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87  structures 2650  species 1  interaction 4100  sequences 7  architectures

Family: Creatininase (PF02633)

Summary: Creatinine amidohydrolase

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This is the Wikipedia entry entitled "Creatininase". More...

Creatininase Edit Wikipedia article

Creatininase
3NO4.png
Crystallographic structure of a creatinine amidohydrolase from Nostoc pruniforme.[1]
Identifiers
EC number 3.5.2.10
CAS number 9025-13-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Creatininase
PDB 1v7z EBI.jpg
creatininase-product complex
Identifiers
Symbol Creatininase
Pfam PF02633
InterPro IPR003785
SCOP 1v7z
SUPERFAMILY 1v7z

In enzymology, a creatininase (EC 3.5.2.10) is an enzyme that catalyses the hydrolysis of creatinine to creatine, which can then be metabolised to urea and sarcosine by creatinase.

creatinine + H2O creatine

Thus, the two substrates of this enzyme are creatinine and H2O, whereas its product is creatine.

Creatininase is a member of the urease-related amidohydrolases,[2] the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is creatinine amidohydrolase. This enzyme is also called creatinine hydrolase. This enzyme participates in arginine and proline metabolism.

Structural studies

Creatininase from Pseudomonas putida has a core structure consisting of 3-layers, alpha/beta/alpha.[3]

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1J2T, 1J2U, 1Q3K, and 1V7Z.

References

  1. ^ PDB: 3NO4​; Joint Center for Structural Genomics (2010). "Crystal structure of a creatinine amidohydrolase (Npun_F1913) from Nostoc punctiforme PCC 73102 at 2.00 A resolution". doi:10.2210/pdb3no4/pdb. 
  2. ^ Yamamoto K, Oka M, Kikuchi T, Emi S (1995). "Cloning of the creatinine amidohydrolase gene from Pseudomonas sp. PS-7". Biosci. Biotechnol. Biochem. 59 (7): 1331–1332. doi:10.1271/bbb.59.1331. PMID 7670196. 
  3. ^ Yoshimoto T, Tanaka N, Kanada N, Inoue T, Nakajima Y, Haratake M, Nakamura KT, Xu Y, Ito K (March 2004). "Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism". J. Mol. Biol. 337 (2): 399–416. doi:10.1016/j.jmb.2004.01.022. PMID 15003455. 
  • Tsuru D, Oka I & Yoshimoto T (1976). "Creatinine decomposing enzymes in Pseudomonas putida". Agric. Biol. Chem. 40: 1011–1018. doi:10.1271/bbb1961.40.1011. 

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.

Creatinine amidohydrolase Provide feedback

Creatinine amidohydrolase ( EC:3.5.2.10), or creatininase, catalyses the hydrolysis of creatinine to creatine [1].

Literature references

  1. Yamamoto K, Oka M, Kikuchi T, Emi S; , Biosci Biotechnol Biochem 1995;59:1331-1332.: Cloning of the creatinine amidohydrolase gene from Pseudomonas sp. PS-7. PUBMED:7670196 EPMC:7670196


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003785

This family includes the enzymes creatininase and 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase, also known as formamide hydrolase.

Creatinase or creatinine amidohydrolase (EC) catalyses the hydrolysis of creatinine to creatine, which can then be metabolised to urea and sarcosine by creatinase (EC). Creatininase is a member of the urease-related amidohydrolase superfamily [PUBMED:15003455]. Formamide hydrolase catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy) (EC) [PUBMED:19309161].

This family also includes 3-dehydro-scyllo-inosose hydrolase from the marine, hyperthermophilic bacterium Thermotoga maritima. The enzyme converts 3-dehydro-scyllo-inosose (diketo-inositol) to 5-dehydro-L-gluconate by catalysing ring-opening hydrolysis, and is a component of the myo-inositol degradation pathway. T. maritima is unable to grow on myo-inositol as a single carbon source [PUBMED:23441918].

Domain organisation

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

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Alignments

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, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics 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
(441)
Full
(4100)
Representative proteomes UniProt
(10863)
NCBI
(13875)
Meta
(595)
RP15
(978)
RP35
(2785)
RP55
(4230)
RP75
(5987)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(441)
Full
(4100)
Representative proteomes UniProt
(10863)
NCBI
(13875)
Meta
(595)
RP15
(978)
RP35
(2785)
RP55
(4230)
RP75
(5987)
Alignment:
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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
(441)
Full
(4100)
Representative proteomes UniProt
(10863)
NCBI
(13875)
Meta
(595)
RP15
(978)
RP35
(2785)
RP55
(4230)
RP75
(5987)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

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 View help on the curation process

Seed source: COG1402
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Mian N , Bateman A
Number in seed: 441
Number in full: 4100
Average length of the domain: 232.50 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 90.27 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 28.8 28.8
Trusted cut-off 28.8 29.0
Noise cut-off 28.5 28.7
Model length: 241
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

Creatininase

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 Creatininase domain has been found. There are 87 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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