Skip Header

Contribute Send feedback
Read comments (?) or add your own

P13650 (DHGB_ACICA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Quinoprotein glucose dehydrogenase B
EC=1.1.5.2
Alternative name(s):
Glucose dehydrogenase B [pyrroloquinoline-quinone]
Soluble glucose dehydrogenase
Short name=s-GDH
Gene names
Name:gdhB
OrganismAcinetobacter calcoaceticus
Taxonomic identifier471 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidizes glucose to gluconolactone.

Catalytic activity

D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol.

Cofactor

Binds 1 PQQ group per subunit.

Binds 3 calcium ions per subunit.

Subunit structure

Homodimer. Ref.2 Ref.3

Biotechnological use

Potent biocatalyst for the accurate in vivo monitoring of blood glucose in the management of diabetes.

Miscellaneous

Acinetobacter calcoaceticus contains two different PQQ dependent enzymes with GDH activity. GDH-A prefers 2-deoxyglucose as substrate, the specific substrates for GDH-B are disaccharides.

Sequence similarities

Belongs to the PQQ oxidoreductase GdhB family.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
Metal-binding
PQQ
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

quinone binding

Inferred from electronic annotation. Source: InterPro

quinoprotein glucose dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 478454Quinoprotein glucose dehydrogenase B
PRO_0000025583

Regions

Region252 – 2532PQQ
Region430 – 4323PQQ

Sites

Active site1681Proton acceptor
Metal binding2711Calcium 1; via carbonyl oxygen
Metal binding2721Calcium 1; via carbonyl oxygen
Metal binding2771Calcium 2
Metal binding2871Calcium 2; via carbonyl oxygen
Metal binding2931Calcium 3; via carbonyl oxygen
Metal binding2951Calcium 3; via carbonyl oxygen
Metal binding2971Calcium 3
Metal binding3331Calcium 3
Binding site1001Glucose
Binding site1671Glucose
Binding site1921Glucose
Binding site2521Glucose
Binding site3671PQQ; via carbonyl oxygen
Binding site3721PQQ
Binding site4011PQQ

Secondary structure

1 .................................................................................. 478
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13650 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: A32CF45F55078648

FASTA47852,773
        10         20         30         40         50         60 
MNKHLLAKIA LLSAVQLVTL SAFADVPLTP SQFAKAKSEN FDKKVILSNL NKPHALLWGP 

        70         80         90        100        110        120 
DNQIWLTERA TGKILRVNPE SGSVKTVFQV PEIVNDADGQ NGLLGFAFHP DFKNNPYIYI 

       130        140        150        160        170        180 
SGTFKNPKST DKELPNQTII RRYTYNKSTD TLEKPVDLLA GLPSSKDHQS GRLVIGPDQK 

       190        200        210        220        230        240 
IYYTIGDQGR NQLAYLFLPN QAQHTPTQQE LNGKDYHTYM GKVLRLNLDG SIPKDNPSFN 

       250        260        270        280        290        300 
GVVSHIYTLG HRNPQGLAFT PNGKLLQSEQ GPNSDDEINL IVKGGNYGWP NVAGYKDDSG 

       310        320        330        340        350        360 
YAYANYSAAA NKSIKDLAQN GVKVAAGVPV TKESEWTGKN FVPPLKTLYT VQDTYNYNDP 

       370        380        390        400        410        420 
TCGEMTYICW PTVAPSSAYV YKGGKKAITG WENTLLVPSL KRGVIFRIKL DPTYSTTYDD 

       430        440        450        460        470 
AVPMFKSNNR YRDVIASPDG NVLYVLTDTA GNVQKDDGSV TNTLENPGSL IKFTYKAK

« Hide

References

[1]"Cloning, characterization and DNA sequencing of the gene encoding the Mr 50,000 quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus."
Cleton-Jansen A.-M., Goosen N., Vink K., van de Putte P.
Mol. Gen. Genet. 217:430-436(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PP24[03,07,10].
[2]"The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat."
Oubrie A., Rozeboom H.J., Kalk K.H., Duine J.A., Dijkstra B.W.
J. Mol. Biol. 289:319-333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, SUBUNIT.
[3]"Structure and mechanism of soluble quinoprotein glucose dehydrogenase."
Oubrie A., Rozeboom H.J., Kalk K.H., Olsthoorn A.J.J., Duine J.A., Dijkstra B.W.
EMBO J. 18:5187-5194(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE; PQQ AND CALCIUM, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X15871 Genomic DNA. Translation: CAA33881.1.
PIRS04784.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9UX-ray2.20A/B25-478[»]
1CQ1X-ray1.90A/B25-478[»]
1CRUX-ray1.50A/B25-478[»]
1QBIX-ray1.72A/B25-478[»]
ProteinModelPortalP13650.
SMRP13650. Positions 25-476.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15518.
BRENDA1.1.5.2. 99.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR012938. Glc/Sorbosone_DH.
IPR019893. PQQ-dependent_DH_s-GDH.
IPR011041. Quinoprot_gluc/sorb_DH.
[Graphical view]
PfamPF07995. GSDH. 2 hits.
[Graphical view]
SUPFAMSSF50952. Quino_gluc_DH. 1 hit.
TIGRFAMsTIGR03606. non_repeat_PQQ. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP13650.

Entry information

Entry nameDHGB_ACICA
AccessionPrimary (citable) accession number: P13650
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents