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3  structures 1716  species 0  interactions 2015  sequences 10  architectures

Family: Fructosamin_kin (PF03881)

Summary: Fructosamine kinase

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This is the Wikipedia entry entitled "Fructosamine kinase family". More...

Fructosamine kinase family Edit Wikipedia article

Fructosamin_kin
Identifiers
Symbol Fructosamin_kin
Pfam PF03881
Pfam clan CL0016
InterPro IPR016477

In molecular biology the fructosamine kinase family is a family of enzymes. This family includes eukaryotic fructosamine-3-kinase enzymes which may initiate a process leading to the deglycation of fructoselysine and of glycated proteins and in the phosphorylation of 1-deoxy-1-morpholinofructose, fructoselysine, fructoseglycine, fructose and glycated lysozyme.[1] The family also includes ketosamine-3-kinases (KT3K). Ketosamines derive from a non-enzymatic reaction between a sugar and a protein.[2] Ketosamine-3-kinases (KT3K) catalyse the phosphorylation of the ketosamine moiety of glycated proteins. The instability of a phosphorylated ketosamine leads to its degradation, and KT3K is thus thought to be involved in protein repair.[3]

The function of the prokaryotic members of this group has not been established. However, several lines of evidence indicate that they may function as fructosamine-3-kinases (FN3K). First, they are similar to characterised FN3K from mouse and human. Second, the Escherichia coli members are found in close proximity on the genome to fructose-6-phosphate kinase (PfkB). Last, FN3K activity has been found in the blue-green algae Anacystis montana indicating such activity-directly demonstrated in eukaryotes-is nonetheless not confined to eukaryotes.[4]

References[edit]

  1. ^ Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, Van Schaftingen E (October 2000). "Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase". Diabetes 49 (10): 1627–34. doi:10.2337/diabetes.49.10.1627. PMID 11016445. 
  2. ^ Armbruster DA (December 1987). "Fructosamine: structure, analysis, and clinical usefulness". Clin. Chem. 33 (12): 2153–63. PMID 3319287. 
  3. ^ Collard F, Delpierre G, Stroobant V, Matthijs G, Van Schaftingen E (December 2003). "A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines". Diabetes 52 (12): 2888–95. doi:10.2337/diabetes.52.12.2888. PMID 14633848. 
  4. ^ Delvalle JA, Asensio C (August 1978). "Distribution of adenosine 5'-triphosphate (ATP)-dependent hexose kinases in microorganisms". BioSystems 10 (3): 265–82. PMID 214181. 

This article incorporates text from the public domain Pfam and InterPro IPR016477

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.

Fructosamine kinase Provide feedback

This family includes eukaryotic fructosamine-3-kinase enzymes [1]. The family also includes bacterial members that have not been characterised but probably have a similar or identical function.

Literature references

  1. Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, Van Schaftingen E; , Diabetes 2000;49:1627-1634.: Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. PUBMED:11016445 EPMC:11016445


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR016477

Ketosamines derive from a non-enzymatic reaction between a sugar and a protein [PUBMED:3319287]. Ketosamine-3-kinases (KT3K), of which fructosamine-3-kinase (FN3K) is the best-known example, catalyse the phosphorylation of the ketosamine moiety of glycated proteins. The instability of a phosphorylated ketosamine leads to its degradation, and KT3K is thus thought to be involved in protein repair [PUBMED:14633848].

The function of the prokaryotic members of this group has not been established. However, several lines of evidence indicate that they may function as fructosamine-3-kinases (FN3K). First, they are similar to characterised FN3K from mouse and human. Second, the Escherichia coli members are found in close proximity on the genome to fructose-6-phosphate kinase (PfkB). Last, FN3K activity has been found in a Anacystis montana (Gloeocapsa montana Kutzing 1843) [PUBMED:214181], indicating such activity-directly demonstrated in eukaryotes-is nonetheless not confined to eukaryotes.

This family includes eukaryotic fructosamine-3-kinase enzymes [PUBMED:11016445] which may initiate a process leading to the deglycation of fructoselysine and of glycated proteins and in the phosphorylation of 1-deoxy-1-morpholinofructose, fructoselysine, fructoseglycine, fructose and glycated lysozyme. The family also includes bacterial members that have not been characterised but probably have a similar or identical function.

For additional information please see [PUBMED:11016445].

Domain organisation

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Alignments

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(35)
Full
(2015)
Representative proteomes NCBI
(1603)
Meta
(432)
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(143)
RP35
(323)
RP55
(454)
RP75
(561)
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  Seed
(35)
Full
(2015)
Representative proteomes NCBI
(1603)
Meta
(432)
RP15
(143)
RP35
(323)
RP55
(454)
RP75
(561)
Alignment:
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  Seed
(35)
Full
(2015)
Representative proteomes NCBI
(1603)
Meta
(432)
RP15
(143)
RP35
(323)
RP55
(454)
RP75
(561)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
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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:

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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.

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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: COG3001
Previous IDs: none
Type: Family
Author: Bateman A
Number in seed: 35
Number in full: 2015
Average length of the domain: 272.80 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 95.06 %

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 20.0 20.0
Trusted cut-off 20.0 20.0
Noise cut-off 19.9 19.9
Model length: 288
Family (HMM) version: 9
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 Fructosamin_kin domain has been found. There are 3 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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