 LUCA
OrthoDBi277080at2

Enzyme and pathway databases

UniPathwayiUPA00238
BRENDAi3.2.1.122 2814
SABIO-RKiQ9AGA6

Family and domain databases

Gene3Di3.90.110.10, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAGLB_KLEPN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9AGA6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 1, 2001
Last modified: December 11, 2019
This is version 109 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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