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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)DescriptionActionsGraphical viewLength
Metal bindingi39Zinc 1; catalytic1 Publication1
Binding sitei41SubstrateUniRule annotation1
Metal bindingi66Zinc 1; via tele nitrogen; catalytic1 Publication1
Metal bindingi67Zinc 1; catalytic1 Publication1
Binding sitei89Substrate1 Publication1
Metal bindingi93Zinc 2; structural1 Publication1
Metal bindingi96Zinc 2; structural1 Publication1
Metal bindingi99Zinc 2; structural1 Publication1
Metal bindingi107Zinc 2; structural1 Publication1
Binding sitei114Substrate1 Publication1
Metal bindingi150Zinc 1; catalytic1 Publication1
Binding sitei150Substrate1 Publication1
Binding sitei154Substrate1 Publication1
Binding sitei307Substrate1 Publication1
Binding sitei354NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi189 – 192NADP1 Publication4
Nucleotide bindingi211 – 213NADP1 Publication3
Nucleotide bindingi277 – 279NADP1 Publication3
Nucleotide bindingi305 – 307NADP1 Publication3

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)DescriptionActionsGraphical viewLength
Mutagenesisi41T → A: Large decrease in catalytic activity and substrate affinity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004148391 – 366Glucose 1-dehydrogenaseAdd BLAST366

Interactioni

Subunit structurei

Homotetramer.3 Publications

Protein-protein interaction databases

STRINGi273057.SSO3003.

Structurei

Secondary structure

1366
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Beta strandi14 – 17Combined sources4
Helixi20 – 22Combined sources3
Beta strandi27 – 38Combined sources12
Helixi40 – 46Combined sources7
Beta strandi66 – 72Combined sources7
Beta strandi84 – 87Combined sources4
Beta strandi89 – 91Combined sources3
Beta strandi94 – 96Combined sources3
Helixi97 – 100Combined sources4
Helixi104 – 106Combined sources3
Beta strandi108 – 110Combined sources3
Turni115 – 117Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi125 – 130Combined sources6
Helixi132 – 134Combined sources3
Beta strandi135 – 138Combined sources4
Helixi140 – 142Combined sources3
Turni143 – 145Combined sources3
Helixi146 – 148Combined sources3
Helixi149 – 165Combined sources17
Helixi166 – 168Combined sources3
Beta strandi177 – 179Combined sources3
Beta strandi183 – 188Combined sources6
Helixi190 – 203Combined sources14
Beta strandi206 – 213Combined sources8
Helixi217 – 226Combined sources10
Beta strandi229 – 232Combined sources4
Helixi238 – 244Combined sources7
Beta strandi247 – 252Combined sources6
Helixi259 – 264Combined sources6
Helixi265 – 267Combined sources3
Beta strandi268 – 276Combined sources9
Beta strandi284 – 288Combined sources5
Helixi289 – 297Combined sources9
Beta strandi301 – 304Combined sources4
Helixi310 – 326Combined sources17
Helixi328 – 331Combined sources4
Beta strandi334 – 340Combined sources7
Helixi344 – 352Combined sources9
Beta strandi360 – 364Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
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: November 2, 2016
This is version 103 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.