The domain within your query sequence starts at position 58 and ends at position 407; the E-value for the Amidohydro_1 domain shown below is 1e-26.
LVLPGGIDTHTHMQFPFMGSQSVDDFYQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETW RNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLARDKGVNSFKMFMAYKGLYMVQDEQLYA AFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIA SAVNCPLYVVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYWSEEWSHAAHHVM GPPLRPDPLTPGFLMDLLANGDLTTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMS VIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWD
Amidohydro_1 |
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PFAM accession number: | PF01979 |
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Interpro abstract (IPR006680): | Proteins containing this domain are enzymes from a large metal dependent hydrolase superfamily [ (PUBMED:9144792) ]. The family includes adenine deaminase ( EC 3.5.4.2 ) that hydrolyses adenine to form hypoxanthine and ammonia. This reaction is important for adenine utilisation as a purine and also as a nitrogen source [ (PUBMED:8550522) ]. The family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases ( EC 3.5.1.25 ). The domain is also found in the urease alpha subunit, where it is the catalytic domain [ (PUBMED:7754395) ]. |
GO function: | hydrolase activity (GO:0016787) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Amidohydro_1