Summary
4Fe-4S binding domain
Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
InterPro entry IPR001450
Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s) PUBMED:3932661, PUBMED:2506358. One group, originally found in bacteria, has been termed "bacterial-type", in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including four Cys residues that bind to a 4Fe-4S centre.
During the evolution of bacterial-type ferredoxins, intrasequence gene duplication, transposition and fusion events occured, resulting in the appearance of proteins with multiple iron-sulphur centres: e.g. dicluster-type (2[4Fe-4S]) and polyferredoxins, iron-sulphur subunits of bacterial succinate dehydrogenase/fumarate reductase, formate hydrogenlyase and formate dehydrogenase complexes, pyruvate-flavodoxin oxidoreductase, NADH:ubiquinone reductase, as well as others. In some bacterial ferredoxins, one of the duplicated domains has lost one or more of the four conserved Cys residues. These domains have either lost their iron-sulphur binding property, or bind to a 3Fe-4S centre instead of a 4Fe-4S centre. 3D structures are now known both for a number of monocluster-type PUBMED:2600971 and dicluster-type PUBMED:7966291 4Fe-4S ferredoxins.
CAUTION: PRINTS signature in the current entry is known to miss protein matches and should be updated in the near future.
Clan
This family is a member of clan 4Fe-4S (CL0344), which contains the following 3 members:
DUF1271 ETF_QO Fer4Gene Ontology
| Molecular function | electron carrier activity (GO:0009055) |
| iron-sulfur cluster binding (GO:0051536) |
Internal database links
| SCOOP: | Tsg UPF0153 DUF1271 DUF1982 |
External database links
| HOMSTRAD: | fer4 Fe_hyd_lg_C |
| PANDIT: | PF00037 |
| PROSITE: | PDOC00176 |
| SCOP: | 5fd1 |
| SYSTERS: | Fer4 |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prosite |
| Previous IDs: | fer4; |
| Type: | Domain |
| Author: | Bateman A, Eddy SR |
| Number in seed: | 533 |
| Number in full: | 9676 |
| Average length of the domain: | 23.80 aa |
| Average identity of full alignment: | 39 % |
| Average coverage of the sequence by the domain: | 9.61 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 24 | ||||||||||||
| Family (HMM) version: | 20 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There are 16 interactions for this family. More...
PsaD TPP_enzyme_C Fe_hyd_lg_C Succ_DH_flav_C Form-deh_trans EKR Fumarate_red_D PSI_PsaE PsaA_PsaB Fer2 Fer4 FAD_binding_2 DHO_dh POR Fe_hyd_SSU Fumarate_red_CStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Fer4 domain has been found.
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