The domain within your query sequence starts at position 39 and ends at position 278; the E-value for the NeuB domain shown below is 4.7e-81.
MIRTAKECGADCAKFQKSELEFKFNRKALERPYTSKHSWGKTYGEHKRHLEFSHDQYKEL QSYAQEIGIFFTASGMDEMAVEFLHELNVPFFKVGSGDTNNFPYLEKTAKKGRPMVISSG MQSMDTMKQVYQIVKPLNPNFCFLQCTSAYPLQPEDANLRVISEYQKLFPDIPIGYSGHE TGIAISVAAVALGAKVLERHITLDKTWKGSDHSASLEPGELAELVRSVRLVERALGSPTK
NeuB |
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PFAM accession number: | PF03102 |
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Interpro abstract (IPR013132): | NeuB is the prokaryotic N-acetylneuraminic acid synthase. It catalyses the direct formation of N-acetylneuraminic acid (Neu5Ac), the most common sialic acid, by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). Mammals synthesise the 9-phosphate form, Neu5Ac-9-P, and utilise ManNAc-6-P instead of ManNAc [ (PUBMED:10749855) (PUBMED:10873658) (PUBMED:15888312) ]. The bacterial and mammalian enzymes share 30%-40% sequence identity and are composed of two distinct domains. The N-terminal domain (NeuB domain) consists of ~250 amino acid residues, and is considered to bind the sugar substrates. The C-terminal domain consists of ~75 amino acid residues, and is called the antifreeze-like (AFL) domain, since it is similar to those observed in a variety of functional type III antifreeze proteins (AFPs) [ (PUBMED:15516336) ]. This entry represents the N-terminal domain. |
GO process: | carbohydrate biosynthetic process (GO:0016051) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry NeuB