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Protein

Glucose 1-dehydrogenase

Gene

gdh

Organism
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD(P)+-dependent oxidation of D-glucose to D-gluconate. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-xylose, D-galactose, and D-fucose, to the corresponding glyconate. Can utilize both NAD+ and NADP+ as electron acceptor, with a preference for NADP+. Physiologically, seems to be involved in the degradation of glucose through a modified Entner-Doudoroff pathway.2 Publications

Catalytic activityi

D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function, according to Ref.4. However, the crystal structures show a single zinc ion, the catalytic one.1 Publication

Enzyme regulationi

Activated by molar concentrations of KCl or NaCl. Inhibited by EDTA in vitro.2 Publications

Kineticsi

  1. KM=1.2 mM for NAD+ (at 40 degrees Celsius and pH 8.8)1 Publication
  2. KM=0.024 mM for NADP+ (at 40 degrees Celsius and pH 8.8)1 Publication
  3. KM=3.9 mM for beta-D-glucose (in the presence of NADP+, at 40 degrees Celsius and pH 8.8)1 Publication
  4. KM=4.7 mM for D-glucose (at 40 degrees Celsius and pH 8.8)1 Publication
  5. KM=6.9 mM for D-xylose (at 40 degrees Celsius and pH 8.8)1 Publication
  1. Vmax=93 µmol/min/mg enzyme for the oxidation of D-glucose by NADP+ (at 40 degrees Celsius and pH 8.8)1 Publication
  2. Vmax=80 µmol/min/mg enzyme for the oxidation of D-xylose by NADP+ (at 40 degrees Celsius and pH 8.8)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi38Zinc; catalytic2 Publications1
Binding sitei40Substrate1 Publication1
Binding sitei49Substrate1 Publication1
Metal bindingi63Zinc; via tele nitrogen; catalytic2 Publications1
Metal bindingi64Zinc; catalytic2 Publications1
Binding sitei114Substrate1 Publication1
Metal bindingi150Zinc; catalytic2 Publications1
Binding sitei150Substrate1 Publication1
Binding sitei228NADP2 Publications1
Binding sitei303Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi181 – 184NADP2 Publications4
Nucleotide bindingi207 – 208NADP2 Publications2
Nucleotide bindingi272 – 274NADP2 Publications3
Nucleotide bindingi301 – 303NADP2 Publications3

GO - Molecular functioni

  • glucose 1-dehydrogenase [NAD(P)] activity Source: UniProtKB
  • glucose binding Source: UniProtKB
  • NAD+ binding Source: UniProtKB
  • NADP+ binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • non-phosphorylated glucose catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Metal-binding, NAD, NADP, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-4902.
BRENDAi1.1.1.113. 2566.
1.1.1.119. 2566.
1.1.1.175. 2566.
1.1.1.47. 2566.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose 1-dehydrogenaseUniRule annotation (EC:1.1.1.47UniRule annotation2 Publications)
Short name:
GDHUniRule annotation
Short name:
GlcDHUniRule annotation
Gene namesi
Name:gdhImported
Ordered Locus Names:HFX_1090
OrganismiHaloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Taxonomic identifieri523841 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHaloferacalesHaloferacaceaeHaloferax
Proteomesi
  • UP000006469 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi172D → K: Does not affect the kinetic parameters but results in a slightly less halotolerant protein. 1 Publication1
Mutagenesisi216D → K: Does not affect the kinetic parameters but results in a slightly less halotolerant protein. 1 Publication1
Mutagenesisi344D → K: Does not affect the kinetic parameters and has no effect on the salt activity profile. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004148321 – 357Glucose 1-dehydrogenaseAdd BLAST357

Expressioni

Inductioni

Up-regulated by glucose.1 Publication

Interactioni

Subunit structurei

Homodimer.3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-48672N.

Structurei

Secondary structure

1357
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Beta strandi14 – 17Combined sources4
Beta strandi27 – 37Combined sources11
Helixi39 – 46Combined sources8
Beta strandi47 – 49Combined sources3
Beta strandi57 – 60Combined sources4
Beta strandi63 – 71Combined sources9
Beta strandi82 – 85Combined sources4
Beta strandi87 – 89Combined sources3
Helixi97 – 100Combined sources4
Helixi104 – 106Combined sources3
Turni115 – 117Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi125 – 131Combined sources7
Helixi132 – 134Combined sources3
Beta strandi135 – 137Combined sources3
Helixi140 – 142Combined sources3
Helixi146 – 148Combined sources3
Helixi149 – 164Combined sources16
Turni165 – 168Combined sources4
Beta strandi175 – 179Combined sources5
Helixi183 – 194Combined sources12
Beta strandi201 – 206Combined sources6
Helixi213 – 220Combined sources8
Beta strandi224 – 227Combined sources4
Turni228 – 230Combined sources3
Helixi233 – 235Combined sources3
Helixi236 – 239Combined sources4
Beta strandi243 – 248Combined sources6
Helixi253 – 262Combined sources10
Beta strandi263 – 271Combined sources9
Helixi284 – 293Combined sources10
Beta strandi297 – 300Combined sources4
Helixi306 – 318Combined sources13
Helixi321 – 327Combined sources7
Beta strandi328 – 333Combined sources6
Helixi334 – 341Combined sources8
Beta strandi349 – 353Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B5VX-ray2.00A1-357[»]
2B5WX-ray1.60A1-357[»]
2VWGX-ray2.00A1-357[»]
2VWHX-ray2.03A1-357[»]
2VWPX-ray2.01A1-357[»]
2VWQX-ray2.10A1-357[»]
ProteinModelPortaliQ977U7.
SMRiQ977U7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ977U7.

Family & Domainsi

Sequence similaritiesi

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.UniRule annotation

Phylogenomic databases

OMAiMVLHNKA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_02127. Glucose_DH. 1 hit.
InterProiIPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR026583. Glc_1-DH.
IPR031640. Glu_dehyd_C.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF16912. Glu_dehyd_C. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q977U7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAIAVKRGE DRPVVIEKPR PEPESGEALV RTLRVGVDGT DHEVIAGGHG
60 70 80 90 100
GFPEGEDHLV LGHEAVGVVV DPNDTELEEG DIVVPTVRRP PASGTNEYFE
110 120 130 140 150
RDQPDMAPDG MYFERGIVGA HGYMSEFFTS PEKYLVRIPR SQAELGFLIE
160 170 180 190 200
PISITEKALE HAYASRSAFD WDPSSAFVLG NGSLGLLTLA MLKVDDKGYE
210 220 230 240 250
NLYCLGRRDR PDPTIDIIEE LDATYVDSRQ TPVEDVPDVY EQMDFIYEAT
260 270 280 290 300
GFPKHAIQSV QALAPNGVGA LLGVPSDWAF EVDAGAFHRE MVLHNKALVG
310 320 330 340 350
SVNSHVEHFE AATVTFTKLP KWFLEDLVTG VHPLSEFEAA FDDDDTTIKT

AIEFSTV
Length:357
Mass (Da):39,242
Last modified:December 1, 2001 - v1
Checksum:iE19ABC275A31BCBA
GO

Mass spectrometryi

Molecular mass is 39248±4 Da from positions 1 - 303. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ251111 Genomic DNA. Translation: CAC42505.1.
CP001868 Genomic DNA. Translation: AFK18806.1.
PIRiS66213.
RefSeqiWP_004572583.1. NZ_CP007551.1.

Genome annotation databases

EnsemblBacteriaiAFK18806; AFK18806; HFX_1090.
GeneIDi13027256.
KEGGihme:HFX_1090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ251111 Genomic DNA. Translation: CAC42505.1.
CP001868 Genomic DNA. Translation: AFK18806.1.
PIRiS66213.
RefSeqiWP_004572583.1. NZ_CP007551.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B5VX-ray2.00A1-357[»]
2B5WX-ray1.60A1-357[»]
2VWGX-ray2.00A1-357[»]
2VWHX-ray2.03A1-357[»]
2VWPX-ray2.01A1-357[»]
2VWQX-ray2.10A1-357[»]
ProteinModelPortaliQ977U7.
SMRiQ977U7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48672N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFK18806; AFK18806; HFX_1090.
GeneIDi13027256.
KEGGihme:HFX_1090.

Phylogenomic databases

OMAiMVLHNKA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-4902.
BRENDAi1.1.1.113. 2566.
1.1.1.119. 2566.
1.1.1.175. 2566.
1.1.1.47. 2566.

Miscellaneous databases

EvolutionaryTraceiQ977U7.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_02127. Glucose_DH. 1 hit.
InterProiIPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR026583. Glc_1-DH.
IPR031640. Glu_dehyd_C.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF16912. Glu_dehyd_C. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLCDH_HALMT
AccessioniPrimary (citable) accession number: Q977U7
Secondary accession number(s): I3R3J6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction follows an ordered Bi-Bi kinetic mechanism, involving an ordered binding of NADP+ and D-glucose, followed by an ordered released of gluconolactone and NADPH.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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.