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| The predicted function based on the evolution and structure | | The predicted function based on the evolution and structure |
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| | <font size = "4">'''Hydrolase'''</font> |
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| | == Function of sulfatases == |
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| <font size = "4">'''Gene Ontology'''</font>
| | Sulfatases are enzymes,which hydrolyse sulfate ester bonds of substrates. |
| | | Most of the family members has shown to contain a highly conserved cystine residue and a bivalent metal binding site. |
| [[Image:Document17_01.png]]
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| List of all matched protein name terms for 2gfh. The score in red is a measure of how strongly the term is predicted from the hits obtained by
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| the different methods. The scores in blue show each method<nowiki>’</nowiki>s contribution to the total score (with the number of relevant
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| sequences/structures shown in brackets in grey).(http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/)
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| * Higest score in GO - Hydrolase
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| * Followed by - Phosphatase
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| *Polymer: Haloacid dehalogenase-like hydrolase domain containing 4
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| *Molecular Function: None
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| *Biological Process: None
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| *Cellular Component: None
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| <font size = "4">'''Surface Properties'''</font>
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| [[Image:Document7_07.png]]
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| '''Figure 13. (A) '''Molecular structure of 2gfh with the ligand PO<sub>4.</sub>''' (B) '''Molecular and chemical structure of PO<sub>4.</sub>''' (C) '''Ligand interaction involving PO<sub>4.</sub> (Picture adapted from Profunc)
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| * Identify the likely biochemical function from the 3D structure
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| * Possible binding sites and potential ligands - PO<sub>4</sub>
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| * PO<sub>4</sub> most likely be an active site and fuction
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| <font size = "4">'''Phostphatase'''</font>
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| [[Image:Document9_01.png]]
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| MSA of the 2gfh with 35 others proteins. Only the 60<sup>th</sup> – 70<sup>th</sup> and the 210<sup>th</sup> -300<sup>th</sup> amino acid
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| sequence were shown to illustrate the conserved and invariant regions. The 3 boxed-up sequences were either conserved or invariant regions.
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| * 1st - aspartic acid (D)
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| * 2nd - threonine (T), asparagine (N) and glycine (G)
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| * 3rd - lysine (K) and aspartates (D)
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| * MSA corelate with with study done by Maliekal et al
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| **N-acetylneuraminic acid phosphatase orthologs shared 3 motifs found in phosphatases
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| *HAD (Haloacid dehalogenase-like) family
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| ** Phosphatase activity: CO–P bond hydrolysis
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| ** Dehalogenase activity: C–halogen bond hydrolysis
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| ** Phosphonatase: C–P bond hydrolysis
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| ** Phosphoglucomutase: CO–P bond hydrolysis and intramolecular phosphoryl transfer
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| <font size = "4">'''Role in Human'''</font>
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| * OMIM
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| ** Haloacid dehalogenase-like hydrolase domain
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| ** Gene map locus 20p11
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| [[Image:Document2_01.png]]
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| Dephosphorylation of Neu5Ac-9-P is a reversible reaction with an end product of Neu5Ac (sialic acid) and a free phosphate.
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| * Main form of sialic acid in vertebrates
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| ** Important roles in protein-protein and cell-cell recognition
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| ** Dependent on the presence of Mg<sup>2+</sup>
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| ** Inhibited by vanadate and Ca<sup>2+</sup>
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| <font size = "4">'''Role in Bacteria - ''E.coli'''''</font>
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| * Hydrolyze a wide range of phosphorylated metabolites
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| ** Carbohydrates
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| ** Nucleotides,
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| ** Organic acids
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| * Kuznetsova ''et al'' - glycolysis and pentose phosphate pathway
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| ** Fructose-1-phosphate
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| ** Glucose-6-phosphate
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| ** Mannose-6-phosphate
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| ** 2-deoxyglucose-6-phosphate
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| ** Fructose-6- phosphate
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| ** Ribose-5-phosphate
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| ** Erythrose- 4-phosphate
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| [[Image:Document20_01.png]]
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| [[Image:Document20_02.png]]
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| Schematic diagrams of glycolysis and pentose phosphate metabolic pathways. The green arrows show the substrates that are hydrolyzed by HADs (http://www.steve.gb.com/science/core_metabolism.html)
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| [[N-acetylneuraminic acid phosphatase| Previous page]]
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| [[Pfam| Next page]]
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| | == Functional site== |
| | MSA data revealed some conserved residues on the sequence. They were mapped on the three dimantional structure. |
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| | [[Image:Zn_Cl_surface]] |
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| ---- | | ---- |
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| Press here to go [http://compbio.chemistry.uq.edu.au/mediawiki/index.php/BIOL3004_2007 ''Back'']
| | Click here to go [http://compbio.chemistry.uq.edu.au/mediawiki/index.php/BIOL3004_2007 ''Back''] |
