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.
83  structures 5363  species 0  interactions 8160  sequences 72  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

EC number3.6.1.7
CAS number9012-34-4
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
PDB 1aps EBI.jpg
Structure of acylphosphatase.[2]

In enzymology, an acylphosphatase (EC is an enzyme that catalyzes the following chemical reaction:[3]

The chemical reaction catalyzed by acylphosphatase enzymes.

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:

Structural studies

Structures of this enzyme have been solved by both NMR and X-ray crystallography. See the links to PDB structures in the info boxes on the right for a current list of structures available in the PDB. The protein contains a beta sheet stacked on two alpha helices described by CATH as an Alpha-Beta Plait fold. The active site sits between sheet and helices and contains an arginine and an asparagine.[4] Most structures are monomeric [5]


Humans express the following two acylphosphatase isozymes:

acylphosphatase 1, erythrocyte (common) type
NCBI gene97
Other data
EC number3.6.1.7
LocusChr. 14 q24.3
acylphosphatase 2, muscle type
NCBI gene98
Other data
EC number3.6.1.7
LocusChr. 2 p16.2


  1. ^ "RCSB Protein Data Bank - Structure Summary for 2W4P - HUMAN COMMON-TYPE ACYLPHOSPHATASE VARIANT, A99G".
  2. ^ Pastore A, Saudek V, Ramponi G, Williams RJ (March 1992). "Three-dimensional structure of acylphosphatase. Refinement and structure analysis". J. Mol. Biol. 224 (2): 427–40. doi:10.1016/0022-2836(92)91005-A. PMID 1313885.
  3. ^ Stefani M, Taddei N, Ramponi G (February 1997). "Insights into acylphosphatase structure and catalytic mechanism". Cell. Mol. Life Sci. 53 (2): 141–51. doi:10.1007/PL00000585. PMID 9118002.
  4. ^ Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI (February 2009). "Rational stabilization of enzymes by computational redesign of surface charge-charge interactions". Proceedings of the National Academy of Sciences of the United States of America. 106 (8): 2601–6. doi:10.1073/pnas.0808220106. PMC 2650310. PMID 19196981.
  5. ^ "Enzyme". PDBe Enzyme Browser.

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...

Loading domain graphics...

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
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

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

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

Format an alignment

Representative proteomes UniProt

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.

Representative proteomes UniProt
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...


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: 8160
Average length of the domain: 83.70 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 30.54 %

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 22.5 22.5
Trusted cut-off 22.6 22.5
Noise cut-off 22.4 22.4
Model length: 85
Family (HMM) version: 20
Download: download the raw HMM for this family

Species distribution

Sunburst controls


Weight segments by...

Change the size of the sunburst


Colour assignments

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


Align selected sequences to HMM

Generate a FASTA-format file

Clear selection

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


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


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.


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 83 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.

Loading structure mapping...