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HAMAP rule MF_02127

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General rule information [?]

Accession MF_02127
Dates 21-NOV-2011 (Created)
19-NOV-2022 (Last updated, Version 12)
Name Glucose_DH
Scope
Archaea
Templates O93715 (GLCDH_SACSO); Q977U7 (GLCDH_HALMT); Q6L047 (GLCD2_PICTO); P13203 (GLCDH_THEAC); Q703W7 (GLCDH_THETK): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
GLCDH
Protein name
RecName: Full=Glucose 1-dehydrogenase;
Short=GDH;
Short=GlcDH;
EC 1.1.1.47;
Gene name
gdh

Comments [?]

case <OC:Halobacteria>
Function Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a modified Entner-Doudoroff pathway.
else
Function Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.
end case
Catalytic activity RHEA:14293: D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH
EC 1.1.1.47
RHEA:14405: D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH
EC 1.1.1.47
case <FTGroup:1> and <FTGroup:2>
Cofactor Zn(2+)
Note: Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function.
else
Cofactor Zn(2+)
end case
Similarity Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

Keywords [?]

Carbohydrate metabolism
Metal-binding
NAD
NADP
Nucleotide-binding
Oxidoreductase
Zinc

Gene Ontology [?]

GO:0005536; Molecular function: glucose binding.
GO:0047936; Molecular function: glucose 1-dehydrogenase [NAD(P)] activity.
GO:0070401; Molecular function: NADP+ binding.
GO:0070403; Molecular function: NAD+ binding.
GO:0008270; Molecular function: zinc ion binding.
GO:0019595; Biological process: non-phosphorylated glucose catabolic process.

Cross-references [?]

PROSITE PS00059; ADH_ZINC; 1;
Pfam PF08240; ADH_N; 1;
PF00107; ADH_zinc_N; 1;

Features [?]

From: GLCDH_SACSO (O93715)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING (Optional)     189     192       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     [TNSA]-x-x-[ILV]  
BINDING (Optional)     211     213       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     N-x-[RH]  
BINDING (Optional)     277     279       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     [FL]-x-[FVILT]  
BINDING     305     307       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     [LSTAV]-x-[ND]  
BINDING     41     41       /ligand="substrate     [TS]  
BINDING (Optional)     89     89       /ligand="substrate     N  
BINDING (Optional)     114     114       /ligand="substrate     E  
BINDING     150     150       /ligand="substrate     [QE]  
BINDING (Optional)     154     154       /ligand="substrate     [DN]  
BINDING     307     307       /ligand="substrate     [ND]  
BINDING     39     39       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic     [CD]   1
BINDING     66     66       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic     H   1
BINDING     67     67       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic     E   1
BINDING (Optional)     93     93       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="structural     C   2
BINDING (Optional)     96     96       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="structural     C   2
BINDING (Optional)     99     99       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="structural     C   2
BINDING (Optional)     107     107       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="structural     C   2
BINDING     150     150       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic     [QE]   1
BINDING (Optional)     354     354       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     K  
case not <FT:2>
From: GLCDH_HALMT (Q977U7)
BINDING (Optional)     207     208       /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349     R-R  
end case

Additional information [?]

Size range 347-368 amino acids
Related rules None
Fusion None
Comments Some members of this family also display good catalytic efficiency with D-galactose as substrate (SULSF, Q6L047 in PICTO, THEAC), which seems to be a physiological substrate in some species.


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