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P39485 (DHG4_BACME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose 1-dehydrogenase 4

EC=1.1.1.47
Alternative name(s):
GLCDH-IV
Gene names
Name:gdhIV
OrganismBacillus megaterium
Taxonomic identifier1404 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
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.

Miscellaneous

Prefers NAD to NADP; 2M NaCl enhances its pH and thermostability.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Molecular_functionglucose 1-dehydrogenase [NAD(P)] activity

Inferred from electronic annotation. Source: UniProtKB-EC

identical protein binding

Inferred from physical interaction PubMed 22804868. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-7977646,EBI-7977646

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Glucose 1-dehydrogenase 4
PRO_0000054612

Regions

Nucleotide binding11 – 3525NAD By similarity

Sites

Active site1581Proton acceptor By similarity
Binding site1451Substrate By similarity

Secondary structure

................................................. 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39485 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 6FBEC9397BCF417C

FASTA26128,157
        10         20         30         40         50         60 
MYTDLKDKVV VITGGSTGLG RAMAVRFGQE EAKVVINYYN NEEEALDAKK EVEEAGGQAI 

        70         80         90        100        110        120 
IVQGDVTKEE DVVNLVQTAI KEFGTLDVMI NNAGVENPVP SHELSLDNWN KVIDTNLTGA 

       130        140        150        160        170        180 
FLGSREAIKY FVENDIKGNV INMSSVHEMI PWPLFVHYAA SKGGMKLMTE TLALEYAPKG 

       190        200        210        220        230        240 
IRVNNIGPGA MNTPINAEKF ADPVQRADVE SMIPMGYIGK PEEVAAVAAF LASSQASYVT 

       250        260 
GITLFADGGM TKYPSFQAGR G 

« Hide

References

[1]"Cloning, nucleotide sequences, and enzymatic properties of glucose dehydrogenase isozymes from Bacillus megaterium IAM1030."
Nagao T., Mitamura T., Wang X.H., Negoro S., Yomo T., Urabe I., Okada H.
J. Bacteriol. 174:5013-5020(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IAM 1030.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10626 Genomic DNA. Translation: BAA01476.1.
PIRI40225.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AUSX-ray2.00A/B1-261[»]
3AUTX-ray2.00A/B1-261[»]
3AUUX-ray2.00A/B1-261[»]
3AY6X-ray2.10A/B/C/D1-261[»]
3AY7X-ray1.90A/B1-261[»]
ProteinModelPortalP39485.
SMRP39485. Positions 1-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-8386740.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP39485.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHG4_BACME
AccessionPrimary (citable) accession number: P39485
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references