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Protein

Glucose 1-dehydrogenase

Gene

gdh

Organism
Sulfolobus solfataricus
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. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-galactose, D-xylose and L-arabinose, to the corresponding glyconate. Can utilize both NAD+ and NADP+ as electron acceptor. Physiologically, seems to be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway.2 Publications

Catalytic activityi

D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H.2 Publications
D-galactose + NAD+ = D-galactono-1,4-lactone + NADH.1 Publication
D-galactose + NADP+ = D-galactono-1,5-lactone + NADPH.2 Publications
An aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function.1 Publication

Enzyme regulationi

Inhibited by EDTA in vitro.1 Publication

Kineticsi

  1. KM=8.0 mM for D-glucose (in the presence of NAD+, at 70 degrees Celsius and pH 8)1 Publication
  2. KM=1.50 mM for D-glucose (in the presence of NAD+, at 70 degrees Celsius and pH 7.5)1 Publication
  3. KM=0.44 mM for D-glucose (in the presence of NADP+, at 70 degrees Celsius and pH 8)1 Publication
  4. KM=1.30 mM for D-glucose (in the presence of NADP+, at 70 degrees Celsius and pH 7.5)1 Publication
  5. KM=0.57 mM for D-galactose (in the presence of NAD+, at 70 degrees Celsius and pH 7.5)1 Publication
  6. KM=22 mM for D-galactose (in the presence of NADP+, at 70 degrees Celsius and pH 8)1 Publication
  7. KM=0.44 mM for D-galactose (in the presence of NADP+, at 70 degrees Celsius and pH 7.5)1 Publication
  8. KM=0.25 mM for D-xylose (in the presence of NAD+, at 70 degrees Celsius and pH 7.5)1 Publication
  9. KM=0.18 mM for D-xylose (in the presence of NADP+, at 70 degrees Celsius and pH 7.5)1 Publication
  10. KM=1.2 mM for NAD+ (at 70 degrees Celsius and pH 8)1 Publication
  11. KM=0.03 mM for NADP+ (at 70 degrees Celsius and pH 8)1 Publication
  1. Vmax=110 µmol/min/mg enzyme for the oxidation of D-glucose by NAD+ (at 70 degrees Celsius and pH 7.5)1 Publication
  2. Vmax=70 µmol/min/mg enzyme for the oxidation of D-glucose by NADP+ (at 70 degrees Celsius and pH 7.5)1 Publication
  3. Vmax=90 µmol/min/mg enzyme for the oxidation of D-galactose by NAD+ (at 70 degrees Celsius and pH 7.5)1 Publication
  4. Vmax=55 µmol/min/mg enzyme for the oxidation of D-galactose by NADP+ (at 70 degrees Celsius and pH 7.5)1 Publication
  5. Vmax=90 µmol/min/mg enzyme for the oxidation of D-xylose by NAD+ (at 70 degrees Celsius and pH 7.5)1 Publication
  6. Vmax=65 µmol/min/mg enzyme for the oxidation of D-xylose by NADP+ (at 70 degrees Celsius and pH 7.5)1 Publication

pH dependencei

Optimum pH is 9.1 Publication

Temperature dependencei

Optimum temperature is 77 degrees Celsius. At 37 degrees Celsius, shows about 20% activity as compared with the maximal value.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Zinc 1; catalytic1 Publication
Binding sitei41 – 411SubstrateUniRule annotation
Metal bindingi66 – 661Zinc 1; via tele nitrogen; catalytic1 Publication
Metal bindingi67 – 671Zinc 1; catalytic1 Publication
Binding sitei89 – 891Substrate1 Publication
Metal bindingi93 – 931Zinc 2; structural1 Publication
Metal bindingi96 – 961Zinc 2; structural1 Publication
Metal bindingi99 – 991Zinc 2; structural1 Publication
Metal bindingi107 – 1071Zinc 2; structural1 Publication
Binding sitei114 – 1141Substrate1 Publication
Metal bindingi150 – 1501Zinc 1; catalytic1 Publication
Binding sitei150 – 1501Substrate1 Publication
Binding sitei154 – 1541Substrate1 Publication
Binding sitei307 – 3071Substrate1 Publication
Binding sitei354 – 3541NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1924NADP1 Publication
Nucleotide bindingi211 – 2133NADP1 Publication
Nucleotide bindingi277 – 2793NADP1 Publication
Nucleotide bindingi305 – 3073NADP1 Publication

GO - Molecular functioni

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

GO - Biological processi

  • galactose catabolic process via D-galactonate Source: UniProtKB
  • non-phosphorylated glucose catabolic process Source: UniProtKB
  • protein tetramerization 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

