DB code: S00324

RLCP classification 9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.47
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P40288 Glucose 1-dehydrogenase
EC 1.1.1.47
PF00106 (adh_short)
[Graphical View]

KEGG enzyme name
glucose 1-dehydrogenase
D-glucose dehydrogenase (NAD(P)+)
hexose phosphate dehydrogenase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P40288 DHG_BACME Beta-D-glucose + NAD(P)(+) = D-glucono-1,5- lactone + NAD(P)H. Homotetramer.

KEGG Pathways
Map code Pathways E.C.
MAP00030 Pentose phosphate pathway

Compound table
Substrates Products Intermediates
KEGG-id C00221 C00003 C00006 C00198 C00004 C00005 C00080
E.C.
Compound beta-D-Glucose NAD+ NADP+ D-Glucono-1,5-lactone NADH NADPH H+
Type carbohydrate amide group,amine group,nucleotide amide group,amine group,nucleotide carbohydrate amide group,amine group,nucleotide amide group,amine group,nucleotide others
ChEBI 15903
 15903
 		15846
 15846
 		18009
 18009
 		16217
 16217
 		16908
 16908
 		16474
 16474
 		15378
 15378
PubChem 64689
 64689
 		5893
 5893
 		5886
 5886
 		7027
 7027
 		439153
 439153
 		5884
 5884
 		1038
 1038
1g6kA Unbound Bound:NAD Unbound Unbound Unbound Unbound
1g6kB Unbound Bound:NAD Unbound Unbound Unbound Unbound
1g6kE Unbound Bound:NAD Unbound Unbound Unbound Unbound
1g6kF Unbound Bound:NAD Unbound Unbound Unbound Unbound
1gcoA Unbound Bound:NAD Unbound Unbound Unbound Unbound
1gcoB Unbound Bound:NAD Unbound Unbound Unbound Unbound
1gcoE Unbound Bound:NAD Unbound Unbound Unbound Unbound
1gcoF Unbound Bound:NAD Unbound Unbound Unbound Unbound
1geeA Unbound Bound:NAD Unbound Unbound Unbound Unbound
1geeB Unbound Bound:NAD Unbound Unbound Unbound Unbound
1geeE Unbound Bound:NAD Unbound Unbound Unbound Unbound
1geeF Unbound Bound:NAD Unbound Unbound Unbound Unbound
1rwbA Unbound Bound:NAD Unbound Unbound Unbound Unbound
1rwbB Unbound Bound:NAD Unbound Unbound Unbound Unbound
1rwbE Unbound Bound:NAD Unbound Unbound Unbound Unbound
1rwbF Unbound Bound:NAD Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P40288

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1g6kA SER 145;TYR 158;LYS 162 mutant E96A
1g6kB SER 145;TYR 158;LYS 162 mutant E96A
1g6kE SER 145;TYR 158;LYS 162 mutant E96A
1g6kF SER 145;TYR 158;LYS 162 mutant E96A
1gcoA SER 145;TYR 158;LYS 162
1gcoB SER 145;TYR 158;LYS 162
1gcoE SER 145;TYR 158;LYS 162
1gcoF SER 145;TYR 158;LYS 162
1geeA SER 145;TYR 158;LYS 162 mutant Q252L
1geeB SER 145;TYR 158;LYS 162 mutant Q252L
1geeE SER 145;TYR 158;LYS 162 mutant Q252L
1geeF SER 145;TYR 158;LYS 162 mutant Q252L
1rwbA SER 145;TYR 158;LYS 162 mutant E170K, Q252L
1rwbB SER 145;TYR 158;LYS 162 mutant E170K, Q252L
1rwbE SER 145;TYR 158;LYS 162 mutant E170K, Q252L
1rwbF SER 145;TYR 158;LYS 162 mutant E170K, Q252L

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
p.308

References
[1]
Resource
Comments
Medline ID
PubMed ID 3113945
Journal Eur J Biochem
Year 1987
Volume 167
Pages 123-4
Authors Pal GP, Jany KD, Saenger W
Title Crystallization of and X-ray investigations on glucose dehydrogenase from Bacillus megaterium.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2803257
Journal Biochem J
Year 1989
Volume 261
Pages 973-7
Authors Smith LD, Budgen N, Bungard SJ, Danson MJ, Hough DW
Title Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 2503396
Journal FEBS Lett
Year 1989
Volume 253
Pages 113-6
Authors Nagao T, Makino Y, Yamamoto K, Urabe I, Okada H
Title Stability-increasing mutants of glucose dehydrogenase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 2495285
Journal J Biol Chem
Year 1989
Volume 264
Pages 6381-5
Authors Makino Y, Negoro S, Urabe I, Okada H
Title Stability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1915348
Journal Eur J Biochem
Year 1991
Volume 200
Pages 759-66
Authors Yomo T, Urabe I, Okada H
Title Preparation and kinetic properties of 5-ethylphenazine-glucose-dehydrogenase-NAD+ conjugate, a semisynthetic glucose oxidase.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD.
Medline ID
PubMed ID 11173533
Journal J Biochem (Tokyo)
Year 2001
Volume 129
Pages 303-12
Authors Yamamoto K, Kurisu G, Kusunoki M, Tabata S, Urabe I, Osaki S
Title Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 A resolution.
Related PDB 1gco
Related UniProtKB P40288
[7]
Resource
Comments
Medline ID
PubMed ID 12743762
Journal Appl Microbiol Biotechnol
Year 2003
Volume 61
Pages 329-35
Authors Baik SH, Ide T, Yoshida H, Kagami O, Harayama S
Title Significantly enhanced stability of glucose dehydrogenase by directed evolution.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 15933031
Journal Appl Environ Microbiol
Year 2005
Volume 71
Pages 3285-93
Authors Baik SH, Michel F, Aghajari N, Haser R, Harayama S
Title Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state.
Related PDB 1rwb
Related UniProtKB

Comments
There are several types of glucose dehydrogenase such as PQQ-dependent GDH (E.C. 1.1.5.2), "short" NAD(P)-dependent GDH (E.C. 1.1.1.47), "long" NAD(P)-dependent GDH.
This enzyme belongs to "short" NAD(P)-dependent GDH (E.C. 1.1.1.47).
This enzyme has got the same catalytic triad (Ser/Tyr/Lys) as those of Drosophia alcohol dehydrogenase (E.C. 1.1.1.1; S00319 in EzCatDB) and tetrahydroxynaphthalene reductase (E.C. 1.1.1.252; S00336 in EzCatDB). Thus, it must have a similar catalytic reaction mechanism to those enzymes.

Created Updated
2005-01-20 2011-06-23