Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

6-phospho-beta-glucosidase BglT

Gene

bglT

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes cellobiose 6'-phosphate into glucose 6-phosphate (Glc6P) and glucose.

Catalytic activityi

6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate.

Cofactori

Protein has several cofactor binding sites:
  • NAD(+)Note: Binds 1 NAD(+) per subunit.
  • Mn2+Note: Binds 1 Mn2+ ion per subunit.

Kineticsi

  1. KM=41 µM for p-nitrophenyl-beta-D-glucopyranoside 6-phosphate

    pH dependencei

    Optimum pH is 8.0. Active from pH 6.5 to 10.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei87 – 871Substrate
    Sitei103 – 1031Increases basicity of active site TyrBy similarity
    Binding sitei140 – 1401Substrate
    Metal bindingi162 – 1621Manganese
    Binding sitei163 – 1631Substrate
    Metal bindingi192 – 1921Manganese
    Active sitei241 – 2411Proton acceptor
    Binding sitei261 – 2611Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1 – 6464NADAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Manganese, Metal-binding, NAD

    Enzyme and pathway databases

    BRENDAi3.2.1.86. 6331.
    SABIO-RKQ9X108.

    Protein family/group databases

    CAZyiGH4. Glycoside Hydrolase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phospho-beta-glucosidase BglT (EC:3.2.1.86)
    Gene namesi
    Name:bglT
    Ordered Locus Names:TM_1281
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4154156-phospho-beta-glucosidase BglTPRO_0000169857Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer or homotetramer. Exists in a homodimer/homotetramer equilibrium state in solution.

    Protein-protein interaction databases

    STRINGi243274.TM1281.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76Combined sources
    Helixi13 – 2311Combined sources
    Turni24 – 263Combined sources
    Beta strandi31 – 355Combined sources
    Helixi39 – 5315Combined sources
    Beta strandi56 – 616Combined sources
    Helixi65 – 695Combined sources
    Beta strandi73 – 775Combined sources
    Helixi83 – 9210Combined sources
    Helixi93 – 975Combined sources
    Beta strandi103 – 1053Combined sources
    Helixi107 – 12923Combined sources
    Beta strandi134 – 1374Combined sources
    Beta strandi139 – 1413Combined sources
    Helixi142 – 15110Combined sources
    Beta strandi156 – 1605Combined sources
    Helixi164 – 17512Combined sources
    Helixi180 – 1823Combined sources
    Beta strandi183 – 1908Combined sources
    Beta strandi193 – 2019Combined sources
    Helixi207 – 2148Combined sources
    Helixi228 – 2347Combined sources
    Beta strandi236 – 2383Combined sources
    Helixi240 – 2423Combined sources
    Helixi243 – 2464Combined sources
    Helixi248 – 2569Combined sources
    Helixi261 – 27616Combined sources
    Helixi284 – 2885Combined sources
    Turni290 – 2934Combined sources
    Helixi294 – 30613Combined sources
    Beta strandi307 – 3093Combined sources
    Beta strandi311 – 3188Combined sources
    Beta strandi331 – 3399Combined sources
    Beta strandi342 – 3465Combined sources
    Helixi353 – 37422Combined sources
    Helixi378 – 38710Combined sources
    Helixi394 – 40714Combined sources
    Turni408 – 4114Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UP4X-ray2.85A/B/C/D/E/F/G/H1-415[»]
    1UP6X-ray2.55A/B/C/D/E/F/G/H1-415[»]
    1UP7X-ray2.40A/B/C/D/E/F/G/H1-415[»]
    ProteinModelPortaliQ9X108.
    SMRiQ9X108. Positions 1-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X108.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 4 family.Curated

