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Protein

Glucose 1-dehydrogenase

Gene

gdh

Organism
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD(P)+-dependent oxidation of D-glucose to D-gluconate via gluconolactone. To a lesser extent, is also active with xylose as substrate, but mannose, arabinose, galactose, fructose 6-phosphate, glucose 6-phosphate, glycerinaldehyde 3-phosphate, ribose, sorbitol, ethanol, erythritol, or lactose are not oxidized by the enzyme. Can utilize both NAD+ and NADP+ as electron acceptor, with a marked preference for NADP+. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.1 Publication

Catalytic activityi

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

Cofactori

Zn2+By similarity

Kineticsi

  1. KM=0.3 mM for glucose (in the presence of NADP+, at 70 degrees Celsius and pH 7)1 Publication
  2. KM=8 mM for xylose (in the presence of NADP+, at 70 degrees Celsius and pH 7)1 Publication
  3. KM=0.7 mM for NADP+ (at 70 degrees Celsius and pH 7)1 Publication
  4. KM=86 mM for NAD+ (at 70 degrees Celsius and pH 7)1 Publication
  1. Vmax=40 µmol/min/mg enzyme for the oxidation of D-glucose by NADP+ (at 70 degrees Celsius and pH 7)1 Publication
  2. Vmax=150 µmol/min/mg enzyme for the oxidation of D-glucose by NAD+ (at 70 degrees Celsius and pH 7)1 Publication
  3. Vmax=60 µmol/min/mg enzyme for the oxidation of D-xylose by NADP+ (at 70 degrees Celsius and pH 7)1 Publication

Temperature dependencei

Highly thermostable with a half-life of inactivation of 10 minutes at 103 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Zinc; catalyticBy similarity
Binding sitei41 – 411SubstrateBy similarity
Metal bindingi64 – 641Zinc; via tele nitrogen; catalyticBy similarity
Metal bindingi65 – 651Zinc; catalyticBy similarity
Binding sitei110 – 1101SubstrateBy similarity
Metal bindingi146 – 1461Zinc; catalyticBy similarity
Binding sitei146 – 1461SubstrateBy similarity
Binding sitei291 – 2911SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1814NADPBy similarity
Nucleotide bindingi260 – 2623NADPBy similarity
Nucleotide bindingi289 – 2913NADPBy similarity

GO - Molecular functioni

  • glucose 1-dehydrogenase [NAD(P)] activity Source: UniProtKB
  • glucose binding Source: UniProtKB
  • NAD+ binding Source: UniProtKB
  • NADP+ binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • xylose binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • non-phosphorylated glucose catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Metal-binding, NAD, NADP, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciTTEN768679:GJSY-335-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose 1-dehydrogenase (EC:1.1.1.47)
Short name:
GDH
Short name:
GlcDH
Gene namesi
Name:gdh
Ordered Locus Names:TTX_0329
OrganismiThermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Taxonomic identifieri768679 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus
Proteomesi
  • UP000002654 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Glucose 1-dehydrogenasePRO_0000414843Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi768679.TTX_0329.

Structurei

3D structure databases

ProteinModelPortaliQ703W7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG01459. Archaea.
COG1063. LUCA.
OMAiMVLHNKA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_02127. Glucose_DH.
InterProiIPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR026583. Glc_1-DH.
IPR031640. Glu_dehyd_C.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF16912. Glu_dehyd_C. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q703W7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAVTVTPGV PESLRLREVP EPKPGPGQVL LKPLLVGVCG TDKEIIEGRY
60 70 80 90 100
GKAPEGSDYL ILGHEALAEV AALGKGVDNV SEGDLVVPTV RRPLDCQLPV
110 120 130 140 150
DYCPPGKYLE HGIWGLHGHA AELSITDAAY LVKVPKELRD IAVLTEPLSV
160 170 180 190 200
VEKGVELGVE SYKARLGSPP KTALVLGAGP VGLLASMVLR LMGVSITAVA
210 220 230 240 250
TRPHDSLKAR LVEELGGRYI DAVHERLEGE FDLVIEATGA PSLAVQGLER
260 270 280 290 300
LAPGGVEVLL GVYPPTGELK GLGSLLTDAV LKNKLVVGSV NAGLRHFERA
310 320 330 340
LAHLKEANDS LNGFPKRLIT KVVPLERYQE AYVWTHDDIK VVLQVQT
Length:347
Mass (Da):37,072
Last modified:July 5, 2004 - v1
Checksum:iC292E175C4ECA071
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ621346 Genomic DNA. Translation: CAF18527.1.
FN869859 Genomic DNA. Translation: CCC81005.1.
RefSeqiWP_014126262.1. NC_016070.1.

Genome annotation databases

EnsemblBacteriaiCCC81005; CCC81005; TTX_0329.
GeneIDi11263340.
KEGGittn:TTX_0329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ621346 Genomic DNA. Translation: CAF18527.1.
FN869859 Genomic DNA. Translation: CCC81005.1.
RefSeqiWP_014126262.1. NC_016070.1.

3D structure databases

ProteinModelPortaliQ703W7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi768679.TTX_0329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCC81005; CCC81005; TTX_0329.
GeneIDi11263340.
KEGGittn:TTX_0329.

Phylogenomic databases

eggNOGiarCOG01459. Archaea.
COG1063. LUCA.
OMAiMVLHNKA.

Enzyme and pathway databases

BioCyciTTEN768679:GJSY-335-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_02127. Glucose_DH.
InterProiIPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR026583. Glc_1-DH.
IPR031640. Glu_dehyd_C.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF16912. Glu_dehyd_C. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Reconstruction of the central carbohydrate metabolism of Thermoproteus tenax using genomic and biochemical data."
    Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M., Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.
    J. Bacteriol. 186:2179-2194(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
  3. "Carbohydrate metabolism in Thermoproteus tenax: in vivo utilization of the non-phosphorylative Entner-Doudoroff pathway and characterization of its first enzyme, glucose dehydrogenase."
    Siebers B., Wendisch V.F., Hensel R.
    Arch. Microbiol. 168:120-127(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-29, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.

Entry informationi

Entry nameiGLCDH_THETK
AccessioniPrimary (citable) accession number: Q703W7
Secondary accession number(s): G4RN61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.