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P39485

- DHG4_BACME

UniProt

P39485 - DHG4_BACME

Protein

Glucose 1-dehydrogenase 4

Gene

gdhIV

Organism
Bacillus megaterium
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei145 – 1451SubstrateBy similarity
    Active sitei158 – 1581Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 3525NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. glucose 1-dehydrogenase [NAD(P)] activity Source: UniProtKB-EC
    2. identical protein binding Source: IntAct

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKP39485.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucose 1-dehydrogenase 4 (EC:1.1.1.47)
    Alternative name(s):
    GLCDH-IV
    Gene namesi
    Name:gdhIV
    OrganismiBacillus megaterium
    Taxonomic identifieri1404 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Glucose 1-dehydrogenase 4PRO_0000054612Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-7977646,EBI-7977646

    Protein-protein interaction databases

    MINTiMINT-8386740.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Beta strandi9 – 124
    Turni13 – 164
    Helixi18 – 2912
    Beta strandi33 – 408
    Helixi42 – 5514
    Beta strandi58 – 636
    Helixi69 – 8315
    Beta strandi88 – 914
    Helixi101 – 1033
    Helixi106 – 11611
    Helixi118 – 13316
    Beta strandi139 – 1435
    Helixi146 – 1483
    Helixi156 – 17621
    Helixi177 – 1793
    Beta strandi182 – 1887
    Beta strandi190 – 1934
    Helixi194 – 1963
    Helixi197 – 2015
    Helixi203 – 2119
    Helixi221 – 23212
    Helixi234 – 2363
    Beta strandi243 – 2475
    Helixi250 – 2523
    Helixi254 – 2563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AUSX-ray2.00A/B1-261[»]
    3AUTX-ray2.00A/B1-261[»]
    3AUUX-ray2.00A/B1-261[»]
    3AY6X-ray2.10A/B/C/D1-261[»]
    3AY7X-ray1.90A/B1-261[»]
    ProteinModelPortaliP39485.
    SMRiP39485. Positions 1-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39485-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYTDLKDKVV VITGGSTGLG RAMAVRFGQE EAKVVINYYN NEEEALDAKK    50
    EVEEAGGQAI IVQGDVTKEE DVVNLVQTAI KEFGTLDVMI NNAGVENPVP 100
    SHELSLDNWN KVIDTNLTGA FLGSREAIKY FVENDIKGNV INMSSVHEMI 150
    PWPLFVHYAA SKGGMKLMTE TLALEYAPKG IRVNNIGPGA MNTPINAEKF 200
    ADPVQRADVE SMIPMGYIGK PEEVAAVAAF LASSQASYVT GITLFADGGM 250
    TKYPSFQAGR G 261
    Length:261
    Mass (Da):28,157
    Last modified:February 1, 1995 - v1
    Checksum:i6FBEC9397BCF417C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10626 Genomic DNA. Translation: BAA01476.1.
    PIRiI40225.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10626 Genomic DNA. Translation: BAA01476.1 .
    PIRi I40225.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AUS X-ray 2.00 A/B 1-261 [» ]
    3AUT X-ray 2.00 A/B 1-261 [» ]
    3AUU X-ray 2.00 A/B 1-261 [» ]
    3AY6 X-ray 2.10 A/B/C/D 1-261 [» ]
    3AY7 X-ray 1.90 A/B 1-261 [» ]
    ProteinModelPortali P39485.
    SMRi P39485. Positions 1-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-8386740.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P39485.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, nucleotide sequences, and enzymatic properties of glucose dehydrogenase isozymes from Bacillus megaterium IAM1030."
      Nagao T., Mitamura T., Wang X.H., Negoro S., Yomo T., Urabe I., Okada H.
      J. Bacteriol. 174:5013-5020(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: IAM 1030.

    Entry informationi

    Entry nameiDHG4_BACME
    AccessioniPrimary (citable) accession number: P39485
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Prefers NAD to NADP; 2M NaCl enhances its pH and thermostability.

    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