    Phylogenomic databases

    eggNOGiCOG1486.
    InParanoidiQ9X108.
    KOiK01222.
    OMAiCNVPINF.
    OrthoDBiEOG6CP3SG.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProiIPR019802. 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]
    PfamiPF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view]
    PRINTSiPR00732. GLHYDRLASE4.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9X108-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRIAVIGGGS SYTPELVKGL LDISEDVRID EVIFYDIDEE KQKIVVDFVK
    60 70 80 90 100
    RLVKDRFKVL ISDTFEGAVV DAKYVIFQFR PGGLKGREND EGIPLKYGLI
    110 120 130 140 150
    GQETTGVGGF SAALRAFPIV EEYVDTVRKT SNATIVNFTN PSGHITEFVR
    160 170 180 190 200
    NYLEYEKFIG LCNVPINFIR EIAEMFSARL EDVFLKYYGL NHLSFIEKVF
    210 220 230 240 250
    VKGEDVTEKV FENLKLKLSN IPDEDFPTWF YDSVRLIVNP YLRYYLMEKK
    260 270 280 290 300
    MFKKISTHEL RAREVMKIEK ELFEKYRTAV EIPEELTKRG GSMYSTAAAH
    310 320 330 340 350
    LIRDLETDEG KIHIVNTRNN GSIENLPDDY VLEIPCYVRS GRVHTLSQGK
    360 370 380 390 400
    GDHFALSFIH AVKMYERLTI EAYLKRSKKL ALKALLSHPL GPDVEDAKDL
    410
    LEEILEANRE YVKLG
    Length:415
    Mass (Da):47,627
    Last modified:November 1, 1999 - v1
    Checksum:iFB4E3B358245BFEE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36356.1.
    PIRiE72273.
    RefSeqiNP_229086.1. NC_000853.1.
    WP_004079953.1. NZ_CP011107.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36356; AAD36356; TM_1281.
    GeneIDi898202.
    KEGGitma:TM1281.
    tmi:THEMA_07930.
    tmm:Tmari_1286.
    PATRICi23937500. VBITheMar51294_1296.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36356.1.
    PIRiE72273.
    RefSeqiNP_229086.1. NC_000853.1.
    WP_004079953.1. NZ_CP011107.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UP4X-ray2.85A/B/C/D/E/F/G/H1-415[»]
    1UP6X-ray2.55A/B/C/D/E/F/G/H1-415[»]
    1UP7X-ray2.40A/B/C/D/E/F/G/H1-415[»]
    ProteinModelPortaliQ9X108.
    SMRiQ9X108. Positions 1-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243274.TM1281.

    Protein family/group databases

    CAZyiGH4. Glycoside Hydrolase Family 4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD36356; AAD36356; TM_1281.
    GeneIDi898202.
    KEGGitma:TM1281.
    tmi:THEMA_07930.
    tmm:Tmari_1286.
    PATRICi23937500. VBITheMar51294_1296.

    Phylogenomic databases

    eggNOGiCOG1486.
    InParanoidiQ9X108.
    KOiK01222.
    OMAiCNVPINF.
    OrthoDBiEOG6CP3SG.

    Enzyme and pathway databases

    BRENDAi3.2.1.86. 6331.
    SABIO-RKQ9X108.

    Miscellaneous databases

    EvolutionaryTraceiQ9X108.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProiIPR019802. 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]
    PfamiPF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view]
    PRINTSiPR00732. GLHYDRLASE4.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima."
      Yip V.L.Y., Varrot A., Davies G.J., Rajan S.S., Yang X., Thompson J., Anderson W.F., Withers S.G.
      J. Am. Chem. Soc. 126:8354-8355(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, REACTION MECHANISM.
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    3. "NAD(+) and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-beta-D-glucosides."
      Varrot A., Yip V.L.Y., Li Y., Rajan S.S., Yang X., Anderson W.F., Thompson J., Withers S.G., Davies G.J.
      J. Mol. Biol. 346:423-435(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH NAD(+) AND GLUCOSE-6-PHOSPHATE.

    Entry informationi

    Entry nameiBGLT_THEMA
    AccessioniPrimary (citable) accession number: Q9X108
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: November 1, 1999
    Last modified: July 22, 2015
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Is a retaining glucosidase as it hydrolyzes glycosidic bond with retention of anomeric configuration. Reaction mechanism includes redox steps involving NAD and stabilization of intermediates by Mn2+.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.