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608  structures 8554  species 0  interactions 73114  sequences 447  architectures

Family: Amidohydro_1 (PF01979)

Summary: Amidohydrolase family

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Amidohydrolase family Provide feedback

This family of enzymes are a a large metal dependent hydrolase superfamily [1]. The family includes Adenine deaminase EC: 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 [2]. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC: 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 [3]. Dihydroorotases ( EC: are also included [4-5].

Literature references

  1. Holm L, Sander C; , Proteins 1997;28:72-82.: An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. PUBMED:9144792 EPMC:9144792

  2. 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

  3. Jabri E, Carr MB, Hausinger RP, Karplus PA; , Science 1995;268:998-1004.: The crystal structure of urease from Klebsiella aerogenes. PUBMED:7754395 EPMC:7754395

  4. 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

  5. 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

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006680

Proteins 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 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Amidohydrolase (CL0034), which has the following description:

This family includes a large family of metal dependent amidohydrolase enzymes [1].

The clan contains the following 17 members:

A_deaminase Amidohydro_1 Amidohydro_2 Amidohydro_3 AMP_deaminase CpsB_CapC DHOase DUF3604 DUF6282 Peptidase_M19 PHP PHP_C PTE RNase_P_p30 TatD_DNase Urease_alpha UxaC


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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Representative proteomes UniProt

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Bateman A
Previous IDs: Adenine_deam;
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Eberhardt R
Number in seed: 57
Number in full: 73114
Average length of the domain: 321.50 aa
Average identity of full alignment: 14 %
Average coverage of the sequence by the domain: 67.98 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.6 21.6
Trusted cut-off 21.6 21.6
Noise cut-off 21.5 21.5
Model length: 344
Family (HMM) version: 22
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
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Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 608 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 sequence.

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