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Q9X108

- BGLT_THEMA

UniProt

Q9X108 - BGLT_THEMA

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Protein

6-phospho-beta-glucosidase BglT

Gene

bglT

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - 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 Mn(2+) 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

  1. 6-phospho-beta-glucosidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Manganese, Metal-binding, NAD

Enzyme and pathway databases

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: 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.
OMAiPSGHITE.
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. NC_023151.1.
YP_007977635.1. NC_021214.1.
YP_008991622.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36356; AAD36356; TM_1281.
GeneIDi18093432.
898202.
KEGGitma:TM1281.
PATRICi23937500. VBITheMar51294_1296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36356.1 .
PIRi E72273.
RefSeqi NP_229086.1. NC_000853.1.
WP_004079953.1. NC_023151.1.
YP_007977635.1. NC_021214.1.
YP_008991622.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UP4 X-ray 2.85 A/B/C/D/E/F/G/H 1-415 [» ]
1UP6 X-ray 2.55 A/B/C/D/E/F/G/H 1-415 [» ]
1UP7 X-ray 2.40 A/B/C/D/E/F/G/H 1-415 [» ]
ProteinModelPortali Q9X108.
SMRi Q9X108. Positions 1-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM1281.

Protein family/group databases

CAZyi GH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36356 ; AAD36356 ; TM_1281 .
GeneIDi 18093432.
898202.
KEGGi tma:TM1281.
PATRICi 23937500. VBITheMar51294_1296.

Phylogenomic databases

eggNOGi COG1486.
InParanoidi Q9X108.
KOi K01222.
OMAi PSGHITE.
OrthoDBi EOG6CP3SG.

Enzyme and pathway databases

SABIO-RK Q9X108.

Miscellaneous databases

EvolutionaryTracei Q9X108.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProi IPR019802. 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 ]
Pfami PF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view ]
PRINTSi PR00732. GLHYDRLASE4.
SUPFAMi SSF56327. SSF56327. 1 hit.
PROSITEi PS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 88 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