AC   MF_02127;
DC   Protein; auto
TR   HAMAP; MF_02127; -; 1; level=0
XX
Names: Glucose_DH
XX
ID   GLCDH
DE   RecName: Full=Glucose 1-dehydrogenase;
DE            Short=GDH;
DE            Short=GlcDH;
DE            EC=1.1.1.47;
GN   Name=gdh;
XX
case <OC:Halobacteria>
CC   -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to
CC       D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as
CC       electron acceptor. Is involved in the degradation of glucose through a
CC       modified Entner-Doudoroff pathway.
else
CC   -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to
CC       D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as
CC       electron acceptor. Is involved in the degradation of glucose through a
CC       non-phosphorylative variant of the Entner-Doudoroff pathway.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH;
CC         Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.47;
case <FTGroup:1> and <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is
CC       essential for catalytic activity while the other has a structural
CC       function.;
else
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
end case
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Glucose 1-dehydrogenase subfamily.
XX
DR   PROSITE; PS00059; ADH_ZINC; 1; trigger=no
DR   Pfam; PF08240; ADH_N; 1; trigger=no
DR   Pfam; PF00107; ADH_zinc_N; 1; trigger=no
XX
KW   Carbohydrate metabolism
KW   Metal-binding
KW   NAD
KW   NADP
KW   Nucleotide-binding
KW   Oxidoreductase
KW   Zinc
XX
GO   GO:0005536; F:glucose binding
GO   GO:0047936; F:glucose 1-dehydrogenase [NAD(P)] activity
GO   GO:0070401; F:NADP+ binding
GO   GO:0070403; F:NAD+ binding
GO   GO:0008270; F:zinc ion binding
GO   GO:0019595; P:non-phosphorylated glucose catabolic process
XX
FT   From: GLCDH_SACSO (O93715)
FT   BINDING         189..192
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: [TNSA]-x-x-[ILV]
FT   BINDING         211..213
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: N-x-[RH]
FT   BINDING         277..279
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: [FL]-x-[FVILT]
FT   BINDING         305..307
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [LSTAV]-x-[ND]
FT   BINDING         41
FT                   /ligand="substrate"
FT   Condition: [TS]
FT   BINDING         89
FT                   /ligand="substrate"
FT   Optional; Condition: N
FT   BINDING         114
FT                   /ligand="substrate"
FT   Optional; Condition: E
FT   BINDING         150
FT                   /ligand="substrate"
FT   Condition: [QE]
FT   BINDING         154
FT                   /ligand="substrate"
FT   Optional; Condition: [DN]
FT   BINDING         307
FT                   /ligand="substrate"
FT   Condition: [ND]
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: [CD]
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: E
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="structural"
FT   Optional; Group: 2; Condition: C
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="structural"
FT   Optional; Group: 2; Condition: C
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="structural"
FT   Optional; Group: 2; Condition: C
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="structural"
FT   Optional; Group: 2; Condition: C
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: [QE]
FT   BINDING         354
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: K
FT   From: GLCDH_HALMT (Q977U7)
case not <FT:2>
FT   BINDING         207..208
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: R-R
end case
XX
Size: 347-368;
Related: None;
Template: O93715; Q977U7; Q6L047; P13203; Q703W7;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in CALMQ, HALTV, PICTO, SACS2, VULM7
Plasmid: in HALTV
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.
XX
# Revision 1.12 2022/11/19
//