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85  structures 5526  species 0  interactions 8678  sequences 78  architectures

Family: Acylphosphatase (PF00708)

Summary: Acylphosphatase

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 "Acylphosphatase". More...

Acylphosphatase Edit Wikipedia article

In enzymology, an acylphosphatase (EC is an enzyme that catalyzes the chemical reaction

an acylphosphate + H2O a carboxylate + phosphate

Thus, the two substrates of this enzyme are acylphosphate and H2O, whereas its two products are carboxylate and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is acylphosphate phosphohydrolase. Other names in common use include acetylphosphatase, 1,3-diphosphoglycerate phosphatase, acetic phosphatase, Ho 1-3, and GP 1-3. This enzyme participates in 3 metabolic pathways: glycolysis / gluconeogenesis, pyruvate metabolism, and benzoate degradation via coa ligation.

Structural studies

As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1APS, 1ULR, 1URR, 1V3Z, 1W2I, 1Y9O, 2ACY, 2BJD, 2BJE, 2FHM, 2GV1, 2HLT, and 2HLU.


Template:Enzyme references

  • Raijman L, Grisolia S and Edelhoch H (1960). "Further purification and properties of brain acyl phosphatase". J. Biol. Chem. 235: 2340–2342.
  • Ramponi G, Guerritore A, Treves C, Nassi P, Baccari V (1969). "Horse muscle acyl phosphatase: purification and some properties". Arch. Biochem. Biophys. 130: 362–9. PMID 4305161.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Ramponi G, Nassi P, Cappugi G, Treves C, Manao G (1972). "Purification and some molecular properties of horse liver acyl phosphatase". Biochim. Biophys. Acta. 284: 485–96. PMID 4344156.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Shiokawa H, Noda L (1970). "Isolation and crystallization of acyl phosphatase from rabbit muscle". J. Biol. Chem. 245: 669–73. PMID 4313603.

External links

The CAS registry number for this enzyme class is Template:CAS registry.

Template:Enzyme links

Gene Ontology (GO) codes

Template:GO code links

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.

Acylphosphatase Provide feedback

No Pfam abstract.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001792

Acylphosphatase ( EC ) is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [ PUBMED:1664426 ], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [ PUBMED:2538623 ]. The enzyme has a mainly beta-sheet structure with 2 short alpha-helical segments. It is distributed in a tissue-specific manner in a wide variety of species, although its physiological role is as yet unknown [ PUBMED:2538623 ]: it may, however, play a part in the regulation of the glycolytic pathway and pyrimidine biosynthesis [ PUBMED:2830253 ]. There are two known isozymes. One seems to be specific to muscular tissues, the other, called 'organ-common type', is found in many different tissues. A number of bacterial and archebacterial hypothetical proteins are highly similar to that enzyme and that probably possess the same activity.

An acylphosphatase-like domain is also found in some prokaryotic hydrogenase maturation HypF carbamoyltransferases [ PUBMED:9799289 , PUBMED:12206761 ].

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 Acylphosphatase (CL0622), which has the following description:

This superfamily has a ferredoxin fold. It contains the BLUF domain and the acylphosphatase family.

The clan contains the following 4 members:

Acylphosphatase BLUF DUF1115 UPF0176_N


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.

Representative proteomes UniProt
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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.

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Representative proteomes UniProt

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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.

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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...


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_686 (release 2.1)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 43
Number in full: 8678
Average length of the domain: 83.7 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 30.96 %

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 22.5 22.5
Trusted cut-off 22.6 22.5
Noise cut-off 22.4 22.4
Model length: 85
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Colour assignments

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


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


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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 Acylphosphatase domain has been found. There are 85 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
A0A077Z9X3 View 3D Structure Click here
A0A0D2EWT8 View 3D Structure Click here
A0A0H3GL55 View 3D Structure Click here
A0A0H3GUB8 View 3D Structure Click here
A0A146MJ81 View 3D Structure Click here
A0A1C1CYF0 View 3D Structure Click here
A0A1D6NY72 View 3D Structure Click here
A0A5K4F8I2 View 3D Structure Click here
A0B571 View 3D Structure Click here
A0JTE5 View 3D Structure Click here
A0KKF3 View 3D Structure Click here
A0LI66 View 3D Structure Click here
A0LV84 View 3D Structure Click here
A0QV24 View 3D Structure Click here
A1A6Q5 View 3D Structure Click here
A1KAG5 View 3D Structure Click here
A1R3U5 View 3D Structure Click here
A1RZ22 View 3D Structure Click here
A1S579 View 3D Structure Click here
A1SPV1 View 3D Structure Click here
A1SWQ8 View 3D Structure Click here
A1T739 View 3D Structure Click here
A1UED9 View 3D Structure Click here
A1VW83 View 3D Structure Click here
A1WDC8 View 3D Structure Click here
A1WUX3 View 3D Structure Click here
A3MYL5 View 3D Structure Click here
A4FMH0 View 3D Structure Click here
A4I1P4 View 3D Structure Click here
A4YHE5 View 3D Structure Click here
A5D1R6 View 3D Structure Click here
A5G1Y9 View 3D Structure Click here
A5GA97 View 3D Structure Click here
A5GM25 View 3D Structure Click here
A5GS00 View 3D Structure Click here
A5UQ40 View 3D Structure Click here
A5VFP2 View 3D Structure Click here
A6T769 View 3D Structure Click here
A6VN24 View 3D Structure Click here
A7H8A3 View 3D Structure Click here