[1]	PROTEIN SEQUENCE. DOI=10.1016/0014-5793(84)80003-4; PubMed=6420184 [NCBI, ExPASy, EBI, Israel, Japan] Jany K.-D., Ulmer W., Froschle M., Pfleiderer G.; "Complete amino acid sequence of glucose dehydrogenase from Bacillus megaterium."; FEBS Lett. 165:6-10(1984).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52, AND SEQUENCE REVISION TO 207 AND 258. STRAIN=M1286; PubMed=3134196 [NCBI, ExPASy, EBI, Israel, Japan] Heilmann H.J., Maegert H.-J., Gassen H.G.; "Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coli."; Eur. J. Biochem. 174:485-490(1988).
[3]	PROTEIN SEQUENCE OF 27-204. PubMed=6413208 [NCBI, ExPASy, EBI, Israel, Japan] Ulmer W., Froschle M., Jany K.-D.; "Evidence for an essential histidine residue in glucose dehydrogenase from Bacillus megaterium and sequence analysis of the peptides labeled with bromoacetyl pyridine."; Eur. J. Biochem. 136:183-194(1983).
[4]	PROTEIN SEQUENCE OF 218-262. PubMed=6432532 [NCBI, ExPASy, EBI, Israel, Japan] Froschle M., Ulmer W., Jany K.-D.; "Tyrosine modification of glucose dehydrogenase from Bacillus megaterium. Effect of tetranitromethane on the enzyme in the tetrameric and monomeric state."; Eur. J. Biochem. 142:533-540(1984).

Comments

CATALYTIC ACTIVITY: Beta-D-glucose + NAD(P)⁺ = D-glucono-1,5-lactone + NAD(P)H.
SUBUNIT: Homotetramer.
DEVELOPMENTAL STAGE: Expressed during sporulation.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A23260; A23260.
S01227; S01227.
S02299; S02299.

3D structure databases

HSSP

P40288; 1GCO. [HSSP ENTRY / PDB]

SMR

P07999; 1-262.

ModBase

P07999.

Ontologies

GO:0047936;	Molecular function: glucose 1-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0030435;	Biological process: sporulation resulting in formation of a cellular spore (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; NADP; Oxidoreductase; Sporulation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 262`	`262`	`Glucose 1-dehydrogenase B.`	`PRO_0000054614`
`NP_BIND`	`11 35`	`25`	`NADP (By similarity).`
`ACT_SITE`	`160 160`		`Proton acceptor (By similarity).`
`BINDING`	`146 146`		`Substrate (By similarity).`

Sequence information

Length: 262 AA [This is the length of the unprocessed precursor]

Molecular weight: 28347 Da [This is the MW of the unprocessed precursor]

CRC64: C9281328D634E789 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYKDLEGKVV VITGSSTGLG KSMAIRFATE KAKVVVNYRS KEDEANSVLE EEIKKVGGEA 

        70         80         90        100        110        120 
IAVKGDVTVE SDVINLVQSA IKEFGKLDVM INNAGMENPV SSHEMSLSDW NKVIDTNLTG 

       130        140        150        160        170        180 
AFLGSREAIK YFVENDIKGT VINMSSVHEW KIPWPLFVHY AASKGGMKLM TETLALEYAP 

       190        200        210        220        230        240 
KGIRVNNIGP GAINTPINAE KFADPEQRAD VESMIPMGYI GEPEEIAAVA WLASSEASYV 

       250        260 
TGITLFADGG MTQYPSFQAG RG

P07999 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools