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40  structures 4001  species 2  interactions 7541  sequences 18  architectures

Family: Creatinase_N (PF01321)

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 Edit Wikipedia article

creatinase
Identifiers
EC number 3.5.3.3
CAS number 37340-58-2
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
Creatinase/Prolidase N-terminal domain
3O5V.pdb.jpg
The Crystal Structure of the Creatinase/Prolidase N-terminal domain of an X-PRO dipeptidase from Streptococcus pyogenes to 1.85A [1]
Identifiers
Symbol Creatinase_N
Pfam PF01321
InterPro IPR000587
SCOP 1chm
SUPERFAMILY 1chm

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

creatine + H2O \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's 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[edit]

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1CHM and 1KP0.

References[edit]

"RCSB Protein Data Bank - Structure Summary for 3O5V - The Crystal Structure of the Creatinase/Prolidase N-terminal domain of an X-PRO dipeptidase from Streptococcus pyogenes to 1.85A". 

  1. ^ "RCSB Protein Data Bank - Structure Summary for 3O5V - The Crystal Structure of the Creatinase/Prolidase N-terminal domain of an X-PRO dipeptidase from Streptococcus pyogenes to 1.85A". 
  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): 1381–3. 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): 210–6. PMID 14791411. 
  • Yoshimoto T, Oka I, Tsuru D (Tokyo). "Purification, crystallization, and some properties of creatine amidinohydrolase from Pseudomonas putida". J. Biochem. (6): 1381–3. PMID 8443. 


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

  1. 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

  2. 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


External database links

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.

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 contains the following 2 members:

AMP_N Creatinase_N

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, 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
(170)
Full
(7541)
Representative proteomes NCBI
(5872)
Meta
(3626)
RP15
(667)
RP35
(1256)
RP55
(1650)
RP75
(1991)
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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
(170)
Full
(7541)
Representative proteomes NCBI
(5872)
Meta
(3626)
RP15
(667)
RP35
(1256)
RP55
(1650)
RP75
(1991)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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
(170)
Full
(7541)
Representative proteomes NCBI
(5872)
Meta
(3626)
RP15
(667)
RP35
(1256)
RP55
(1650)
RP75
(1991)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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: Bateman A
Previous IDs: none
Type: Domain
Author: Finn RD, Bateman A
Number in seed: 170
Number in full: 7541
Average length of the domain: 132.50 aa
Average identity of full alignment: 18 %
Average coverage of the sequence by the domain: 31.80 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.4 21.4
Trusted cut-off 21.4 21.4
Noise cut-off 21.3 21.3
Model length: 132
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

Peptidase_M24 Creatinase_N

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 40 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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