Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
18  structures 794  species 4  interactions 798  sequences 2  architectures

Family: Fumarate_red_C (PF02300)

Summary: Fumarate reductase subunit C

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Fumarate reductase". More...

Fumarate reductase Edit Wikipedia article

Fumarate reductase respiratory complex
PDB 2bs3 EBI.jpg
Structure of Quinol-Fumarate Reductase Flavoprotein Subunit A.[1]
Identifiers
Symbol Fum_red_TM
Pfam PF01127
Pfam clan CL0335
InterPro IPR004224
SCOP 1qla
SUPERFAMILY 1qla
OPM superfamily 3
OPM protein 2bs3
CDD cd03494
Fumarate reductase subunit C
PDB 1l0v EBI.jpg
quinol-fumarate reductase with menaquinol molecules
Identifiers
Symbol Fumarate_red_C
Pfam PF02300
Pfam clan CL0335
InterPro IPR003510
SCOP 1fum
SUPERFAMILY 1fum
CDD cd00546
Fumarate reductase subunit D
PDB 1kfy EBI.jpg
quinol-fumarate reductase with quinol inhibitor 2-[1-(4-chloro-phenyl)-ethyl]-4,6-dinitro-phenol
Identifiers
Symbol Fumarate_red_D
Pfam PF02313
Pfam clan CL0335
InterPro IPR003418
SCOP 1fum
SUPERFAMILY 1fum
CDD cd00547

Fumarate reductase is the enzyme that converts fumarate to succinate, and is important in microbial metabolism as a part of anaerobic respiration.[2]

Succinate + acceptor <=> fumarate + reduced acceptor

In other words, fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase).[3]

Fumarate reductase complex includes three subunits. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules.[3] The D subunit may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.

See also

References

  1. ^ Lancaster CR, Sauer US, Gross R, et al. (December 2005). "Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase". Proc. Natl. Acad. Sci. U.S.A. 102 (52): 18860–5. doi:10.1073/pnas.0509711102. PMC 1323215. PMID 16380425. 
  2. ^ Iverson TM, Luna-Chavez C, Cecchini G, Rees DC (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex". Science 284 (5422): 1961–6. doi:10.1126/science.284.5422.1961. PMID 10373108. 
  3. ^ a b Michel H, Lancaster CR, Kroger A, Auer M (1999). "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution". Nature 402 (6760): 377–385. doi:10.1038/46483. PMID 10586875. 

External links

This article incorporates text from the public domain Pfam and InterPro IPR004224

This article incorporates text from the public domain Pfam and InterPro IPR003510

This article incorporates text from the public domain Pfam and InterPro IPR003418

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Fumarate reductase subunit C Provide feedback

Fumarate reductase is a membrane-bound flavoenzyme consisting of four subunits, A-B. A and B comprise the membrane-extrinsic catalytic domain and C and D link the catalytic centres to the electron-transport chain. This family consists of the 15kD hydrophobic subunit C.

Literature references

  1. Cole ST; , Eur J Biochem 1987;167:481-488.: Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris. Extensive sequence divergence of the membrane anchors and absence of an frd-linked ampC cephalosporinase gene. PUBMED:3308458 EPMC:3308458


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003510

Fumarate reductase is a membrane-bound flavoenzyme consisting of four subunits, A-B. A and B comprise the membrane-extrinsic catalytic domain and C and D link the catalytic centres to the electron-transport chain. This family consists of the 15kDa hydrophobic subunit C.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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

Loading domain graphics...

Pfam Clan

This family is a member of clan FumRed-TM (CL0335), which has the following description:

This superfamily constitutes two distinct families: in one family the common fold is contained in a single-chain subunit, in the other it is formed by two chains.

The clan contains the following 5 members:

CybS DUF1691 Fumarate_red_C Fumarate_red_D Sdh_cyt

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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
(23)
Full
(798)
Representative proteomes NCBI
(276)
Meta
(17)
RP15
(8)
RP35
(27)
RP55
(50)
RP75
(71)
Jalview View  View  View  View  View  View  View  View 
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

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

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

Format an alignment

  Seed
(23)
Full
(798)
Representative proteomes NCBI
(276)
Meta
(17)
RP15
(8)
RP35
(27)
RP55
(50)
RP75
(71)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

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
(23)
Full
(798)
Representative proteomes NCBI
(276)
Meta
(17)
RP15
(8)
RP35
(27)
RP55
(50)
RP75
(71)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   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.

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 HMMER3.

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: Pfam-B_11568 (release 5.2)
Previous IDs: none
Type: Domain
Author: Mian N, Bateman A
Number in seed: 23
Number in full: 798
Average length of the domain: 127.10 aa
Average identity of full alignment: 62 %
Average coverage of the sequence by the domain: 97.67 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.5 22.5
Trusted cut-off 22.7 22.6
Noise cut-off 22.1 22.2
Model length: 129
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

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...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Interactions

There are 4 interactions for this family. More...

Fumarate_red_D FAD_binding_2 Succ_DH_flav_C Fer4

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 Fumarate_red_C domain has been found. There are 18 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 seqence.

Loading structure mapping...