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245  structures 5666  species 0  interactions 17112  sequences 232  architectures

Family: FMN_dh (PF01070)

Summary: FMN-dependent dehydrogenase

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

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

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.

FMN-dependent dehydrogenase Provide feedback

No Pfam abstract.

Literature references

  1. Lindqvist Y; , J Mol Biol 1989;209:151-166.: Refined structure of spinach glycolate oxidase at 2 A resolution. PUBMED:2681790 EPMC:2681790

  2. Xia ZX, Mathews FS; , J Mol Biol 1990;212:837-863.: Molecular structure of flavocytochrome b2 at 2.4 A resolution. PUBMED:2329585 EPMC:2329585


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000262

A number of oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins have been shown [ PUBMED:2324094 , PUBMED:2271624 , PUBMED:1939137 ] to be structurally related. These enzymes are:

  • Lactate dehydrogenase ( EC ), which consists of a dehydrogenase domain and a haem-binding domain called cytochrome b2 and which catalyses the conversion of lactate into pyruvate.
  • Glycolate oxidase ( EC ) ((S)-2-hydroxy-acid oxidase), a peroxisomal enzyme that catalyses the conversion of glycolate and oxygen to glyoxylate and hydrogen peroxide.
  • Long chain alpha-hydroxy acid oxidase from rat ( EC ), a peroxisomal enzyme.
  • Lactate 2-monooxygenase ( EC ) (lactate oxidase) from Mycobacterium smegmatis, which catalyses the conversion of lactate and oxygen to acetate, carbon dioxide and water.
  • (S)-mandelate dehydrogenase from Pseudomonas putida (gene mdlB), which catalyses the reduction of (S)-mandelate to benzoylformate.

The first step in the reaction mechanism of these enzymes is the abstraction of the proton from the alpha-carbon of the substrate producing a carbanion which can subsequently attach to the N5 atom of FMN. A conserved histidine has been shown [ PUBMED:2644287 ] to be involved in the removal of the proton. The region around this active site residue is highly conserved and contains an arginine residue which is involved in substrate binding.

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...

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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
(173)
Full
(17112)
Representative proteomes UniProt
(59248)
RP15
(1900)
RP35
(7224)
RP55
(14891)
RP75
(25121)
Jalview View  View  View  View  View  View  View 
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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
(173)
Full
(17112)
Representative proteomes UniProt
(59248)
RP15
(1900)
RP35
(7224)
RP55
(14891)
RP75
(25121)
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
(173)
Full
(17112)
Representative proteomes UniProt
(59248)
RP15
(1900)
RP35
(7224)
RP55
(14891)
RP75
(25121)
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: Pfam-B_829 (release 3.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD , Bateman A
Number in seed: 173
Number in full: 17112
Average length of the domain: 292.80 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 81.97 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.9 24.9
Trusted cut-off 24.9 24.9
Noise cut-off 24.8 24.8
Model length: 348
Family (HMM) version: 20
Download: download the raw HMM for this family

Species distribution

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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 FMN_dh domain has been found. There are 245 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
A0A0R0HEQ1 View 3D Structure Click here
A0A0R0IJK4 View 3D Structure Click here
A0A0R0IJK4 View 3D Structure Click here
A0A0R0IJM4 View 3D Structure Click here
A0A0R0IJM4 View 3D Structure Click here
A0A0R0IPJ7 View 3D Structure Click here
A0A0R0IU91 View 3D Structure Click here
A0A1D6DYT6 View 3D Structure Click here
A0A1D6DYT6 View 3D Structure Click here
A0A1D6DYU9 View 3D Structure Click here
A0A1D6F1Q0 View 3D Structure Click here
A0A1D6F1Q0 View 3D Structure Click here
A0A1D6HSJ1 View 3D Structure Click here
A0A1D6HSJ1 View 3D Structure Click here
A0A1D6IVF6 View 3D Structure Click here
A0A1D6IYR2 View 3D Structure Click here
A1Z8D3 View 3D Structure Click here
A4IC51 View 3D Structure Click here
A4IC51 View 3D Structure Click here
B0BNF9 View 3D Structure Click here
B0M1B1 View 3D Structure Click here
B1GRK5 View 3D Structure Click here
C7J5K1 View 3D Structure Click here
F1QCD8 View 3D Structure Click here
I1K3F6 View 3D Structure Click here
I1KRU6 View 3D Structure Click here
I1KRV0 View 3D Structure Click here
I1MJ29 View 3D Structure Click here
K7DY73 View 3D Structure Click here
K7KQ62 View 3D Structure Click here
O49506 View 3D Structure Click here
P00175 View 3D Structure Click here
P33232 View 3D Structure Click here
P9WND5 View 3D Structure Click here
P9WND7 View 3D Structure Click here
Q07523 View 3D Structure Click here
Q10CE4 View 3D Structure Click here
Q24JJ8 View 3D Structure Click here
Q2FVR9 View 3D Structure Click here
Q4CLD8 View 3D Structure Click here
Q4D572 View 3D Structure Click here
Q4DXZ1 View 3D Structure Click here
Q54E41 View 3D Structure Click here
Q58272 View 3D Structure Click here
Q5AKX8 View 3D Structure Click here
Q6YT73 View 3D Structure Click here
Q7FAS1 View 3D Structure Click here
Q7XPR4 View 3D Structure Click here
Q8H3I4 View 3D Structure Click here
Q9HDX2 View 3D Structure Click here
Q9LJH5 View 3D Structure Click here
Q9LRR9 View 3D Structure Click here
Q9LRS0 View 3D Structure Click here
Q9NYQ2 View 3D Structure Click here
Q9NYQ3 View 3D Structure Click here
Q9UJM8 View 3D Structure Click here
Q9WU19 View 3D Structure Click here