Difference between revisions of "Phosphatase Subfamily LHPP"

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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_LHPP|Subfamily LHPP]]
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_LHPP|Subfamily LHPP]]
  
LHPP is a protein histidine phosphatase conserved in holozoan.
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LHPP is a protein histidine phosphatase, similar to [[Phosphatase_Subfamily_PHP|PHP]]
  
 
=== Evolution ===
 
=== Evolution ===
LHPP is found across [[holozoa]]. Distinct HDHD2 and LHPP genes are found as single copies in most animals, though Drosophila lacks LHPP and Sea Urchin has a HDHD2 pseudogene with frameshift. Several fungi and oomycetes also have HDHD2-like genes. HDHD2-like genes are also found in a small number of bacteria.
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Two clear subsets of this subfamily are seen across eumetazoa: LHPP (lysine histidine pyrophosphate phosphatase) and HDHD2 (Haloacid Dehalogenase-like Hydrolase Domain containing 2). Distinct HDHD2 and LHPP genes are found as single copies in most animals, though Drosophila lacks LHPP and sea urchin has an additional HDHD2 pseudogene <cite>Chen</cite>. A HDHD2 homolog is seen in other holozoa, and very similar genes are seen fungi (but lost in ascomycetes), in a few algae and in both bacteria and archaea.
  
 
=== Domain ===
 
=== Domain ===
LHPP subfamily has a single domain, HAD domain.
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LHPP proteins consist of a twin HAD domains, from different subfamilies (Hydrolase_6 and Hydolase_like in Pfam), part of the IIA subfamily of HAD superfamily hydrolases. A number of structure are available from the structural genomics consortium, but have not been analyzed for publication.
  
 
=== Function ===
 
=== Function ===
LHPP (lysine histidine pyrophosphate phosphatase) from cow was shown to dephosphorylate succinic thiokinase and nucleoside diphosphate kinase autophosphorylated at His residues. LHPP also has activity against free phospho-lysine and phospho-histidine amino acids  <cite>Hiraishi</cite>.  
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LHPP from cow was shown to dephosphorylate succinic thiokinase and nucleoside diphosphate kinase autophosphorylated at His residues. LHPP also has activity against free phospho-lysine and phospho-histidine amino acids  <cite>Hiraishi</cite>.
HDHD2 (Haloacid Dehalogenase-like Hydrolase Domain containing 2) is found in most animals but has not been experimentally studied.
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HDHD2 has not been experimentally studied in any species.
  
 
=== References ===
 
=== References ===
 
<biblio>
 
<biblio>
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#Chen pmid=28400531
 
#Hiraishi pmid=10423531
 
#Hiraishi pmid=10423531
 
</biblio>
 
</biblio>

Latest revision as of 05:49, 24 July 2017

Phosphatase Classification: Fold HAD: Superfamily HAD: Family NagD: Subfamily LHPP

LHPP is a protein histidine phosphatase, similar to PHP

Evolution

Two clear subsets of this subfamily are seen across eumetazoa: LHPP (lysine histidine pyrophosphate phosphatase) and HDHD2 (Haloacid Dehalogenase-like Hydrolase Domain containing 2). Distinct HDHD2 and LHPP genes are found as single copies in most animals, though Drosophila lacks LHPP and sea urchin has an additional HDHD2 pseudogene [1]. A HDHD2 homolog is seen in other holozoa, and very similar genes are seen fungi (but lost in ascomycetes), in a few algae and in both bacteria and archaea.

Domain

LHPP proteins consist of a twin HAD domains, from different subfamilies (Hydrolase_6 and Hydolase_like in Pfam), part of the IIA subfamily of HAD superfamily hydrolases. A number of structure are available from the structural genomics consortium, but have not been analyzed for publication.

Function

LHPP from cow was shown to dephosphorylate succinic thiokinase and nucleoside diphosphate kinase autophosphorylated at His residues. LHPP also has activity against free phospho-lysine and phospho-histidine amino acids [2].

HDHD2 has not been experimentally studied in any species.

References

  1. Chen MJ, Dixon JE, and Manning G. Genomics and evolution of protein phosphatases. Sci Signal. 2017 Apr 11;10(474). DOI:10.1126/scisignal.aag1796 | PubMed ID:28400531 | HubMed [Chen]
  2. Hiraishi H, Yokoi F, and Kumon A. Bovine liver phosphoamidase as a protein histidine/lysine phosphatase. J Biochem. 1999 Aug;126(2):368-74. DOI:10.1093/oxfordjournals.jbchem.a022459 | PubMed ID:10423531 | HubMed [Hiraishi]
All Medline abstracts: PubMed | HubMed