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Q9AGA6 (AGLB_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phospho-alpha-glucosidase

EC=3.2.1.122
Gene names
Name:aglB
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Catalytic activity

Alpha-maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate.

Cofactor

NAD. Ref.1

Divalent metal ion. Requires Mn2+, Co2+ or Ni2+. Ref.1

Pathway

Glycan biosynthesis; sucrose metabolism.

Subunit structure

Homodimer. Ref.1

Induction

By the five linkage-isomeric alpha-D-glucosyl-D-fructoses, or by maltose or maltitol. Ref.1 Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 4 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.23 mM for trehalulose-6'-phosphate Ref.1

KM=1.68 mM for turanose-6'-phosphate

KM=1.20 mM for maltulose-6'-phosphate

KM=5.63 mM for leucrose-6'-phosphate

KM=2.42 mM for palatinose-6'-phosphate

KM=3.08 mM for maltose-6'-phosphate

KM=4.48 mM for isomaltose-6'-phosphate

KM=0.82 mM for maltitol-6-phosphate

KM=1.16 mM for trehalose-6-phosphate

KM=0.05 mM for p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate

Vmax=0.89 µmol/min/mg enzyme with trehalulose-6'-phosphate as substrate

Vmax=2.41 µmol/min/mg enzyme with turanose-6'-phosphate as substrate

Vmax=1.15 µmol/min/mg enzyme with maltulose-6'-phosphate as substrate

Vmax=0.85 µmol/min/mg enzyme with leucrose-6'-phosphate as substrate

Vmax=0.90 µmol/min/mg enzyme with palatinose-6'-phosphate as substrate

Vmax=1.31 µmol/min/mg enzyme with maltose-6'-phosphate as substrate

Vmax=1.55 µmol/min/mg enzyme with isomaltose-6'-phosphate as substrate

Vmax=1.87 µmol/min/mg enzyme with maltitol-6-phosphate as substrate

Vmax=0.31 µmol/min/mg enzyme with trehalose-6-phosphate as substrate

Vmax=2.42 µmol/min/mg enzyme with p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate as substrate

Mass spectrometry

Molecular mass is 49254 Da from positions 1 - 440. Determined by ESI. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4404406-phospho-alpha-glucosidase
PRO_0000169856

Regions

Nucleotide binding4 – 7067NAD By similarity

Sites

Active site1701Proton donor By similarity
Active site2631Proton acceptor By similarity
Metal binding1691Manganese By similarity
Metal binding2001Manganese By similarity
Binding site931Substrate By similarity
Binding site1471Substrate By similarity
Binding site2831Substrate By similarity
Site1091Increases basicity of active site Tyr By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9AGA6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5D7287435E4DDC45

FASTA44049,255
        10         20         30         40         50         60 
MKKFSVVIAG GGSTFTPGIV LMLLANQDRF PLRSLKFYDN DGARQETIAE ACKVILKEQA 

        70         80         90        100        110        120 
PEIEFSYTTD PQAAFTDVDF VMAHIRVGKY PMREQDEKIP LRHGVLGQET CGPGGIAYGM 

       130        140        150        160        170        180 
RSIGGVLELV DYMEKYSPNA WMLNYSNPAA IVAEATRRLR PNAKILNICD MPIGIEGRMA 

       190        200        210        220        230        240 
QIVGLKDRKQ MRVRYYGLNH FGWWTSIEDL DGNDLMPKLR EYVAKYGYVP PSNDPHTEAS 

       250        260        270        280        290        300 
WNDTFAKAKD VQALDPQTMP NTYLKYYLFP DYVVAHSNPE RTRANEVMDH REKNVFSACR 

       310        320        330        340        350        360 
AIIAAGKSTA GDLEIDEHAS YIVDLATAIA FNTQERMLLI VPNNGAIHNF DADAMVEIPC 

       370        380        390        400        410        420 
LVGHNGPEPL TVGDIPHFQK GLMSQQVAVE KLVVDAWEQR SYHKLWQAIT LSKTVPSASV 

       430        440 
AKAILDDLIA ANKDYWPELH 

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References

[1]"Metabolism of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-fructoses by Klebsiella pneumoniae. Participation and properties of sucrose-6-phosphate hydrolase and phospho-alpha-glucosidase."
Thompson J., Robrish S.A., Immel S., Lichtenthaler F.W., Hall B.G., Pikis A.
J. Biol. Chem. 276:37415-37425(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION, CHARACTERIZATION, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, INDUCTION, SUBUNIT, MASS SPECTROMETRY.
Strain: ATCC 23357 / A-11.
[2]"Phosphorylation and metabolism of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-fructoses by Klebsiella pneumoniae."
Thompson J., Robrish S.A., Pikis A., Brust A., Lichtenthaler F.W.
Carbohydr. Res. 331:149-161(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, INDUCTION.
Strain: ATCC 23357 / A-11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF337811 Genomic DNA. Translation: AAK01457.1.

3D structure databases

ProteinModelPortalQ9AGA6.
SMRQ9AGA6. Positions 2-439.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.122. 2814.
SABIO-RKQ9AGA6.
UniPathwayUPA00238.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR019802. 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]
PfamPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSPR00732. GLHYDRLASE4.
SUPFAMSSF56327. SSF56327. 1 hit.
PROSITEPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGLB_KLEPN
AccessionPrimary (citable) accession number: Q9AGA6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 1, 2001
Last modified: February 19, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries