PROSITE documentation PDOC00136

Acylphosphatase-like domain signatures and profile

Description

Acylphosphatase (EC 3.6.1.7) [1,2] catalyzes the hydrolysis of various acyl phosphate carboxyl-phosphate bonds such as carbamyl phosphate, succinyl phosphate, 1,3-diphosphoglycerate, etc. The physiological role of this enzyme is not yet clear. Acylphosphatase is a small protein of around 100 amino-acid residues. Two different isoenzymes are expressed in mammalian tissues: muscle type (MT) acylphosphatase is prevalently found in the skeletal muscle and heart, whereas the organ common type (CT) acylphosphatase is expressed in erythrocytes, brain and testis.

While acylphosphatase have been so far only characterized in vertebrates, there are a number of bacterial and archebacterial hypothetical proteins that are highly similar to that enzyme and that probably possess the same activity. These proteins are:

  • Escherichia coli probable acylphosphatase yccX.
  • Bacillus subtilis probable acylphosphatase yflL.
  • Archaeoglobus fulgidus probable acylphosphatase AF0818.

An acylphosphatase-like domain is also found in the N-terminus of prokaryotic hydrogenase maturation protein hypF [3,4].

The acylphosphatase-like domain forms a compact, pear-shaped, stucture (see <PDB:2ACY>). It has a globular α/β fold, consisting of a β sheet with five antiparallel strands and two α helices packed parallel on the same side of the sheet, forming an α/β sandwich protein. The acylphosphatase-like domain is stabilized by intramolecular contacts of the two antiparallel amphipatic α-helices, which pack their hydrophobic residues against the inner face of the β-sheet, leaving no core cavities in the proteins structure [4,5].

As signature patterns, we selected two conserved regions. The first is located in the N-terminal section, while the second is found in the central part of the protein sequence. We also developed a profile that covers the entire acylphosphatase-like domain.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

ACYLPHOSPHATASE_3, PS51160; Acylphosphatase-like domain profile  (MATRIX)
Sequences known to belong to this class detected by the profile: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Domain architecture view of Swiss-Prot proteins matching PS51160
PS51160
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51160
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51160
• Scan Swiss-Prot/TrEMBL entries against PS51160
• view ligand binding statistics
Matching PDB structures: 1APS 1GXT 1GXU 1ULR ... [ALL]
ACYLPHOSPHATASE_1, PS00150; Acylphosphatase signature 1  (PATTERN)
Consensus pattern: [LIV]-x-G-x-V-Q-[GH]-V-x-[FM]-R
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00150
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00150
• Scan Swiss-Prot/TrEMBL entries against PS00150
• view ligand binding statistics
Matching PDB structures: 1APS 1GXT 1GXU 1URR ... [ALL]
ACYLPHOSPHATASE_2, PS00151; Acylphosphatase signature 2  (PATTERN)
Consensus pattern: G-[FYW]-[AVC]-[KRQAM]-N-x(3)-G-x-V-x(5)-G
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00151
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00151
• Scan Swiss-Prot/TrEMBL entries against PS00151
• view ligand binding statistics
Matching PDB structures: 1APS 1V3Z 1W2I 1Y9O ... [ALL]

References

1 Authors Stefani M., Ramponi G.
Title Acylphosphate phosphohydrolases.
Source Life Chem. Rep. 12:271-301(1995).
2 Authors Stefani M., Taddei N., Ramponi G.
Title Insights into acylphosphatase structure and catalytic mechanism.
Source Cell. Mol. Life Sci. 53:141-151(1997).
PubMed ID 9118002
3 Authors Wolf I., Buhrke T., Dernedde J., Pohlmann A., Friedrich B.
Title Duplication of hyp genes involved in maturation of [NiFe] hydrogenases in Alcaligenes eutrophus H16.
Source Arch. Microbiol. 170:451-459(1998).
PubMed ID 9799289
4 Authors Rosano C., Zuccotti S., Bucciantini M., Stefani M., Ramponi G., Bolognesi M.
Title Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain.
Source J. Mol. Biol. 321:785-796(2002).
PubMed ID 12206761
5 Authors Thunnissen M.M.G.M., Taddei N., Liguri G., Ramponi G., Nordlund P.
Title Crystal structure of common type acylphosphatase from bovine testis.
Source Structure 5:69-79(1997).
PubMed ID 9016712

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