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P13650

- DHGB_ACICA

UniProt

P13650 - DHGB_ACICA

Protein

Quinoprotein glucose dehydrogenase B

Gene

gdhB

Organism
Acinetobacter calcoaceticus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    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 – 1001Glucose1 Publication
    Binding sitei167 – 1671Glucose1 Publication
    Active sitei168 – 1681Proton acceptor
    Binding sitei192 – 1921Glucose1 Publication
    Binding sitei252 – 2521Glucose1 Publication
    Metal bindingi271 – 2711Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi272 – 2721Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi277 – 2771Calcium 21 Publication
    Metal bindingi287 – 2871Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi293 – 2931Calcium 3; via carbonyl oxygen1 Publication
    Metal bindingi295 – 2951Calcium 3; via carbonyl oxygen1 Publication
    Metal bindingi297 – 2971Calcium 31 Publication
    Metal bindingi333 – 3331Calcium 31 Publication
    Binding sitei367 – 3671PQQ; via carbonyl oxygen1 Publication
    Binding sitei372 – 3721PQQ1 Publication
    Binding sitei401 – 4011PQQ1 Publication

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13650.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the PQQ oxidoreductase GdhB family.Curated

    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: October 1, 2014
    This is version 83 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