2VFR

Alditol Oxidase from Streptomyces coelicolor A3(2): Native Enzyme

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)
A	d2vfra1	Alpha and beta proteins (a+b)	Ferredoxin-like	FAD-linked oxidases, C-terminal domain	Alditol oxidase	Alditol oxidase	(Streptomyces coelicolor A3(2) ) [TaxId: 100226 ],	SCOPe (2.08)
A	d2vfra2	Alpha and beta proteins (a+b)	FAD-binding/transporter-associated domain-like	FAD-binding/transporter-associated domain-like	FAD-linked oxidases, N-terminal domain	Alditol oxidase	(Streptomyces coelicolor A3(2) ) [TaxId: 100226 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	AldO C-terminal domain-like	8045165	4004332	SCOP2 (2022-06-29)
A	SCOP2 Family	FAD-linked oxidases, N-terminal domain	8057018	4002178	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	FAD-linked oxidases C-terminal domain-like	8057017	3001317	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	FAD-binding/transporter-associated domain-like	8057019	3000913	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ALO	e2vfrA2	A: a+b two layers	X: Alpha-beta plaits	H: FAD-linked oxidases, C-terminal domain (From Topology)	T: FAD-linked oxidases, C-terminal domain	F: ALO	ECOD (1.6)
A	FAD_binding_4	e2vfrA1	A: a+b complex topology	X: FAD-binding domain-like	H: FAD-binding domain (From Topology)	T: FAD-binding domain	F: FAD_binding_4	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.43.10	Alpha Beta	2-Layer Sandwich	Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase	domain 2	CATH (4.3.0)
A	3.30.465.10	Alpha Beta	2-Layer Sandwich	Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase	domain 3	CATH (4.3.0)
A	3.30.70.2530	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	3.30.70.2520	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	1.10.45.10	Mainly Alpha	Orthogonal Bundle	Vanillyl-alcohol Oxidase	Chain A, domain 4	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF04030	D-arabinono-1,4-lactone oxidase (ALO)	D-arabinono-1,4-lactone oxidase	-	Family
A	PF01565	FAD binding domain (FAD_binding_4)	FAD binding domain	This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, call ...	This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [1]. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	XYLITOL OXIDASE	L-gulono-1,4-lactone dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors, cytochrome as acceptor oxidoreductase activity, acting on the CH-CH group of donors catalytic activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding L-gulono-1,4-lactone dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors, cytochrome as acceptor oxidoreductase activity, acting on the CH-CH group of donors catalytic activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor oxidoreductase activity, acting on CH-OH group of donors D-arabinono-1,4-lactone oxidase activity xylitol oxidase activity	-	cellular anatomical structure membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR016167	FAD-binding, type PCMH, subdomain 1	Homologous Superfamily
A	IPR006094	FAD linked oxidase, N-terminal	Domain
A	IPR010031	L-gulonolactone/D-arabinono-1,4-lactone oxidase-like	Family
A	IPR016166	FAD-binding domain, PCMH-type	Domain
A	IPR016171	Vanillyl-alcohol oxidase, C-terminal subdomain 2	Homologous Superfamily
A	IPR007173	D-arabinono-1,4-lactone oxidase, C-terminal domain	Domain
A	IPR036318	FAD-binding, type PCMH-like superfamily	Homologous Superfamily
A	IPR016169	FAD-binding, type PCMH, subdomain 2	Homologous Superfamily

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.