AC   MF_02123;
DC   Protein; auto
TR   HAMAP; MF_02123; -; 1; level=0
XX
Names: F420_G6P_DH
XX
ID   FGD
DE   RecName: Full=F420-dependent glucose-6-phosphate dehydrogenase;
DE            Short=FGD;
DE            Short=G6PD;
DE            EC=1.1.98.2;
GN   Name=fgd;
XX
case <OC:Mycobacterium>
CC   -!- FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-
CC       phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in
CC       resistance to oxidative stress, via its consumption of G6P that serves
CC       as a source of reducing power to combat oxidative stress in
CC       mycobacteria.
else
CC   -!- FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-
CC       phosphate (G6P) to 6-phosphogluconolactone.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + H(+) + oxidized coenzyme F420-(gamma-
CC         L-Glu)(n) = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420-
CC         (gamma-L-Glu)(n); Xref=Rhea:RHEA:27294, Rhea:RHEA-COMP:12939,
CC         Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57955,
CC         ChEBI:CHEBI:61548, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC         EC=1.1.98.2;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the F420-dependent glucose-6-phosphate
CC       dehydrogenase family.
XX
DR   Pfam; PF00296; Bac_luciferase; 1; trigger=no
DR   NCBIfam; TIGR03554; F420_G6P_DH; 1; trigger=no
DR   NCBIfam; TIGR03557; F420_G6P_family; 1; trigger=no
XX
KW   Carbohydrate metabolism
KW   Oxidoreductase
XX
GO   GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors
GO   GO:0070967; F:coenzyme F420 binding
GO   GO:0005975; P:carbohydrate metabolic process
XX
FT   From: FGD_MYCTU (P9WNE1)
FT   BINDING         107..108
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT   Condition: [TS]-G
FT   BINDING         177..178
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT   Condition: [GS]-G
FT   BINDING         180..181
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT   Condition: [VALGSEQ]-[VMA]
FT   ACT_SITE        40
FT                   /note="Proton donor"
FT   Condition: H
FT   ACT_SITE        109
FT                   /note="Proton acceptor"
FT   Condition: E
FT   BINDING         39
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT   Condition: D
FT   BINDING         76
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT   Condition: T
FT   BINDING         112
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT   Condition: N
FT   BINDING         195
FT                   /ligand="substrate"
FT   Condition: T
FT   BINDING         198
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         259
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         283
FT                   /ligand="substrate"
FT   Condition: R
XX
Size: 330-345;
Related: None;
Template: A0QQJ4; P9WNE1;
Scope:
 Bacteria; Actinomycetota
Fusion:
 Nter: None
 Cter: None
Duplicate: in RHOJR
Plasmid: in RHOJR
Comments: None
XX
# Revision 1.14 2023/06/01
//