BioCyciMetaCyc:MONOMER-4842.
BRENDAi1.1.1.359. 6163.
1.1.1.47. 6163.
SABIO-RKO93715.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose 1-dehydrogenaseUniRule annotation (EC:1.1.1.47UniRule annotation2 Publications)
Short name:
GDHUniRule annotation
Short name:
GlcDHUniRule annotation
Alternative name(s):
Aldose 1-dehydrogenase [NAD(P)(+)]1 Publication (EC:1.1.1.3592 Publications)
Galactose 1-dehydrogenase1 Publication (EC:1.1.1.1202 Publications, EC:1.1.1.481 Publication)
Gene namesi
Name:gdhImported
OrganismiSulfolobus solfataricus
Taxonomic identifieri2287 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411T → A: Large decrease in catalytic activity and substrate affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Glucose 1-dehydrogenasePRO_0000414839Add
BLAST

Interactioni

Subunit structurei

Homotetramer.3 Publications

Protein-protein interaction databases

STRINGi273057.SSO3003.

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Beta strandi14 – 174Combined sources
Helixi20 – 223Combined sources
Beta strandi27 – 3812Combined sources
Helixi40 – 467Combined sources
Beta strandi66 – 727Combined sources
Beta strandi84 – 874Combined sources
Beta strandi89 – 913Combined sources
Beta strandi94 – 963Combined sources
Helixi97 – 1004Combined sources
Helixi104 – 1063Combined sources
Beta strandi108 – 1103Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi125 – 1306Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1384Combined sources
Helixi140 – 1423Combined sources
Turni143 – 1453Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 16517Combined sources
Helixi166 – 1683Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi183 – 1886Combined sources
Helixi190 – 20314Combined sources
Beta strandi206 – 2138Combined sources
Helixi217 – 22610Combined sources
Beta strandi229 – 2324Combined sources
Helixi238 – 2447Combined sources
Beta strandi247 – 2526Combined sources
Helixi259 – 2646Combined sources
Helixi265 – 2673Combined sources
Beta strandi268 – 2769Combined sources
Beta strandi284 – 2885Combined sources
Helixi289 – 2979Combined sources
Beta strandi301 – 3044Combined sources
Helixi310 – 32617Combined sources
Helixi328 – 3314Combined sources
Beta strandi334 – 3407Combined sources
Helixi344 – 3529Combined sources
Beta strandi360 – 3645Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CD9X-ray1.80A/B1-366[»]
2CDAX-ray2.28A/B1-366[»]
2CDBX-ray1.60A/B/C/D1-366[»]
2CDCX-ray1.50A/B/C/D1-366[»]
ProteinModelPortaliO93715.
SMRiO93715. Positions 1-366.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO93715.

Family & Domainsi

Sequence similaritiesi

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01459. Archaea.
COG1063. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_02127. Glucose_DH. 1 hit.
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. 2 hits.
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.

O93715-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAIIVKPPN AGVQVKDVDE KKLDSYGKIK IRTIYNGICG TDREIVNGKL
60 70 80 90 100
TLSTLPKGKD FLVLGHEAIG VVEESYHGFS QGDLVMPVNR RGCGICRNCL
110 120 130 140 150
VGRPDFCETG EFGEAGIHKM DGFMREWWYD DPKYLVKIPK SIEDIGILAQ
160 170 180 190 200
PLADIEKSIE EILEVQKRVP VWTCDDGTLN CRKVLVVGTG PIGVLFTLLF
210 220 230 240 250
RTYGLEVWMA NRREPTEVEQ TVIEETKTNY YNSSNGYDKL KDSVGKFDVI
260 270 280 290 300
IDATGADVNI LGNVIPLLGR NGVLGLFGFS TSGSVPLDYK TLQEIVHTNK
310 320 330 340 350
TIIGLVNGQK PHFQQAVVHL ASWKTLYPKA AKMLITKTVS INDEKELLKV
360
LREKEHGEIK IRILWE
Length:366
Mass (Da):40,891
Last modified:May 1, 1999 - v1
Checksum:i59D4AC33B447D3EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012093 Genomic DNA. Translation: CAA09918.1.
PIRiT44937.
RefSeqiWP_009992653.1. NZ_LT549890.1.

Genome annotation databases

GeneIDi27429263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012093 Genomic DNA. Translation: CAA09918.1.
PIRiT44937.
RefSeqiWP_009992653.1. NZ_LT549890.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CD9X-ray1.80A/B1-366[»]
2CDAX-ray2.28A/B1-366[»]
2CDBX-ray1.60A/B/C/D1-366[»]
2CDCX-ray1.50A/B/C/D1-366[»]
ProteinModelPortaliO93715.
SMRiO93715. Positions 1-366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO3003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi27429263.

Phylogenomic databases

eggNOGiarCOG01459. Archaea.
COG1063. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-4842.
BRENDAi1.1.1.359. 6163.
1.1.1.47. 6163.
SABIO-RKO93715.

Miscellaneous databases

EvolutionaryTraceiO93715.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_02127. Glucose_DH. 1 hit.
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. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF16912. Glu_dehyd_C. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLCDH_SULSF
AccessioniPrimary (citable) accession number: O93715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 101 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.