The domain within your query sequence starts at position 15 and ends at position 138; the E-value for the Ala_racemase_N domain shown below is 2e-13.
FALRAVNERVQQSVARRPRDLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYILSSC PEIKWHFIGHLQKQNVNKLMAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQIN TSGE
Ala_racemase_N |
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PFAM accession number: | PF01168 |
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Interpro abstract (IPR001608): | Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. The molecular structure of alanine racemase from Bacillus stearothermophilus was determined by X-ray crystallography to a resolution of 1.9 A [ (PUBMED:9063881) ]. The alanine racemase monomer is composed of two domains, an eight-stranded alpha/beta barrel at the N terminus, and a C-terminal domain essentially composed of beta-strands. The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the mouth of the alpha/beta barrel and is covalently linked via an aldimine linkage to a lysine residue, which is at the C terminus of the first beta-strand of the alpha/beta barrel. This N-terminal domain is also found in the PROSC (proline synthetase co-transcribed bacterial homologue) family of proteins, which are not known to have alanine racemase activity. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ala_racemase_N