4GDP | pdb_00004gdp

Yeast polyamine oxidase FMS1, N195A mutant

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	KOG0029_like	e4gdpA4	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: KOG0029_like	ECOD (1.6)
A	Amino_oxidase_1st	e4gdpA3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Amino_oxidase_1st	ECOD (1.6)
B	KOG0029_like	e4gdpB4	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: KOG0029_like	ECOD (1.6)
B	Amino_oxidase_1st	e4gdpB3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Amino_oxidase_1st	ECOD (1.6)
C	KOG0029_like	e4gdpC4	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: KOG0029_like	ECOD (1.6)
C	Amino_oxidase_1st	e4gdpC3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Amino_oxidase_1st	ECOD (1.6)
D	KOG0029_like	e4gdpD4	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: KOG0029_like	ECOD (1.6)
D	Amino_oxidase_1st	e4gdpD3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Amino_oxidase_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
A	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)
B	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
B	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)
C	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
C	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)
D	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
D	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01593	Flavin containing amine oxidoreductase (Amino_oxidase)	Flavin containing amine oxidoreductase	This family consists of various amine oxidases, including maze polyamine oxidase (PAO) [1] and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene ...	This family consists of various amine oxidases, including maze polyamine oxidase (PAO) [1] and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines [2]. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium [3]. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines [1]. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Polyamine oxidase FMS1	oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor polyamine oxidase activity oxidoreductase activity, acting on the CH-NH group of donors spermine oxidase activity catalytic activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding anion binding nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor polyamine oxidase activity oxidoreductase activity, acting on the CH-NH group of donors spermine oxidase activity catalytic activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding anion binding nucleotide binding heterocyclic compound binding small molecule binding N(1)-acetylpolyamine oxidase (3-acetamidopropanal-forming) activity chromatin binding FAD-dependent H3K4me/H3K4me3 demethylase activity catalytic activity, acting on a protein protein demethylase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen histone demethylase activity demethylase activity histone H3 demethylase activity histone modifying activity histone H3K4 demethylase activity N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity	catabolic process polyamine metabolic process biogenic amine catabolic process spermine catabolic process amine metabolic process spermine metabolic process metabolic process cellular process polyamine catabolic process biogenic amine metabolic process amine catabolic process regulation of biosynthetic process regulation of biological process regulation of cellular process catabolic process polyamine metabolic process biogenic amine catabolic process spermine catabolic process amine metabolic process spermine metabolic process metabolic process cellular process polyamine catabolic process biogenic amine metabolic process amine catabolic process regulation of biosynthetic process regulation of biological process regulation of cellular process epigenetic regulation of gene expression biological regulation regulation of macromolecule metabolic process gene expression macromolecule biosynthetic process cellular component organization regulation of gene expression biosynthetic process chromatin organization chromatin remodeling regulation of macromolecule biosynthetic process cellular component organization or biogenesis macromolecule metabolic process regulation of metabolic process pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process modified amino acid biosynthetic process carboxylic acid metabolic process modified amino acid metabolic process vitamin biosynthetic process amide biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process vitamin metabolic process pantothenate biosynthetic process small molecule metabolic process amide metabolic process monocarboxylic acid metabolic process water-soluble vitamin metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR002937	Amine oxidase	Domain
A, B, C, D	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D	IPR050281	Flavin monoamine oxidase and related enzymes	Family

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.