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442  structures 4015  species 0  interactions 6892  sequences 80  architectures

Family: FBPase (PF00316)

Summary: Fructose-1-6-bisphosphatase, N-terminal domain

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 "Fructose 1,6-bisphosphatase". More...

Fructose 1,6-bisphosphatase Edit Wikipedia article

Fructose bisphosphatase is an enzyme in the liver, that converts fructose-1,6-bisphosphate to fructose-6-phosphate in gluconeogenesis (the making of glucose from smaller substrates). Fructose bisphosphatase does the opposite job to phosphofructokinase, and both these enzymes only work in one direction.

Fructose bisphosphatase deficiency

If there is a deficiency in fructose bisphosphatase, gluconeogenesis will not occur correctly. Glycolysis (the break-down of glucose) will still work, as this does not use this enzyme.

Without effective gluconeogenesis (GNG), hypoglycaemia will set in after about 12 hours. This is the time when liver glycogen stores have been exhausted, and the body has to rely on GNG. When given a dose of glucagon (which would normally increase blood glucose) nothing will happen, as stores are depleted and GNG doesn't work. (In fact, the patient would already have high glucagon levels.)

There is no problem with the metabolism of glucose or galactose, but fructose and glycerol cannot be used as fuels. If fructose or glycerol are given, there will be a build up of phophorylated three-carbon sugars. This leads to phosphate depletion within the cells, and also in the blood. Without phosphate, ATP cannot be made, and many cell processes cannot occur.

High levels of glucagon will tend to release fatty acids from adipose tissue, and this will combine with glycerol that cannot be used in the liver, to make triacylglycerides causing a fatty liver.

As three carbon molecules cannot be used to make glucose, the will instead be made into pyruvate and lactate. These acids cause a drop in the pH of the blood (a metabolic acidosis). Acetyl CoA will also build up, leading to the creation of ketone bodies.

To treat people with a deficiency of this enzyme, they must avoid needing gluconeogenesis to make glucose. This can be accomplished by not fasting for long periods, and eating high-carbohydrate food. They should avoid fructose containing foods (as well as sucrose which breaks down to fructose).

As with all single-gene metabolic disorders, there is always hope for genetic therapy, inserting a healthy copy of the gene into the liver.

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.

Fructose-1-6-bisphosphatase, N-terminal domain Provide feedback

This family represents the N-terminus of this protein family.

Literature references

  1. Weeks CM, Roszak AW, Erman M, Kaiser R, Jornvall H, Ghosh D; , Acta Crystallogr D Biol Crystallogr 1999;55:93-102.: Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution. PUBMED:10089399 EPMC:10089399


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR033391

Fructose-1,6-bisphosphatase (FBPase) is a critical regulatory enzyme in gluconeogenesis that catalyses the removal of 1-phosphate from fructose 1,6-bis-phosphate to form fructose 6-phosphate [ PUBMED:2159755 , PUBMED:3008716 ]. Five different classes (or types) of FBPases have been identified based on their amino acid sequences, with class I most widely distributed among living organisms [ PUBMED:16670087 ].

This entry represents the N terminus of the FBPase class 1 family.

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 Phospoesterase (CL0171), which has the following description:

Members of this clan show metal-dependent / lithium sensitive phosphomonoesterase activity. The clan includes inositol polyphosphate 1 phosphatase and fructose 1,6-bisphosphatase [1].

The clan contains the following 3 members:

FBPase FBPase_glpX Inositol_P

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
(7)
Full
(6892)
Representative proteomes UniProt
(23444)
RP15
(1167)
RP35
(3203)
RP55
(6301)
RP75
(10184)
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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
(7)
Full
(6892)
Representative proteomes UniProt
(23444)
RP15
(1167)
RP35
(3203)
RP55
(6301)
RP75
(10184)
Alignment:
Format:
Order:
Sequence:
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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
(7)
Full
(6892)
Representative proteomes UniProt
(23444)
RP15
(1167)
RP35
(3203)
RP55
(6301)
RP75
(10184)
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: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD , Griffiths-Jones SR
Number in seed: 7
Number in full: 6892
Average length of the domain: 179.3 aa
Average identity of full alignment: 40 %
Average coverage of the sequence by the domain: 52.83 %

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 34.8 34.8
Trusted cut-off 34.9 34.9
Noise cut-off 34.3 34.7
Model length: 191
Family (HMM) version: 23
Download: download the raw HMM for this family

Species distribution

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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 FBPase domain has been found. There are 442 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
A0A044TCB2 View 3D Structure Click here
A0A077Z8N6 View 3D Structure Click here
A0A077ZFV1 View 3D Structure Click here
A0A0D2EU40 View 3D Structure Click here
A0A0H3GMG0 View 3D Structure Click here
A0A0H5S425 View 3D Structure Click here
A0A0K0ESQ9 View 3D Structure Click here
A0A0P0WMW5 View 3D Structure Click here
A0A0R0EC38 View 3D Structure Click here
A0A0R0G4G2 View 3D Structure Click here
A0A0R0HVD4 View 3D Structure Click here
A0A0R0J4T8 View 3D Structure Click here
A0A0R4J3Q0 View 3D Structure Click here
A0A0R4J5J8 View 3D Structure Click here
A0A0U1RVK6 View 3D Structure Click here
A0A158Q5R9 View 3D Structure Click here
A0A175VQH1 View 3D Structure Click here
A0A175VVY7 View 3D Structure Click here
A0A1C1C6J1 View 3D Structure Click here
A0A1D6JXJ7 View 3D Structure Click here
A0A1D6N6G5 View 3D Structure Click here
A0A1D6N713 View 3D Structure Click here
A0A1D8PKW2 View 3D Structure Click here
A0KJT2 View 3D Structure Click here
A1APW8 View 3D Structure Click here
A1B2P8 View 3D Structure Click here
A1BEB4 View 3D Structure Click here
A1K430 View 3D Structure Click here
A1S351 View 3D Structure Click here
A1T0H3 View 3D Structure Click here
A1TN89 View 3D Structure Click here
A1VL56 View 3D Structure Click here
A1VNR3 View 3D Structure Click here
A1W9H6 View 3D Structure Click here
A1WH14 View 3D Structure Click here
A1WZH0 View 3D Structure Click here
A2SFV4 View 3D Structure Click here
A2SJJ0 View 3D Structure Click here
A2SJK3 View 3D Structure Click here
A2ST39 View 3D Structure Click here