Summary: Acylphosphatase
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This is the Wikipedia entry entitled "Acylphosphatase". More...
Acylphosphatase Edit Wikipedia article
In enzymology, an acylphosphatase (EC 3.6.1.7) 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.
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.
Gene Ontology (GO) codes
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.
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No Pfam abstract.
Internal database links
Similarity to PfamA using HHSearch: | UPF0176_N |
External database links
HOMSTRAD: | acyo |
PROSITE: | PDOC00136 |
SCOP: | 1aps |
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_NAlignments
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...
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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.
Seed (43) |
Full (8678) |
Representative proteomes | UniProt (40955) |
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RP15 (1283) |
RP35 (4047) |
RP55 (8440) |
RP75 (14172) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (43) |
Full (8678) |
Representative proteomes | UniProt (40955) |
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RP15 (1283) |
RP35 (4047) |
RP55 (8440) |
RP75 (14172) |
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Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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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.
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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
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
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 85 | ||||||||||||
Family (HMM) version: | 21 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 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.