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Protein

Glucose 1-dehydrogenase 4

Gene

gdhIV

Organism
Bacillus megaterium
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Beta-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 acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 3525NADBy similarityAdd
BLAST

GO - Molecular functioni

  1. glucose 1-dehydrogenase [NAD(P)] activity Source: UniProtKB-EC
  2. identical protein binding Source: IntAct
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.1.1.47. 656.
SABIO-RKP39485.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose 1-dehydrogenase 4 (EC:1.1.1.47)
Alternative name(s):
GLCDH-IV
Gene namesi
Name:gdhIV
OrganismiBacillus megaterium
Taxonomic identifieri1404 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Glucose 1-dehydrogenase 4PRO_0000054612Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-7977646,EBI-7977646

Protein-protein interaction databases

MINTiMINT-8386740.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi9 – 124Combined sources
Turni13 – 164Combined sources
Helixi18 – 2912Combined sources
Beta strandi33 – 408Combined sources
Helixi42 – 5514Combined 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
Beta strandi190 – 1934Combined sources
Helixi194 – 1963Combined sources
Helixi197 – 2015Combined sources
Helixi203 – 2119Combined sources
Helixi221 – 23212Combined sources
Helixi234 – 2363Combined sources
Beta strandi243 – 2475Combined sources
Helixi250 – 2523Combined sources
Helixi254 – 2563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP39485.
SMRiP39485. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39485-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYTDLKDKVV VITGGSTGLG RAMAVRFGQE EAKVVINYYN NEEEALDAKK
60 70 80 90 100
EVEEAGGQAI IVQGDVTKEE DVVNLVQTAI KEFGTLDVMI NNAGVENPVP
110 120 130 140 150
SHELSLDNWN KVIDTNLTGA FLGSREAIKY FVENDIKGNV INMSSVHEMI
160 170 180 190 200
PWPLFVHYAA SKGGMKLMTE TLALEYAPKG IRVNNIGPGA MNTPINAEKF
210 220 230 240 250
ADPVQRADVE SMIPMGYIGK PEEVAAVAAF LASSQASYVT GITLFADGGM
260
TKYPSFQAGR G
Length:261
Mass (Da):28,157
Last modified:February 1, 1995 - v1
Checksum:i6FBEC9397BCF417C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10626 Genomic DNA. Translation: BAA01476.1.
PIRiI40225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10626 Genomic DNA. Translation: BAA01476.1.
PIRiI40225.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP39485.
SMRiP39485. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8386740.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.1.47. 656.
SABIO-RKP39485.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiDHG4_BACME
AccessioniPrimary (citable) accession number: P39485
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 1, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure

Documents

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

External Data

Dasty 3

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 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.