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InterPro: IPR007419 BFD-like [2Fe-2S]-binding domain

Protein matches Help

UniProtKB

Matches:

2628 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

IPR007419 BFD-like_2Fe2S-bd_dom

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF04324	Fer2_BFD	2628
Signatures in BioMart

InterPro Relationships Help

Found in

IPR010238 NIF system FeS cluster assembly, NifU
IPR012744 Nitrite reductase [NAD(P)H] large subunit, NirB
IPR016217 Nitrogen fixation, NifU
IPR017121 Nitrite reductase [NAD(P)H], large subunit
IPR017224 Opine oxidase, subunit A/hydrogen cyanide synthase, subunit B
IPR017752 Anaerobic glycerol-3-phosphate dehydrogenase, A subunit

InterPro annotation

Entry Details in BioMart

Abstract

The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as bacterioferritin-associated ferredoxin (BFD, P13655). The function of BFD is not known, but it may be a general redox and/or regulatory component involved in the iron storage or mobilisation functions of bacterioferritin in bacteria [1]. This domain is also found in nitrate reductase proteins in association with the nitrite and sulphite reductase 4Fe-4S domain (IPR006067), nitrite/sulphite reductase ferredoxin-like half domain (IPR005117) and pyridine nucleotide-disulphide oxidoreductase (IPR001327). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N-terminal domain (IPR002871) and C-terminal domain (IPR001075).

Database links Help

PANDIT: PF04324

Blocks: IPB007419

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR007419

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O33732 Nitrate reductase

P20628 Nitrogen fixation protein nifU

P22944 Nitrite reductase [NAD(P)H]

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001075	NIF system FeS cluster assembly, NifU, C-terminal
IPR006066	Nitrite/sulphite reductase iron-sulphur/siroheam-binding site
IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
IPR002871	NIF system FeS cluster assembly, NifU, N-terminal
IPR017941	Rieske [2Fe-2S] iron-sulphur domain
IPR010238	NIF system FeS cluster assembly, NifU
IPR006963	Molybdopterin oxidoreductase, Fe4S4 domain
IPR006655	Molybdopterin oxidoreductase, prokaryotic, conserved site
IPR009010	Aspartate decarboxylase-like fold
IPR005117	Nitrite/sulphite reductase, hemoprotein beta-component, ferrodoxin-like
IPR016217	Nitrogen fixation, NifU
IPR006657	Molydopterin dinucleotide-binding domain
IPR006656	Molybdopterin oxidoreductase
IPR012744	Nitrite reductase [NAD(P)H] large subunit, NirB
IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR012748	Nitrite reductase [NAD(P)H] large subunit, NirD
IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
IPR007419	BFD-like [2Fe-2S]-binding domain
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	Garg RP, Vargo CJ, Cui X, Kurtz DM Jr. A [2Fe-2S] protein encoded by an open reading frame upstream of the Escherichia coli bacterioferritin gene. Biochemistry 35 6297-301 1996 [PubMed: 8639572] http://dx.doi.org/10.1021/bi9600862

Additional Reading Open in usermanual
	Andrews SC. Iron storage in bacteria. Adv. Microb. Physiol. 40 1998 281-351 [PubMed: 9889981]
	Quail MA, Jordan P, Grogan JM, Butt JN, Lutz M, Thomson AJ, Andrews SC, Guest JR. Spectroscopic and voltammetric characterisation of the bacterioferritin-associated ferredoxin of Escherichia coli. Biochem. Biophys. Res. Commun. 229 1996 635-42 [PubMed: 8954950] http://dx.doi.org/10.1006/bbrc.1996.1856

InterPro 23.1