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InterPro: IPR008333 Oxidoreductase, FAD-binding domain

Protein matches Help

UniProtKB

Matches:

6075 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR008333 OxRdtase_FAD-bd_dom

Secondary

IPR001834

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00970	FAD_binding_6	6075
Signatures in BioMart

InterPro Relationships Help

Parent

IPR017927 Ferredoxin reductase-type FAD-binding domain

Found in

IPR000951 Phthalate dioxygenase reductase, FPNCR module
IPR001221 Phenol hydroxylase reductase
IPR001834 NADH:cytochrome b5 reductase (CBR)
IPR010205 NADH-quinone reductase, Na(+)-translocating, F subunit
IPR011884 Phenylacetate-CoA oxygenase/reductase, PaaK subunit
IPR012137 Nitrate reductase NADH dependent
IPR012165 Cytochrome-c3 hydrogenase, gamma subunit
IPR014260 Sulphite reductase, subunit B
IPR017634 Benzoyl-CoA oxygenase/reductase, BoxA protein

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

These sequences contain an oxidoreductase FAD-binding domain.

To date, the 3D-structures of the flavoprotein domain of Zea mays (Maize) nitrate reductase [1] and of pig NADH:cytochrome b5 reductase [2] have been solved. The overall fold is similar to that of ferredoxin:NADP⁺ reductase [3]: the FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel, while the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet flanked by 2 helices on each side).

Structural links Help

PDB - click here

SCOP: b.43.4.2 , c.25.1.2 , c.25.1.3

CATH: 2.40.30.10 , 3.40.50.80

Database links Help

Enzyme: EC:1

PANDIT: PF00970

Blocks: IPB008333

Pfam Clan: CL0076.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008333

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A6ZVM6 NADH-cytochrome b5 reductase 1

B1AS42 NADH-cytochrome b5 reductase-like

P00387 NADH-cytochrome b5 reductase 3

P11035 Nitrate reductase [NADH] 2

P16081 Nitrate reductase [NADH] 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008333	Oxidoreductase, FAD-binding domain
IPR001834	NADH:cytochrome b5 reductase (CBR)
IPR005066	Moybdenum cofactor oxidoreductase, dimerisation
IPR001433	Oxidoreductase FAD/NAD(P)-binding
IPR017927	Ferredoxin reductase-type FAD-binding domain
IPR018506	Cytochrome b5, heme-binding site
IPR014756	Immunoglobulin E-set
IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
IPR008335	Eukaryotic molybdopterin oxidoreductase
IPR000572	Oxidoreductase, molybdopterin binding
IPR017938	Riboflavin synthase-like beta-barrel
IPR001199	Cytochrome b5
IPR012137	Nitrate reductase NADH dependent
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Lu G, Campbell WH, Schneider G, Lindqvist Y. Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases. Structure 2 809-21 1994 [PubMed: 7812715] http://dx.doi.org/10.1016/S0969-2126(94)00082-4
2.	Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K. Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution. Biochemistry 34 2763-7 1995 [PubMed: 7893687] http://dx.doi.org/10.1021/bi00009a004
3.	Karplus PA, Bruns CM. Structure-function relations for ferredoxin reductase. J. Bioenerg. Biomembr. 26 89-99 1994 [PubMed: 8027025] http://dx.doi.org/10.1007/BF00763221

Additional Reading Open in usermanual
	Nogues I, Perez-Dorado I, Frago S, Bittel C, Mayhew SG, Gomez-Moreno C, Hermoso JA, Medina M, Cortez N, Carrillo N. The ferredoxin-NADP(H) reductase from Rhodobacter capsulatus: molecular structure and catalytic mechanism. Biochemistry 44 2005 11730-40 [PubMed: 16128574] http://dx.doi.org/10.1021/bi0508183
	Perez-Dorado I, Bittel C, Cortez N, Hermoso JA. Crystallization and preliminary X-ray diffraction analysis of ferredoxin-NADP(H) reductase from Rhodobacter capsulatus. Acta Crystallogr. D Biol. Crystallogr. 60 2004 2332-5 [PubMed: 15583382] http://dx.doi.org/10.1107/S090744490402640X
	Chatwood LL, Muller J, Gross JD, Wagner G, Lippard SJ. NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath). Biochemistry 43 2004 11983-91 [PubMed: 15379538] http://dx.doi.org/10.1021/bi049066n
	Wang A, Zeng Y, Han H, Weeratunga S, Morgan BN, Moenne-Loccoz P, Schonbrunn E, Rivera M. Biochemical and structural characterization of Pseudomonas aeruginosa Bfd and FPR: ferredoxin NADP+ reductase and not ferredoxin is the redox partner of heme oxygenase under iron-starvation conditions. Biochemistry 46 2007 12198-211 [PubMed: 17915950] http://dx.doi.org/10.1021/bi7013135
	Bando S, Takano T, Yubisui T, Shirabe K, Takeshita M, Nakagawa A. Structure of human erythrocyte NADH-cytochrome b5 reductase. Acta Crystallogr. D Biol. Crystallogr. 60 2004 1929-34 [PubMed: 15502298] http://dx.doi.org/10.1107/S0907444904020645
	Hyde GE, Crawford NM, Campbell WH. The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases. J. Biol. Chem. 266 1991 23542-7 [PubMed: 1748631] http://intl.jbc.org/cgi/reprint/266/35/23542.pdf

InterPro 23.1