Function for haloacid dehalogenase-like hydrolase domain containing 2
Haloacid dehalogenase-like hydrolase domain containing 2 (2HO4:A,B)
Where's does the name come from?
Hydolase indicates this protein's main molecular function, hydrolase activity. /Link
Definition of hydrolase activity:
Catalysis of the hydrolysis of various bonds
e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
Hydolysis is a breakdown process of compounds in the body,
by replace the covalent bond with water molecule and making the product more water soluble.
Domain containing 2
Domain containing 2 are illustrating it has 2 domains.
Sequence and Secondary Structure /Link
From the above diagram, two domains are showed separately and color in blue and purple.
Type: polypeptide(L)
Length: 259 residues
Secondary Structure: 44% helical (14 helices; 123 residues) 17% beta sheet (12 strands; 48 residues)
2HO4Aa: pdp domain 2HO4Aa (in purple)
2HO4Ab: pdp domain 2HO4Ab (in blue)
What does it mean when protein with 2 domains?
It could either be 2 binding site?
Or, more than one type of molecular function?
Mouse Genome Informatics(MGI)
Gene Ontology Classifications /Link
We found 5 Category of Function or Process with evidence in this protein.
GO Annotations in Tabular Form
Category | Classification | Term Evidence | Inferred From | Ref(s) |
---|---|---|---|---|
Molecular Function | catalytic activity | IEA | InterPro:IPR005834 | J:72247 |
Molecular Function | hydrolase activity | IEA | InterPro:IPR006357 | J:72247 |
Molecular Function | hydrolase activity | IEA | SP_KW:KW-0378 | J:60000 |
Molecular Function | magnesium ion binding | IEA | SP_KW:KW-0460 | J:60000 |
Biological Process | metabolic process | IEA | InterPro:IPR005834,InterPro:IPR006357 | J:72247 |
Gene Ontology Evidence Code Abbreviations: IC Inferred by curator IDA Inferred from direct assay IEA Inferred from electronic annotation IGI Inferred from genetic interaction IMP Inferred from mutant phenotype IPI Inferred from physical interaction ISS Inferred from sequence or structural similarity NAS Non-traceable author statement ND No biological data available RCA Reviewed computational analysis TAS Traceable author statement
So where's the evidence from?
The evidence was done by Mammalian Orthology Load, which the information was derived from Homologene National Center for Biotechnology Information. This protein was reviewed in 2004 and record with J Number: J:90500.
The Mammalian Orthology Query Result shows the Orthology Evidence were used both Amino acid sequence comparison and NT Nucleotide sequence comparison. With species of human, mouse(laboratory), rat, chimpanzee and dog(domestic) all has the sequence of this protein.
Protein Data Bank (PDB)
Ligands and Prosthetic Groups
ID | Name Chemical | Formula | Weight Ligand | Link |
---|---|---|---|---|
PO4 | Phosphate Ion | O4 P 3- | 94.971 | /View |
MG | Magnesium Ion | Mg 2+ | 24.305 | /View |
MSE | Selenomethionine | C5 H11 N O2 Se | 196.107 | /View |
PBD Biology and Chemistry Report /Link
What about it's functional partners
From /STRING uses orthology information from the excellent COG database, we predicted it's functional partners.
From the result of occurrence we discover KIAA0423 annotation, which is still not available (1723 aa) is it best suit predicted Functional Partners. /Link
The above result shows using protein sequence to compare difference species and their .
e.g. Pan troglodytes and Homo sapiens are two species highly conservatity
How does hydrolase activity function?
The HAD (haloacid dehalogenase) superfamily of hydrolases contains enzymes such as L-2-haloacid dehalogenase, epoxide hydrolase and a variety of phosphatases
A research was done in 1979, by administrating chlorpromazine at the rate of 15 milligram per kilogram to rats. By determining mitochondria of the sensomotor cortex and localize Mg-activated ATPase in the cortex, the result shown hydrolase activity increased in the brain after three hours administration. The disscussion suggest the increase of ATP-hydrolase activity in the cortex will induce depression of glycolytic and respiratory activity of the cells. And this is cause by increase of permeability of the mitochndrial membranes. (Kleshchinov et al., 1979)
Genomics Institute of the Novartis Research Foundation
The diagram illustrate the expression of protein or gene in different organisms
Mammalian Orthology Proteins
Literature to read
http://www.springerlink.com/content/mmt8t16q20131540/