6DXP

The crystal structure of an FMN-dependent NADH-azoreductase from Klebsiella pneumoniae

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	d6dxpa1	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Klebsiella pneumoniae ) [TaxId: 573 ],	SCOPe (2.08)
A	d6dxpa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Klebsiella pneumoniae ) [TaxId: 573 ],	SCOPe (2.08)
B [auth C]	d6dxpc_	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Klebsiella pneumoniae ) [TaxId: 573 ],	SCOPe (2.08)
C [auth B]	d6dxpb1	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Klebsiella pneumoniae ) [TaxId: 573 ],	SCOPe (2.08)
C [auth B]	d6dxpb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Klebsiella pneumoniae ) [TaxId: 573 ],	SCOPe (2.08)
D	d6dxpd1	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Klebsiella pneumoniae ) [TaxId: 573 ],	SCOPe (2.08)
D	d6dxpd2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Klebsiella pneumoniae ) [TaxId: 573 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Flavoproteins	8080963	3001217	SCOP2B (2022-06-29)
B [auth C]	SCOP2 Family	Quinone reductase	8080962	4003674	SCOP2 (2022-06-29)
B [auth C]	SCOP2 Superfamily	Flavoproteins	8080963	3001217	SCOP2 (2022-06-29)
C [auth B]	SCOP2B Superfamily	Flavoproteins	8080963	3001217	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Flavoproteins	8080963	3001217	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)
A	PF02525	e6dxpA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: PF02525	ECOD (1.6)
B [auth C]	PF02525	e6dxpC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: PF02525	ECOD (1.6)
C [auth B]	PF02525	e6dxpB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: PF02525	ECOD (1.6)
D	PF02525	e6dxpD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: PF02525	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
B [auth C]	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
C [auth B]	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
D	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, B [auth C], C [auth B], D	PF02525	Flavodoxin-like fold (Flavodoxin_2)	Flavodoxin-like fold	This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyse the NAD(P)H-dependent two-electron reductions of quinones and protect cell ...	This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyse the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species [1]. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy [1]. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP [2]. This family is related to Pfam:PF03358 and Pfam:PF00258.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C], C [auth B], D	FMN-dependent NADH-azoreductase	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 NAD(P)H, NAD(P) as acceptor oxidoreductase activity, acting on NAD(P)H 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 NAD(P)H, NAD(P) as acceptor oxidoreductase activity, acting on NAD(P)H catalytic activity electron transfer activity oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C], C [auth B], D	IPR023048	NADH:quinone oxidoreductase, FMN-dependent	Family
A, B [auth C], C [auth B], D	IPR003680	Flavodoxin-like fold	Domain
A, B [auth C], C [auth B], D	IPR029039	Flavoprotein-like superfamily	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 R01GM133198.