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30  structures 7028  species 0  interactions 16223  sequences 69  architectures

Family: FeS_assembly_P (PF01883)

Summary: Iron-sulfur cluster assembly protein

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Iron-sulfur cluster assembly protein Provide feedback

This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core and a putative active site containing a highly conserved cysteine [1]. Members of this family are involved in a range of physiological functions. The family includes PaaJ (PhaH) O84984 from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF) O84982 PaaI (PhaG) O84983 and PaaK (PhaI) O84985 which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid [2]. It also includes PaaD P76080 from Escherichia coli, a member of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation [3]. Furthermore, several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts [4]. They are involved in diverse cellular processes including cellular respiration, DNA replication and repair, antibiotic resistance, and dinitrogen fixation [5]. The biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set of specialised proteins. Proteins containing this domain include the chloroplast protein HCF101 (high chlorophyll fluorescence 101), Q6STH5 which has been described as an essential and specific factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex [4] and is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins [4]. The mature HCF101 protein contains this domain at the N-terminal as well as eight cysteine residues along the sequence. All cysteine residues are conserved among higher plants, but of the two cysteine residues located in this domain only Cys128 is highly conserved and is present in the highly conserved P-loop domain of the plant HCF101 (CKGGVGKS) [4]. SufT protein from Staphylococcus aureus is composed of this domain solely and is shown to be involved in the maturation of FeS proteins [5]. Given all this data, it is hypothesised that this domain might play a role in FeS cluster assembly.

Literature references

  1. Almeida MS, Herrmann T, Peti W, Wilson IA, Wuthrich K;, Protein Sci. 2005;14:2880-2886.: NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins. PUBMED:16199668 EPMC:16199668

  2. Olivera ER, Minambres B, Garcia B, Muniz C, Moreno MA, Ferrandez A, Diaz E, Garcia JL, Luengo JM; , Proc Natl Acad Sci U S A 1998;95:6419-6424.: Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: the phenylacetyl-CoA catabolon. PUBMED:9600981 EPMC:9600981

  3. Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E; , J Biol Chem 1998;273:25974-25986.: Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. PUBMED:9748275 EPMC:9748275

  4. Schwenkert S, Netz DJ, Frazzon J, Pierik AJ, Bill E, Gross J, Lill R, Meurer J;, Biochem J. 2009;425:207-214.: Chloroplast HCF101 is a scaffold protein for [4Fe-4S] cluster assembly. PUBMED:19817716 EPMC:19817716

  5. Mashruwala AA, Bhatt S, Poudel S, Boyd ES, Boyd JM;, PLoS Genet. 2016;12:e1006233.: The DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureus. PUBMED:27517714 EPMC:27517714


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002744

This domain (previously known as DUF59) is found in proteins that are mostly defined as members of the MIP18 family. This includes iron-sulfur cluster carrier proteins, where the domain is found in the N terminus. This domain is also found in protein AE7 from Arabidopsis and its homologues. Protein AE7 is thought to be a central member of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) pathway, however protein AE7-like 1 and 2 (also containing this domain) are probably not involved in this pathway [ PUBMED:23104832 ]. MIP18 family protein YHR122W (CIA2) from S. cerevisiae is a component of the CIA machinery, and acts at a late step of Fe-S cluster assembly [ PUBMED:22678362 ]. The SufT protein from Staphylococcus aureus is composed of this domain solely and is involved in the maturation of FeS proteins [ PUBMED:27517714 ].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan NifU (CL0232), which has the following description:

This clan includes the C-terminal domain of NifU as well as a large family of uncharacterised domains.

The clan contains the following 2 members:

FeS_assembly_P NifU

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(39)
Full
(16223)
Representative proteomes UniProt
(66791)
RP15
(2037)
RP35
(7426)
RP55
(16402)
RP75
(27653)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(39)
Full
(16223)
Representative proteomes UniProt
(66791)
RP15
(2037)
RP35
(7426)
RP55
(16402)
RP75
(27653)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(39)
Full
(16223)
Representative proteomes UniProt
(66791)
RP15
(2037)
RP35
(7426)
RP55
(16402)
RP75
(27653)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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's seed alignment. 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 alignment.

Note: You can also download the data file for the tree.

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 View help on the curation process

Seed source: Enright A
Previous IDs: DUF59; Iron-sulfur;
Type: Domain
Sequence Ontology: SO:0000417
Author: Enright A , Ouzounis C , Bateman A , Eberhardt R
Number in seed: 39
Number in full: 16223
Average length of the domain: 74.6 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 32.25 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.5 23.5
Trusted cut-off 23.5 23.5
Noise cut-off 23.4 23.4
Model length: 75
Family (HMM) version: 22
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Structures

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 FeS_assembly_P domain has been found. There are 30 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044VB20 View 3D Structure Click here
A0A077Z0I0 View 3D Structure Click here
A0A0D2GZ66 View 3D Structure Click here
A0A0H3GMJ6 View 3D Structure Click here
A0A0K0JDA0 View 3D Structure Click here
A0A158Q649 View 3D Structure Click here
A0A175VX41 View 3D Structure Click here
A0A1C1CEH8 View 3D Structure Click here
A0A1D6E0U5 View 3D Structure Click here
A0A1D6EFP7 View 3D Structure Click here
A0A1D6JDE4 View 3D Structure Click here
A0A2R8RVQ7 View 3D Structure Click here
A0A368UJC9 View 3D Structure Click here
A0A3P7DJ51 View 3D Structure Click here
A4HTC5 View 3D Structure Click here
A8MR89 View 3D Structure Click here
C0NNR2 View 3D Structure Click here
C1HA55 View 3D Structure Click here
D3Z8Q7 View 3D Structure Click here
G4VKB5 View 3D Structure Click here
I1J4N8 View 3D Structure Click here
I1J8W2 View 3D Structure Click here
I1L4F4 View 3D Structure Click here
I1LHS1 View 3D Structure Click here
K0EUM7 View 3D Structure Click here
K0FC22 View 3D Structure Click here
K7LF51 View 3D Structure Click here
O24999 View 3D Structure Click here
O53157 View 3D Structure Click here
O62252 View 3D Structure Click here
P38829 View 3D Structure Click here
P53382 View 3D Structure Click here
P53383 View 3D Structure Click here
P70949 View 3D Structure Click here
P76080 View 3D Structure Click here
P9WJN7 View 3D Structure Click here
Q0JAJ1 View 3D Structure Click here
Q0JJS8 View 3D Structure Click here
Q0P822 View 3D Structure Click here
Q2FZT0 View 3D Structure Click here