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5  structures 3262  species 0  interactions 4570  sequences 50  architectures

# Summary: Creatinase/Prolidase N-terminal domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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

# Creatinase

creatinase
Identifiers
EC number3.5.3.3
CAS number37340-58-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structures
Gene Ontology
Creatinase/Prolidase N-terminal domain
The Crystal Structure of the Creatinase/Prolidase N-terminal domain of an X-PRO dipeptidase from Streptococcus pyogenes to 1.85A [1]
Identifiers
SymbolCreatinase_N
PfamPF01321
InterProIPR000587
SCOPe1chm / SUPFAM

In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction

creatine + H2O ${\displaystyle \rightleftharpoons }$ sarcosine + urea

Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea.

The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. The molecular weights of these subunits was estimated to be 47,000 g/mol.[2] 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. Each of the two active sites is made by residues of the large domain of one monomer and some residues of the small domain of the other monomer. It has been suggested that a sulfhydryl group is located on or near the active site of the enzyme following inhibition experiments.[2] Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees.[2]

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

1. ^
2. ^ a b c Yoshimoto T, Oka I, Tsuru D (June 1976). "Purification, crystallization, and some properties of creatine amidinohydrolase from Pseudomonas putida". J. Biochem. 79 (6): 1381â€“3. PMID 8443.
• ROCHE J, LACOMBE G, GIRARD H (1950). "[On the specificity of certain bacterial deguanidases generating urea and on arginindihydrolase.]". Biochim. Biophys. Acta. 6 (1): 210â€“6. doi:10.1016/0006-3002(50)90093-x. PMID 14791411.

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

No Pfam abstract.

This tab holds annotation information from the InterPro database.

No InterPro data for this Pfam family.

# Domain organisation

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

# 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:

Creatinase_N_2

# 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...

## View options

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
(585)
Full
(4570)
Representative proteomes UniProt
(15612)
NCBI
(23394)
Meta
(1037)
RP15
(698)
RP35
(2157)
RP55
(4000)
RP75
(6592)
Jalview View  View  View  View  View  View  View  View  View
HTML View  View
PP/heatmap 1 View

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, not available.

## Format an alignment

Seed
(585)
Full
(4570)
Representative proteomes UniProt
(15612)
NCBI
(23394)
Meta
(1037)
RP15
(698)
RP35
(2157)
RP55
(4000)
RP75
(6592)
Alignment:
Format:
Order:
Sequence:
Gaps:

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
(585)
Full
(4570)
Representative proteomes UniProt
(15612)
NCBI
(23394)
Meta
(1037)
RP15
(698)
RP35
(2157)
RP55
(4000)
RP75
(6592)

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.

# 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: Phmmer:Q9NQW7 Previous IDs: none Type: Domain Sequence Ontology: SO:0000417 Author: Coggill P Number in seed: 585 Number in full: 4570 Average length of the domain: 162.90 aa Average identity of full alignment: 30 % Average coverage of the sequence by the domain: 25.95 %

## HMM information

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 29.7 29.7
Trusted cut-off 29.8 29.8
Noise cut-off 29.0 29.0
Model length: 160
Family (HMM) version: 6

# Species distribution

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### Colour assignments

 Archea Eukaryota Bacteria Other sequences Viruses Unclassified Viroids Unclassified sequence

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