Evolution

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Query Sequences (2gfh)

The following query protein sequence of N-acetylneuraminic Acid was obtained from GenBank:

N-acetylneuraminic Acid
mgsdkihhhh hhmglsrvra vffdldntli dtagasrrgm levikllqsk yhykeeaeii

cdkvqvklsk ecfhpystci tdvrtshwee aiqetkggad nrklaeecyf lwkstrlqhm

iladdvkaml telrkevrll lltngdrqtq rekieacacq syfdaivigg eqkeekpaps

ifyhccdllg vqpgdcvmvg dtletdiqgg lnaglkatvw inksgrvplt sspmphymvs

svlelpallq sidckvsmsv

Fig. 1: Amino Acid Sequence (260 aa) of N-acetylneuraminic Acid (2gfh) protein from Mus musculus (House Mouse)


BlastP similarity sequence search was carried out on fixed database found on DVD-rom. A total of 500 proteins were yielded. Only a 38 proteins were selected for comparison as these had shown higher homology to the query sequence, in contrast with the remainder of the search results.


These proteins were chosen according to their bit scores and E-values. Two more outlier partial sequences contributing to poor overall alignment (huge deletion gaps) were subsequently removed. The remaining 36 sequences were used for the generation of the phylogenetic tree (and bootstrapped tree as well).


The bacteria sequence matches used for multiple sequence analysis and phylogenetic tree mapping were representative of the other baterial sequences not selected. These selected sequences had the highest bit scores and E-values.



Multiple Sequence Alignments (msa)

Msaseg1b.png


Figure 1. Multiple Sequence Alignments of 2gfh amino acid sequences with that of other similar protein sequences in various organisms (A) Glycolysis pathway with substrates that are hydrolyze by HADs: glucose 6-phosphate, fructose 6-phosphate and dihydroxyacetone phosphate. (B) Pentose phostphate pathway with substrates that are hydrolyze by HADs: glucose-6-phosphate, fructose-6-phosphate, dihydroxyacetone phosphate, glyceraldehyde-3-phosphate, gluconate 6-phosphate and erythrose-4-phosphate.

Msaseg2.png




Msaseg3.png


Table of functions
Catalytic activity N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate
Cofactor Magnesium (By similarity)
Enzyme regulation Inhibited by vanadate and calcium (By similarity)
Pathway Carbohydrate metabolism; aminosugar metabolism
Similarity Belongs to the haloacid dehalogenase-like hydrolase superfamily. NANP family



Separate Enzymes Catalyze the Final Two Steps of Coenzyme A Biosynthesis in Brevibacterium ammoniagenes: Purification of Pantetheine Phosphate Adenylyltransferase