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HAMAP rule MF_02127

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General rule information [?]

Accession MF_02127
Dates 21-NOV-2011 (Created)
28-JUN-2024 (Last updated, Version 13)
Name Glucose_DH
Scope(s) Archaea
Template(s) O93715 (GLCDH_SACSO); Q977U7 (GLCDH_HALMT); Q6L047 (GLCD2_PICTO); P13203 (GLCDH_THEAC); Q703W7 (GLCDH_THETK); [ Recover all ]
Triggered by HAMAP; MF_02127 (Get profile general information and statistics)

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 Name=gdh;

Comments [?]

case <OC:Halobacteria>
FUNCTIONCatalyzes 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
FUNCTIONCatalyzes 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 Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47;
CATALYTIC ACTIVITY Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.47;
case <FTGroup:1> and <FTGroup:2>
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; 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 Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
end case
SIMILARITYBelongs 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:D-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;
Pfam PF00107; ADH_zinc_N; 1;

Features [?]

From: GLCDH_SACSO (O93715)
Key From To Description Tag Condition FTGroup
BINDING 189 192 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"		 [TNSA]-x-x-[ILV]
BINDING 211 213 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"		 N-x-[RH]
BINDING 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 89 89 /ligand="substrate" N
BINDING 114 114 /ligand="substrate" E
BINDING 150 150 /ligand="substrate" [QE]
BINDING 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 93 93 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#2"
/ligand_note="structural"		 C 2
BINDING 96 96 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#2"
/ligand_note="structural"		 C 2
BINDING 99 99 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#2"
/ligand_note="structural"		 C 2
BINDING 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 354 354 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"		 K
From: GLCDH_HALMT (Q977U7)
Key From To Description Tag Condition FTGroup
case not <FT:2>
BINDING 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 Nter: None Cter: 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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