Summary: Creatinase/Prolidase N-terminal domain
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This is the Wikipedia entry entitled "Creatinase". More...
Creatinase Edit Wikipedia article
In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction
- creatine + H2O sarcosine + urea
Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is creatine amidinohydrolase. This enzyme participates in arginine and proline metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1CHM and 1KP0.
References
- ROCHE J, LACOMBE G, GIRARD H (1950). "[On the specificity of certain bacterial deguanidases generating urea and on arginindihydrolase.]". Biochim. Biophys. Acta. 6: 210–6. PMID 14791411.
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: CS1 maint: multiple names: authors list (link) - Yoshimoto T, Oka I, Tsuru D (Tokyo). "Purification, crystallization, and some properties of creatine amidinohydrolase from Pseudomonas putida". J. Biochem.: 1381–3. PMID 8443.
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(help)CS1 maint: multiple names: authors list (link)
External links
- The CAS registry number for this enzyme class is Template:CAS registry.
Gene Ontology (GO) codes
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Creatinase/Prolidase N-terminal domain Provide feedback
This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.
Literature references
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Coll M, Knof SH, Ohga Y, Messerschmidt A, Huber R, Moellering H, Russmann L, Schumacher G; , J Mol Biol 1990;214:597-610.: Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures. PUBMED:1696320 EPMC:1696320
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Maher MJ, Ghosh M, Grunden AM, Menon AL, Adams MW, Freeman HC, Guss JM; , Biochemistry. 2004;43:2771-2783.: Structure of the prolidase from Pyrococcus furiosus. PUBMED:15005612 EPMC:15005612
Internal database links
SCOOP: | Creatinase_N_2 |
Similarity to PfamA using HHSearch: | Creatinase_N_2 |
External database links
SCOP: | 1chm |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000587
Creatinase or creatine amidinohydrolase ( EC ) catalyses the conversion of creatine and water to sarcosine and urea. The enzyme works as a homodimer, and is induced by choline chloride. Each monomer of creatinase has two clearly defined domains, a small N-terminal domain, and a large C-terminal domain.
The structure of the C-terminal region represents the "pita-bread" fold. The fold contains both alpha helices and an anti-parallel beta sheet within two structurally similar domains that are thought to be derived from an ancient gene duplication. The active site, where conserved, is located between the two domains. The fold is common to methionine aminopeptidase ( EC ), aminopeptidase P ( EC ), prolidase ( EC ), agropine synthase and creatinase ( EC ). Though many of these peptidases require a divalent cation, creatinase is not a metal-dependent enzyme [ PUBMED:8146141 , PUBMED:12136144 , PUBMED:8471602 ].
Gene Ontology
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) |
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 AMP_N-like (CL0356), which has the following description:
Bacterial amino-peptidases and creatinases, where the fold is a ribonuclease H-like motif, are grouped in this superfamily.
The clan contains the following 4 members:
AMP_N Creatinase_N Creatinase_N_2 FACT-Spt16_NlobAlignments
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.
Seed (82) |
Full (16139) |
Representative proteomes | UniProt (72028) |
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RP15 (2070) |
RP35 (7567) |
RP55 (15942) |
RP75 (26971) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
— not available.
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (82) |
Full (16139) |
Representative proteomes | UniProt (72028) |
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RP15 (2070) |
RP35 (7567) |
RP55 (15942) |
RP75 (26971) |
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Raw Stockholm | |||||||
Gzipped |
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...
Trees
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.
Note: You can also download the data file for the tree.
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
Seed source: | Bateman A |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 82 |
Number in full: | 16139 |
Average length of the domain: | 135.9 aa |
Average identity of full alignment: | 18 % |
Average coverage of the sequence by the domain: | 28.94 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 130 | ||||||||||||
Family (HMM) version: | 21 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 Creatinase_N domain has been found. There are 91 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.