Reviewed, UniProtKB/Swiss-Prot P40288 (DHG_BACME)

Names and origin

Protein names	Recommended name:     Glucose 1-dehydrogenase     EC=1.1.1.47
Organism	Bacillus megaterium
Taxonomic identifier	1404 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Beta-D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H.
Subunit structure	Homotetramer.
Developmental stage	Expressed during sporulation.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Sporulation
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro glucose 1-dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Glucose 1-dehydrogenase

PRO_0000054615

Regions

Nucleotide binding

11 – 35

25

NADP

Sites

Active site

158

1

Proton acceptor

Binding site

145

1

Substrate By similarity

Experimental info

Mutagenesis

96

1

E → A, G or K: Heat stable

Mutagenesis

108

1

D → N: Heat stable

Mutagenesis

112

1

V → A: Heat stable

Mutagenesis

133

1

E → K: Heat stable

Mutagenesis

183

1

V → I: Heat stable

Mutagenesis

194

1

P → Q: Heat stable

Mutagenesis

210

1

E → K: Heat stable

Mutagenesis

217

1

Y → H: Heat stable

Mutagenesis

252

1

Q → L: Heat stable

Mutagenesis

253

1

Y → C: Heat stable

Mutagenesis

258

1

A → G: Heat stable

Secondary structure

1

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261

Helix Strand Turn

Details...

Helix

3 – 5

3

Beta strand

9 – 12

4

Helix

18 – 29

12

Beta strand

33 – 40

8

Helix

42 – 54

13

Beta strand

58 – 63

6

Helix

69 – 83

15

Beta strand

88 – 91

4

Helix

101 – 103

3

Helix

106 – 116

11

Helix

118 – 133

16

Beta strand

139 – 143

5

Helix

146 – 148

3

Helix

156 – 176

21

Helix

177 – 179

3

Beta strand

182 – 188

7

Helix

194 – 196

3

Turn

197 – 201

5

Helix

203 – 210

8

Helix

221 – 232

12

Helix

234 – 236

3

Beta strand

243 – 247

5

Helix

250 – 252

3

Helix

254 – 259

6

Sequences

	Sequence		Length	Mass (Da)
	P40288-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: C23AC98D304EEB2F	FASTA	261	28,085
	10 20 30 40 50 60 MYKDLEGKVV VITGSSTGLG KSMAIRFATE KAKVVVNYRS KEDEANSVLE EIKKVGGEAI 70 80 90 100 110 120 AVKGDVTVES DVINLVQSAI KEFGKLDVMI NNAGLENPVS SHEMSLSDWN KVIDTNLTGA 130 140 150 160 170 180 FLGSREAIKY FVENDIKGTV INMSSVHEKI PWPLFVHYAA SKGGMKLMTE TLALEYAPKG 190 200 210 220 230 240 IRVNNIGPGA INTPINAEKF ADPEQRADVE SMIPMGYIGE PEEIAAVAAW LASSEASYVT 250 260 GITLFADGGM TQYPSFQAGR G

References

[1]	"Stability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3." Makino Y., Negoro S., Urabe I., Okada H. J. Biol. Chem. 264:6381-6385(1989) [PubMed: 2495285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-29, MUTAGENESIS. Strain: IWG3.
[2]	Urabe I. Submitted (MAR-1989) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 A resolution." Yamamoto K., Kurisu G., Kusunoki M., Tabata S., Urabe I., Osaki S. J. Biochem. 129:303-312(2001) [PubMed: 11173533] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J04805 Genomic DNA. Translation: AAA22475.1.

PIR

A33528.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G6K	X-ray	2.00	A/B/E/F	1-261	[»]
1GCO	X-ray	1.70	A/B/E/F	1-261	[»]
1GEE	X-ray	1.60	A/B/E/F	1-261	[»]
1RWB	X-ray	2.00	A/B/E/F	1-261	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR002198. DHase_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DHG_BACME

Accession

Primary (citable) accession number: P40288

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)