1H6B

Reduced Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas mobilis complexed with glycerol

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1h6bb1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain	Glucose-fructose oxidoreductase, N-terminal domain	(Zymomonas mobilis ) [TaxId: 542 ],	SCOPe (2.08)
B	d1h6bb2	Alpha and beta proteins (a+b)	FwdE/GAPDH domain-like	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	Glucose 6-phosphate dehydrogenase-like	Glucose-fructose oxidoreductase	(Zymomonas mobilis ) [TaxId: 542 ],	SCOPe (2.08)
A	d1h6ba1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain	Glucose-fructose oxidoreductase, N-terminal domain	(Zymomonas mobilis ) [TaxId: 542 ],	SCOPe (2.08)
A	d1h6ba2	Alpha and beta proteins (a+b)	FwdE/GAPDH domain-like	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	Glucose 6-phosphate dehydrogenase-like	Glucose-fructose oxidoreductase	(Zymomonas mobilis ) [TaxId: 542 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	GAPDH-like	8044595	3000043	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GAPDH-like	8044595	3000043	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	GFO_IDH_MocA_C	e1h6bB1	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: GFO_IDH_MocA_C	ECOD (1.6)
B	GFO_IDH_MocA	e1h6bB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GFO_IDH_MocA	ECOD (1.6)
A	GFO_IDH_MocA_C	e1h6bA1	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: GFO_IDH_MocA_C	ECOD (1.6)
A	GFO_IDH_MocA	e1h6bA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GFO_IDH_MocA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01408	Oxidoreductase family, NAD-binding Rossmann fold (GFO_IDH_MocA)	Oxidoreductase family, NAD-binding Rossmann fold	-	Family
A, B	PF02894	Oxidoreductase family, C-terminal alpha/beta domain (GFO_IDH_MocA_C)	Oxidoreductase family, C-terminal alpha/beta domain	This family of enzymes utilise NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PRECURSOR FORM OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding glucose-fructose oxidoreductase activity oxidoreductase activity oxidoreductase activity, acting on CH-OH group of donors catalytic activity	sorbitol biosynthetic process carbohydrate metabolic process hexitol metabolic process polyol metabolic process hexitol biosynthetic process small molecule biosynthetic process organic hydroxy compound metabolic process carbohydrate biosynthetic process alditol biosynthetic process primary metabolic process alcohol metabolic process biosynthetic process alditol metabolic process organic hydroxy compound biosynthetic process polyol biosynthetic process sorbitol biosynthetic process carbohydrate metabolic process hexitol metabolic process polyol metabolic process hexitol biosynthetic process small molecule biosynthetic process organic hydroxy compound metabolic process carbohydrate biosynthetic process alditol biosynthetic process primary metabolic process alcohol metabolic process biosynthetic process alditol metabolic process organic hydroxy compound biosynthetic process polyol biosynthetic process alcohol biosynthetic process metabolic process small molecule metabolic process sorbitol metabolic process	periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR008354	Glucose-fructose oxidoreductase, bacterial	Family
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR050463	Gfo/Idh/MocA family oxidoreductases and glycosidases	Family
A, B	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A, B	IPR004104	Gfo/Idh/MocA-like oxidoreductase, C-terminal	Domain
A, B	IPR000683	Gfo/Idh/MocA-like oxidoreductase, N-terminal	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.