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P13650

- DHGB_ACICA

UniProt

P13650 - DHGB_ACICA

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Protein

Quinoprotein glucose dehydrogenase B

Gene
gdhB
Organism
Acinetobacter calcoaceticus
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Oxidizes glucose to gluconolactone.

Catalytic activityi

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

Cofactori

Binds 1 PQQ group per subunit.
Binds 3 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001Glucose
Binding sitei167 – 1671Glucose
Active sitei168 – 1681Proton acceptor
Binding sitei192 – 1921Glucose
Binding sitei252 – 2521Glucose
Metal bindingi271 – 2711Calcium 1; via carbonyl oxygen
Metal bindingi272 – 2721Calcium 1; via carbonyl oxygen
Metal bindingi277 – 2771Calcium 2
Metal bindingi287 – 2871Calcium 2; via carbonyl oxygen
Metal bindingi293 – 2931Calcium 3; via carbonyl oxygen
Metal bindingi295 – 2951Calcium 3; via carbonyl oxygen
Metal bindingi297 – 2971Calcium 3
Metal bindingi333 – 3331Calcium 3
Binding sitei367 – 3671PQQ; via carbonyl oxygen
Binding sitei372 – 3721PQQ
Binding sitei401 – 4011PQQ

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. quinone binding Source: InterPro
  3. quinoprotein glucose dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Metal-binding, PQQ

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15518.
BRENDAi1.1.5.2. 99.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:gdhB
OrganismiAcinetobacter calcoaceticus
Taxonomic identifieri471 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Pathology & Biotechi

Biotechnological usei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 478454Quinoprotein glucose dehydrogenase BPRO_0000025583Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 345
Beta strandi41 – 477
Beta strandi51 – 588
Beta strandi64 – 685
Turni69 – 713
Beta strandi73 – 775
Turni79 – 813
Beta strandi84 – 896
Beta strandi102 – 1087
Turni110 – 1145
Beta strandi117 – 1259
Beta strandi136 – 14611
Turni147 – 1504
Beta strandi151 – 16212
Beta strandi170 – 1756
Beta strandi181 – 1855
Turni188 – 1914
Helixi193 – 1953
Helixi208 – 2125
Beta strandi220 – 2267
Beta strandi238 – 2414
Beta strandi245 – 2495
Beta strandi252 – 2598
Beta strandi265 – 2706
Beta strandi272 – 2743
Beta strandi276 – 2805
Turni289 – 2913
Beta strandi293 – 2975
Helixi306 – 3083
Helixi333 – 3353
Beta strandi339 – 3413
Beta strandi345 – 3484
Helixi360 – 3623
Helixi366 – 3694
Beta strandi394 – 4029
Beta strandi405 – 4106
Beta strandi414 – 42512
Beta strandi431 – 4366
Beta strandi438 – 4414
Beta strandi443 – 4475
Beta strandi456 – 4583
Beta strandi470 – 4745

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9UX-ray2.20A/B25-478[»]
1CQ1X-ray1.90A/B25-478[»]
1CRUX-ray1.50A/B25-478[»]
1QBIX-ray1.72A/B25-478[»]
ProteinModelPortaliP13650.
SMRiP13650. Positions 25-476.

Miscellaneous databases

EvolutionaryTraceiP13650.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni252 – 2532PQQ
Regioni430 – 4323PQQ

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR012938. Glc/Sorbosone_DH.
IPR019893. PQQ-dependent_DH_s-GDH.
IPR011041. Quinoprot_gluc/sorb_DH.
[Graphical view]
PfamiPF07995. GSDH. 2 hits.
[Graphical view]
SUPFAMiSSF50952. SSF50952. 1 hit.
TIGRFAMsiTIGR03606. non_repeat_PQQ. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13650-1 [UniParc]FASTAAdd to Basket

« Hide

MNKHLLAKIA LLSAVQLVTL SAFADVPLTP SQFAKAKSEN FDKKVILSNL    50
NKPHALLWGP DNQIWLTERA TGKILRVNPE SGSVKTVFQV PEIVNDADGQ 100
NGLLGFAFHP DFKNNPYIYI SGTFKNPKST DKELPNQTII RRYTYNKSTD 150
TLEKPVDLLA GLPSSKDHQS GRLVIGPDQK IYYTIGDQGR NQLAYLFLPN 200
QAQHTPTQQE LNGKDYHTYM GKVLRLNLDG SIPKDNPSFN GVVSHIYTLG 250
HRNPQGLAFT PNGKLLQSEQ GPNSDDEINL IVKGGNYGWP NVAGYKDDSG 300
YAYANYSAAA NKSIKDLAQN GVKVAAGVPV TKESEWTGKN FVPPLKTLYT 350
VQDTYNYNDP TCGEMTYICW PTVAPSSAYV YKGGKKAITG WENTLLVPSL 400
KRGVIFRIKL DPTYSTTYDD AVPMFKSNNR YRDVIASPDG NVLYVLTDTA 450
GNVQKDDGSV TNTLENPGSL IKFTYKAK 478
Length:478
Mass (Da):52,773
Last modified:January 1, 1990 - v1
Checksum:iA32CF45F55078648
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15871 Genomic DNA. Translation: CAA33881.1.
PIRiS04784.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15871 Genomic DNA. Translation: CAA33881.1 .
PIRi S04784.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C9U X-ray 2.20 A/B 25-478 [» ]
1CQ1 X-ray 1.90 A/B 25-478 [» ]
1CRU X-ray 1.50 A/B 25-478 [» ]
1QBI X-ray 1.72 A/B 25-478 [» ]
ProteinModelPortali P13650.
SMRi P13650. Positions 25-476.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-15518.
BRENDAi 1.1.5.2. 99.

Miscellaneous databases

EvolutionaryTracei P13650.

Family and domain databases

Gene3Di 2.120.10.30. 1 hit.
InterProi IPR011042. 6-blade_b-propeller_TolB-like.
IPR012938. Glc/Sorbosone_DH.
IPR019893. PQQ-dependent_DH_s-GDH.
IPR011041. Quinoprot_gluc/sorb_DH.
[Graphical view ]
Pfami PF07995. GSDH. 2 hits.
[Graphical view ]
SUPFAMi SSF50952. SSF50952. 1 hit.
TIGRFAMsi TIGR03606. non_repeat_PQQ. 1 hit.
ProtoNeti Search...

Publicationsi

  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: PP2403, PP2407 and PP2410.
  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.

Entry informationi

Entry nameiDHGB_ACICA
AccessioniPrimary (citable) accession number: P13650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: December 11, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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