Annotations: 1VE9

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1ve9b1	Alpha and beta proteins (a/b)	Nucleotide-binding domain	Nucleotide-binding domain	D-aminoacid oxidase, N-terminal domain	D-aminoacid oxidase, N-terminal domain	pig (Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d1ve9b2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	D-aminoacid oxidase-like	D-aminoacid oxidase	pig (Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
A	d1ve9a1	Alpha and beta proteins (a/b)	Nucleotide-binding domain	Nucleotide-binding domain	D-aminoacid oxidase, N-terminal domain	D-aminoacid oxidase, N-terminal domain	pig (Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
A	d1ve9a2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	D-aminoacid oxidase-like	D-aminoacid oxidase	pig (Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Flavoreductase-like	8056824	3000055	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Flavoreductase-like	8056824	3000055	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	DAO_2nd	e1ve9B1	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: DAO_2nd	ECOD (1.6)
B	DAO_1st	e1ve9B2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Nucleotide-binding domain	F: DAO_1st	ECOD (1.6)
A	DAO_2nd	e1ve9A1	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: DAO_2nd	ECOD (1.6)
A	DAO_1st	e1ve9A2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Nucleotide-binding domain	F: DAO_1st	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	3.30.9.10	Alpha Beta	2-Layer Sandwich	D-Amino Acid Oxidase	Chain A, 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	3.30.9.10	Alpha Beta	2-Layer Sandwich	D-Amino Acid Oxidase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01266	FAD dependent oxidoreductase (DAO)	FAD dependent oxidoreductase	This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	D-amino acid oxidase	oxidoreductase activity, acting on the CH-NH2 group of donors oxidoreductase activity oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor D-amino-acid oxidase activity primary methylamine oxidase activity catalytic activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding oxidoreductase activity, acting on the CH-NH2 group of donors oxidoreductase activity oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor D-amino-acid oxidase activity primary methylamine oxidase activity 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	organic hydroxy compound metabolic process dopamine metabolic process catechol-containing compound metabolic process amine metabolic process biogenic amine biosynthetic process biosynthetic process catecholamine metabolic process amine biosynthetic process dopamine biosynthetic process phenol-containing compound metabolic process organic hydroxy compound biosynthetic process catecholamine biosynthetic process phenol-containing compound biosynthetic process metabolic process organic hydroxy compound metabolic process dopamine metabolic process catechol-containing compound metabolic process amine metabolic process biogenic amine biosynthetic process biosynthetic process catecholamine metabolic process amine biosynthetic process dopamine biosynthetic process phenol-containing compound metabolic process organic hydroxy compound biosynthetic process catecholamine biosynthetic process phenol-containing compound biosynthetic process metabolic process cellular process catechol-containing compound biosynthetic process biogenic amine metabolic process neutrophil-mediated killing of symbiont cell biological process involved in interspecies interaction between organisms response to stimulus disruption of cell in another organism defense response to Gram-negative bacterium response to biotic stimulus myeloid leukocyte mediated immunity biological process involved in symbiotic interaction defense response to bacterium neutrophil mediated immunity response to stress response to bacterium leukocyte mediated immunity response to external biotic stimulus biological process involved in interaction with symbiont killing of cells of another organism neutrophil-mediated killing of bacterium neutrophil mediated cytotoxicity response to other organism defense response response to external stimulus defense response to symbiont leukocyte mediated cytotoxicity immune effector process killing by host of symbiont cells neutrophil-mediated killing of gram-negative bacterium defense response to other organism immune system process disruption of anatomical structure in another organism cell killing catabolic process oxoacid metabolic process non-proteinogenic amino acid catabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid catabolic process D-serine metabolic process alpha-amino acid metabolic process cellular catabolic process non-proteinogenic amino acid metabolic process alpha-amino acid catabolic process carboxylic acid catabolic process D-amino acid metabolic process small molecule metabolic process small molecule catabolic process D-amino acid catabolic process amino acid catabolic process D-serine catabolic process glutamine family amino acid catabolic process proline catabolic process glutamine family amino acid metabolic process proline metabolic process L-amino acid catabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process proteinogenic amino acid catabolic process alanine catabolic process D-alanine catabolic process D-alanine metabolic process alanine metabolic process multicellular organismal process digestion	presynapse cellular anatomical structure synapse cell junction presynaptic active zone extracellular region membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle presynapse cellular anatomical structure synapse cell junction presynaptic active zone extracellular region membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle cytosol peroxisomal matrix membrane-enclosed lumen intracellular organelle lumen organelle lumen microbody lumen cell projection

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR023209	D-amino-acid oxidase	Family
A, B	IPR006181	D-amino acid oxidase, conserved site	Conserved Site
A, B	IPR006076	FAD dependent oxidoreductase	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.