Summary: Amidohydrolase family
Amidohydrolase family Provide feedback
This family of enzymes are a a large metal dependent hydrolase superfamily . The family includes Adenine deaminase EC:18.104.22.168 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source . This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:22.214.171.124 These enzymes catalyse the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit . Dihydroorotases ( EC:126.96.36.199) are also included [4-5].
Nygaard P, Duckert P, Saxild HH; , J Bacteriol 1996;178:846-853.: Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis. PUBMED:8550522 EPMC:8550522
Gao G, Nara T, Nakajima-Shimada J, Aoki T; , J Mol Biol 1999;285:149-161.: Novel organization and sequences of five genes encoding all six enzymes for de novo pyrimidine biosynthesis in Trypanosoma cruzi. PUBMED:9878395 EPMC:9878395
Lollier M, Jaquet L, Nedeva T, Lacroute F, Potier S, Souciet JL; , Curr Genet 1995;28:138-149.: As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe. PUBMED:8590465 EPMC:8590465
Internal database links
|SCOOP:||A_deaminase Amidohydro_2 Amidohydro_3 DHOase TatD_DNase|
|Similarity to PfamA using HHSearch:||TatD_DNase Amidohydro_3|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR006680Proteins containing this domain are enzymes from a large metal dependent hydrolase superfamily [PUBMED:9144792]. The family includes adenine deaminase (EC) 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). The domain is also found in the urease alpha subunit, where it is the catalytic domain [PUBMED:7754395].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||hydrolase activity (GO:0016787)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
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This family includes a large family of metal dependent amidohydrolase enzymes .
The clan contains the following 14 members:A_deaminase Amidohydro_1 Amidohydro_2 Amidohydro_3 DHOase DUF3604 Peptidase_M19 PHP PHP_C PTE RNase_P_p30 TatD_DNase Urease_alpha UxaC
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Bateman A|
|Author:||Bateman A, Eberhardt R|
|Number in seed:||57|
|Number in full:||33076|
|Average length of the domain:||320.70 aa|
|Average identity of full alignment:||14 %|
|Average coverage of the sequence by the domain:||69.13 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||19|
|Download:||download the raw HMM for this family|
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There are 8 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Amidohydro_1 domain has been found. There are 458 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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