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Reviewed, UniProtKB/Swiss-Prot P07999 (DHGB_BACME)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glucose 1-dehydrogenase B
    EC=1.1.1.47
Gene names
Name: gdhB
OrganismBacillus megaterium
Taxonomic identifier1404 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 processSporulation
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

sporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

glucose 1-dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 262262Glucose 1-dehydrogenase B
PRO_0000054614

Regions

Nucleotide binding11 – 3525NADP By similarity

Sites

Active site1601Proton acceptor By similarity
Binding site1461Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P07999-1 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: C9281328D634E789

FASTA26228,347
        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 

« Hide

References

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

Cross-references

Sequence databases

PIRA23260.
S01227.
S02299.

3D structure databases

HSSPHSSP built from PDB template 1GCO based on UniProtKB P40288.
SMRP07999. Positions 1-262.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.47. 325.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHGB_BACME
AccessionPrimary (citable) accession number: P07999
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1989
Last modified: June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents