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70  structures 15285  species 3  interactions 19718  sequences 43  architectures

Family: Acylphosphatase (PF00708)

Summary: Acylphosphatase

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This is the Wikipedia entry entitled "Acylphosphatase". More...

Acylphosphatase Edit Wikipedia article

EC number
CAS number 9012-34-4
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
PDB 1aps EBI.jpg
Structure of acylphosphatase. [2]
Symbol Acylphosphatase
Pfam PF00708
InterPro IPR001792
SCOP 1aps

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
Symbol ACYP1
Entrez 97
HUGO 179
OMIM 600875
RefSeq NM_001107
UniProt P07311
Other data
EC number
Locus Chr. 14 q24.3
acylphosphatase 2, muscle type
Symbol ACYP2
Entrez 98
HUGO 180
OMIM 102595
RefSeq NM_138448
UniProt P14621
Other data
EC number
Locus Chr. 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. ^ Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. Gribenko et al PNAS 2009. PMID 19196981.
  5. ^ PDBe Enzyme Browser.

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

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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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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...

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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.

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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.

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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
Author: Bateman A
Number in seed: 54
Number in full: 19718
Average length of the domain: 89.80 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 35.74 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.5 22.5
Trusted cut-off 22.5 22.5
Noise cut-off 22.4 22.4
Model length: 90
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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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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There are 3 interactions for this family. More...

Sua5_yciO_yrdC zf-HYPF Acylphosphatase


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 70 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.

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