Annotations: 4D02

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4d02a2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
A	d4d02a1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF19583	e4d02A2	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: PF19583	ECOD (1.6)
A	PF00258	e4d02A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: PF00258	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
A	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF19583	ODP family beta lactamase (ODP)	ODP family beta lactamase	The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ...	The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.	Domain
A	PF00258	Flavodoxin (Flavodoxin_1)	Flavodoxin	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN	oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors catalytic activity binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors catalytic activity binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding cation binding transition metal ion binding iron ion binding metal ion binding oxidoreductase activity, acting on other nitrogenous compounds as donors, cytochrome as acceptor nitric oxide reductase activity electron transfer activity identical protein binding protein binding	nitric oxide metabolic process catabolic process nitric oxide catabolic process metabolic process reactive nitrogen species metabolic process response to stimulus response to chemical response to nitric oxide response to oxygen-containing compound response to nitrogen compound response to inorganic substance	intracellular anatomical structure cytoplasm cellular anatomical entity protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR023957	Anaerobic nitric oxide reductase flavorubredoxin	Family
A	IPR001279	Metallo-beta-lactamase	Domain
A	IPR008254	Flavodoxin/nitric oxide synthase	Domain
A	IPR045761	ODP domain	Domain
A	IPR016440	Rubredoxin-oxygen oxidoreductase	Family
A	IPR036866	Ribonuclease Z/Hydroxyacylglutathione hydrolase-like	Homologous Superfamily
A	IPR029039	Flavoprotein-like superfamily	Homologous Superfamily
A	IPR024934	Rubredoxin-like domain	Domain
A	IPR024935	Rubredoxin domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.