2OHI

Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, reduced state

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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)
C [auth D]	d2ohid2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
C [auth D]	d2ohid1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
A	d2ohia2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
A	d2ohia1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
B	d2ohib2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
B	d2ohib1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
D [auth E]	d2ohie2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
D [auth E]	d2ohie1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
E [auth G]	d2ohig2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
E [auth G]	d2ohig1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
F [auth H]	d2ohih2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
F [auth H]	d2ohih1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
G [auth I]	d2ohii2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
G [auth I]	d2ohii1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
H [auth J]	d2ohij2	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
H [auth J]	d2ohij1	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	automated matches	automated matches	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C [auth D]	Lactamase_B_1	e2ohiD1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B_1	ECOD (1.6)
C [auth D]	Flavodoxin_1	e2ohiD2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: Flavodoxin_1	ECOD (1.6)
A	Lactamase_B_1	e2ohiA1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B_1	ECOD (1.6)
A	Flavodoxin_1	e2ohiA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: Flavodoxin_1	ECOD (1.6)
B	Lactamase_B_1	e2ohiB1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B_1	ECOD (1.6)
B	Flavodoxin_1	e2ohiB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: Flavodoxin_1	ECOD (1.6)
D [auth E]	Lactamase_B_1	e2ohiE1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B_1	ECOD (1.6)
D [auth E]	Flavodoxin_1	e2ohiE2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: Flavodoxin_1	ECOD (1.6)
E [auth G]	Lactamase_B_1	e2ohiG1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B_1	ECOD (1.6)
E [auth G]	Flavodoxin_1	e2ohiG2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: Flavodoxin_1	ECOD (1.6)
F [auth H]	Lactamase_B_1	e2ohiH1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B_1	ECOD (1.6)
F [auth H]	Flavodoxin_1	e2ohiH2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: Flavodoxin_1	ECOD (1.6)
G [auth I]	Lactamase_B_1	e2ohiI1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B_1	ECOD (1.6)
G [auth I]	Flavodoxin_1	e2ohiI2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: Flavodoxin_1	ECOD (1.6)
H [auth J]	Lactamase_B_1	e2ohiJ1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B_1	ECOD (1.6)
H [auth J]	Flavodoxin_1	e2ohiJ2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: Flavodoxin_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C [auth D]	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
C [auth D]	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
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)
B	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
B	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
D [auth E]	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
D [auth E]	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
E [auth G]	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
E [auth G]	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
F [auth H]	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
F [auth H]	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
G [auth I]	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
G [auth I]	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
H [auth J]	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
H [auth J]	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, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	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, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	PF00258	Flavodoxin (Flavodoxin_1)	Flavodoxin	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	Type A flavoprotein fprA	oxidoreductase activity 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 electron transfer activity oxidoreductase activity 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 electron transfer activity cation binding metal ion binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	IPR001226	Flavodoxin, conserved site	Conserved Site
A, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	IPR045761	ODP domain	Domain
A, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	IPR016440	Rubredoxin-oxygen oxidoreductase	Family
A, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	IPR036866	Ribonuclease Z/Hydroxyacylglutathione hydrolase-like	Homologous Superfamily
A, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	IPR029039	Flavoprotein-like superfamily	Homologous Superfamily
A, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	IPR001279	Metallo-beta-lactamase	Domain
A, B, C [auth D], D [auth E], E [auth G], A, B, C [auth D], D [auth E], E [auth G], F [auth H], G [auth I], H [auth J]	IPR008254	Flavodoxin/nitric oxide synthase	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.