Q9AGA6 (AGLB_KLEPN) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 63. History...
Names and origin
|Sequence length||440 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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
Maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate.
Divalent metal ion. Manganese, cobalt and nickel ions enhance activity whereas magnesium, calcium, and zinc ions are without effect or inhibitory. Ref.1
Belongs to the glycosyl hydrolase 4 family.
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
|Biological process||Carbohydrate metabolism|
|Technical term||Direct protein sequencing|
|Gene Ontology (GO)|
|Biological_process||sucrose metabolic process|
Inferred from electronic annotation. Source: UniProtKB-UniPathway
|Molecular_function||maltose-6'-phosphate glucosidase activity|
Inferred from electronic annotation. Source: ECmetal ion binding
Inferred from electronic annotation. Source: UniProtKB-KWnucleotide binding
Inferred from electronic annotation. Source: InterProoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Inferred from electronic annotation. Source: InterPro
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 440||440||6-phospho-alpha-glucosidase||PRO_0000169856|
|Nucleotide binding||4 – 70||67||NAD By similarity|
|Active site||170||1||Proton donor By similarity|
|Active site||263||1||Proton acceptor By similarity|
|Metal binding||169||1||Manganese By similarity|
|Metal binding||200||1||Manganese By similarity|
|Binding site||93||1||Substrate By similarity|
|Binding site||147||1||Substrate By similarity|
|Binding site||283||1||Substrate By similarity|
|Site||109||1||Increases basicity of active site Tyr By similarity|
|||"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, COFACTORS, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, INDUCTION, SUBUNIT, MASS SPECTROMETRY.
Strain: ATCC 23357 / A-11.
|||"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.
|AF337811 Genomic DNA. Translation: AAK01457.1.|
3D structure databases
|SMR||Q9AGA6. Positions 2-439. |
Protein family/group databases
|CAZy||GH4. Glycoside Hydrolase Family 4. |
Protocols and materials databases
Enzyme and pathway databases
|BRENDA||22.214.171.124. 2814. |
Family and domain databases
|Gene3D||126.96.36.1990. 1 hit. |
188.8.131.52. 1 hit.
|InterPro||IPR019802. GlycHydrolase_4_CS. |
|Pfam||PF02056. Glyco_hydro_4. 1 hit. |
PF11975. Glyco_hydro_4C. 1 hit.
|PRINTS||PR00732. GLHYDRLASE4. |
|SUPFAM||SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
|PROSITE||PS01324. GLYCOSYL_HYDROL_F4. 1 hit. |
|Accession||Primary (citable) accession number: Q9AGA6|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Prokaryotic Protein Annotation Program|