6-phospho-alpha-glucosidase - Klebsiella pneumoniae

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Q9AGA6 (AGLB_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
6-phospho-alpha-glucosidase
EC=3.2.1.122

Gene names

Name:

aglB

Organism

Klebsiella pneumoniae

Taxonomic identifier

573 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Maltose 6'-phosphate + H₂O = D-glucose + D-glucose 6-phosphate.
Cofactor	NAD. Ref.1 Divalent metal ion. Manganese, cobalt and nickel ions enhance activity whereas magnesium, calcium, and zinc ions are without effect or inhibitory. 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: K_M=1.23 mM for trehalulose-6'-phosphate Ref.1 K_M=1.68 mM for turanose-6'-phosphate K_M=1.20 mM for maltulose-6'-phosphate K_M=5.63 mM for leucrose-6'-phosphate K_M=2.42 mM for palatinose-6'-phosphate K_M=3.08 mM for maltose-6'-phosphate K_M=4.48 mM for isomaltose-6'-phosphate K_M=0.82 mM for maltitol-6-phosphate K_M=1.16 mM for trehalose-6-phosphate K_M=0.05 mM for p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate V_max=0.89 µmol/min/mg enzyme with trehalulose-6'-phosphate as substrate V_max=2.41 µmol/min/mg enzyme with turanose-6'-phosphate as substrate V_max=1.15 µmol/min/mg enzyme with maltulose-6'-phosphate as substrate V_max=0.85 µmol/min/mg enzyme with leucrose-6'-phosphate as substrate V_max=0.90 µmol/min/mg enzyme with palatinose-6'-phosphate as substrate V_max=1.31 µmol/min/mg enzyme with maltose-6'-phosphate as substrate V_max=1.55 µmol/min/mg enzyme with isomaltose-6'-phosphate as substrate V_max=1.87 µmol/min/mg enzyme with maltitol-6-phosphate as substrate V_max=0.31 µmol/min/mg enzyme with trehalose-6-phosphate as substrate V_max=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

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Cobalt Manganese Metal-binding NAD Nickel
Molecular function	Glycosidase Hydrolase
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: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase 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

Molecule processing

Chain

1 – 440

440

6-phospho-alpha-glucosidase

PRO_0000169856

Regions

Nucleotide binding

4 – 70

NAD By similarity

Sites

Active site

170

Proton donor By similarity

Active site

263

Proton acceptor By similarity

Metal binding

169

Manganese By similarity

Metal binding

200

Manganese By similarity

Binding site

Substrate By similarity

Binding site

147

Substrate By similarity

Binding site

283

Substrate By similarity

Site

109

Increases basicity of active site Tyr By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9AGA6 [UniParc].

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

FASTA

440

49,255

        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, COFACTORS, 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
ProteinModelPortal	Q9AGA6.
SMR	Q9AGA6. Positions 2-439.
ModBase	Search...
Protein family/group databases
CAZy	GH4. Glycoside Hydrolase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.2.1.122. 2814.
UniPathway	UPA00238.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
InterPro	IPR019802. 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]
Pfam	PF02056. Glyco_hydro_4. 1 hit. PF11975. Glyco_hydro_4C. 1 hit. [Graphical view]
PRINTS	PR00732. GLHYDRLASE4.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
PROSITE	PS01324. GLYCOSYL_HYDROL_F4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGLB_KLEPN

Accession

Primary (citable) accession number: Q9AGA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents