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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi38 – 381Zinc; catalytic2 Publications
Binding sitei40 – 401Substrate1 Publication
Binding sitei49 – 491Substrate1 Publication
Metal bindingi63 – 631Zinc; via tele nitrogen; catalytic2 Publications
Metal bindingi64 – 641Zinc; catalytic2 Publications
Binding sitei114 – 1141Substrate1 Publication
Metal bindingi150 – 1501Zinc; catalytic2 Publications
Binding sitei150 – 1501Substrate1 Publication
Binding sitei228 – 2281NADP2 Publications
Binding sitei303 – 3031Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1844NADP2 Publications
Nucleotide bindingi207 – 2082NADP2 Publications
Nucleotide bindingi272 – 2743NADP2 Publications
Nucleotide bindingi301 – 3033NADP2 Publications

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

BioCyciHMED523841:GLDU-1084-MONOMER.
MetaCyc: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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi172 – 1721D → K: Does not affect the kinetic parameters but results in a slightly less halotolerant protein. 1 Publication
Mutagenesisi216 – 2161D → K: Does not affect the kinetic parameters but results in a slightly less halotolerant protein. 1 Publication
Mutagenesisi344 – 3441D → K: Does not affect the kinetic parameters and has no effect on the salt activity profile. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Glucose 1-dehydrogenasePRO_0000414832Add
BLAST

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

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi14 – 174Combined sources
Beta strandi27 – 3711Combined sources
Helixi39 – 468Combined sources
Beta strandi47 – 493Combined sources
Beta strandi57 – 604Combined sources
Beta strandi63 – 719Combined sources
Beta strandi82 – 854Combined sources
Beta strandi87 – 893Combined sources
Helixi97 – 1004Combined sources
Helixi104 – 1063Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi125 – 1317Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1373Combined sources
Helixi140 – 1423Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 16416Combined sources
Turni165 – 1684Combined sources
Beta strandi175 – 1795Combined sources
Helixi183 – 19412Combined sources
Beta strandi201 – 2066Combined sources
Helixi213 – 2208Combined sources
Beta strandi224 – 2274Combined sources
Turni228 – 2303Combined sources
Helixi233 – 2353Combined sources
Helixi236 – 2394Combined sources
Beta strandi243 – 2486Combined sources
Helixi253 – 26210Combined sources
Beta strandi263 – 2719Combined sources
Helixi284 – 29310Combined sources
Beta strandi297 – 3004Combined sources
Helixi306 – 31813Combined sources
Helixi321 – 3277Combined sources
Beta strandi328 – 3336Combined sources
Helixi334 – 3418Combined sources
Beta strandi349 – 3535Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-357.
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
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. Positions 1-357.
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

BioCyciHMED523841:GLDU-1084-MONOMER.
MetaCyc: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: January 20, 2016
This is version 79 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.