Summary: FhuF 2Fe-2S C-terminal domain
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FhuF 2Fe-2S C-terminal domain Provide feedback
This family consists of several bacterial ferric iron reductase protein (FhuF) sequences. FhuF is involved in the reduction of ferric iron in cytoplasmic ferrioxamine B . This domain is the C-terminal domain that contains 4 conserved cysteine residues that are found to be part of a 2Fe-2S cluster .
Muller K, Matzanke BF, Schunemann V, Trautwein AX, Hantke K; , Eur J Biochem 1998;258:1001-1008.: FhuF, an iron-regulated protein of Escherichia coli with a new type of [2Fe-2S] center. PUBMED:9990318 EPMC:9990318
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR024726
Ferric iron reductase (FhuF) is involved in the reduction of ferric iron in cytoplasmic ferrioxamine B [PUBMED:9990318]. This entry represents the C-terminal domain that contains 4 conserved cysteine residues found to be part of a 2Fe-2S cluster [PUBMED:9990318].
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|Molecular function||2 iron, 2 sulfur cluster binding (GO:0051537)|
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Curation and family details
|Seed source:||Pfam-B_11690 (release 9.0)|
|Author:||Moxon SJ, Bateman A|
|Number in seed:||60|
|Number in full:||1049|
|Average length of the domain:||22.30 aa|
|Average identity of full alignment:||54 %|
|Average coverage of the sequence by the domain:||8.86 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
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