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Protein

Glucose 1-dehydrogenase

Gene
N/A
Organism
Bacillus megaterium
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei145 – 1451SubstrateBy similarity
Active sitei158 – 1581Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 3525NADP1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Sporulation

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.47. 656.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose 1-dehydrogenase (EC:1.1.1.47)
OrganismiBacillus megaterium
Taxonomic identifieri1404 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi96 – 961E → A, G or K: Heat stable. 1 Publication
Mutagenesisi108 – 1081D → N: Heat stable. 1 Publication
Mutagenesisi112 – 1121V → A: Heat stable. 1 Publication
Mutagenesisi133 – 1331E → K: Heat stable. 1 Publication
Mutagenesisi183 – 1831V → I: Heat stable. 1 Publication
Mutagenesisi194 – 1941P → Q: Heat stable. 1 Publication
Mutagenesisi210 – 2101E → K: Heat stable. 1 Publication
Mutagenesisi217 – 2171Y → H: Heat stable. 1 Publication
Mutagenesisi252 – 2521Q → L: Heat stable. 1 Publication
Mutagenesisi253 – 2531Y → C: Heat stable. 1 Publication
Mutagenesisi258 – 2581A → G: Heat stable. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Glucose 1-dehydrogenasePRO_0000054615Add
BLAST

Expressioni

Developmental stagei

Expressed during sporulation.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi545693.BMQ_0838.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi9 – 124Combined sources
Helixi18 – 2912Combined sources
Beta strandi33 – 408Combined sources
Helixi42 – 5413Combined sources
Beta strandi58 – 636Combined sources
Helixi69 – 8315Combined sources
Beta strandi88 – 914Combined sources
Helixi101 – 1033Combined sources
Helixi106 – 11611Combined sources
Helixi118 – 13316Combined sources
Beta strandi139 – 1435Combined sources
Helixi146 – 1483Combined sources
Helixi156 – 17621Combined sources
Helixi177 – 1793Combined sources
Beta strandi182 – 1887Combined sources
Helixi194 – 1963Combined sources
Helixi197 – 2015Combined sources
Helixi203 – 2108Combined sources
Helixi221 – 23212Combined sources
Helixi234 – 2363Combined sources
Beta strandi243 – 2475Combined sources
Helixi250 – 2523Combined sources
Helixi254 – 2596Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G6KX-ray2.00A/B/E/F1-261[»]
1GCOX-ray1.70A/B/E/F1-261[»]
1GEEX-ray1.60A/B/E/F1-261[»]
1RWBX-ray2.00A/B/E/F1-261[»]
ProteinModelPortaliP40288.
SMRiP40288. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40288.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107EXU. Bacteria.
COG1028. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 3 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40288-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYKDLEGKVV VITGSSTGLG KSMAIRFATE KAKVVVNYRS KEDEANSVLE
60 70 80 90 100
EIKKVGGEAI AVKGDVTVES DVINLVQSAI KEFGKLDVMI NNAGLENPVS
110 120 130 140 150
SHEMSLSDWN KVIDTNLTGA FLGSREAIKY FVENDIKGTV INMSSVHEKI
160 170 180 190 200
PWPLFVHYAA SKGGMKLMTE TLALEYAPKG IRVNNIGPGA INTPINAEKF
210 220 230 240 250
ADPEQRADVE SMIPMGYIGE PEEIAAVAAW LASSEASYVT GITLFADGGM
260
TQYPSFQAGR G
Length:261
Mass (Da):28,085
Last modified:February 1, 1995 - v1
Checksum:iC23AC98D304EEB2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04805 Genomic DNA. Translation: AAA22475.1.
PIRiA33528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04805 Genomic DNA. Translation: AAA22475.1.
PIRiA33528.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G6KX-ray2.00A/B/E/F1-261[»]
1GCOX-ray1.70A/B/E/F1-261[»]
1GEEX-ray1.60A/B/E/F1-261[»]
1RWBX-ray2.00A/B/E/F1-261[»]
ProteinModelPortaliP40288.
SMRiP40288. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi545693.BMQ_0838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107EXU. Bacteria.
COG1028. LUCA.

Enzyme and pathway databases

BRENDAi1.1.1.47. 656.

Miscellaneous databases

EvolutionaryTraceiP40288.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 3 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD.

Entry informationi

Entry nameiDHG_BACME
AccessioniPrimary (citable) accession number: P40288
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.