Hydantoinase/oxoprolinase Provide feedback
This family includes the enzymes hydantoinase and oxoprolinase EC:22.214.171.124. Both reactions involve the hydrolysis of 5-membered rings via hydrolysis of their internal imide bonds .
Ye GJ, Breslow EB, Meister A, Guo-jie GE; , J Biol Chem 1996;271:32293-32300.: The amino acid sequence of rat kidney 5-oxo-L-prolinase determined by cDNA cloning [published erratum appears in J Biol Chem 1997 Feb 14;272(7):4646] PUBMED:8943290 EPMC:8943290
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002821This family includes the enzymes hydantoinase and oxoprolinase (EC). Both reactions involve the hydrolysis of 5-membered rings via hydrolysis of their internal imide bonds [PUBMED:8943290].
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)|
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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
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The actin-like ATPase domain forms an alpha/beta canonical fold. The domain can be subdivided into 1A, 1B, 2A and 2B subdomains. Subdomains 1A and 1B share the same RNAseH-like fold (a five-stranded beta-sheet decorated by a number of alpha-helices). Domains 1A and 2A are conserved in all members of this superfamily, whereas domain 1B and 2B have a variable structure and are even missing from some homologues . Within the actin-like ATPase domain the ATP-binding site is highly conserved. The phosphate part of the ATP is bound in a cleft between subdomains 1A and 2A, whereas the adenosine moiety is bound to residues from domains 2A and 2B.
The clan contains the following 29 members:Acetate_kinase Actin BcrAD_BadFG CmcH_NodU DDR DUF1464 DUF1786 EutA FGGY_C FGGY_N FtsA Fumble GDA1_CD39 Glucokinase Hexokinase_1 Hexokinase_2 HSP70 Hydant_A_N Hydantoinase_A MreB_Mbl MutL Pan_kinase Peptidase_M22 PilM_2 Ppx-GppA ROK StbA T2SL UPF0075
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Enright A|
|Author:||Enright A, Ouzounis C, Bateman A|
|Number in seed:||61|
|Number in full:||2437|
|Average length of the domain:||281.50 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||34.74 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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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 Hydantoinase_A domain has been found. There are 6 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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