Summary: homogentisate 1,2-dioxygenase
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Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers .
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This tab holds annotation information from the InterPro database.
InterPro entry IPR005708
Alkaptonuria (AKU), a rare hereditary disorder, was the first disease to be interpreted as an inborn error of metabolism. The
deficiency causes homogentisic aciduria, ochronosis, and arthritis. AKU patients are deficient for homogentisate 1,2 dioxygenase (EC), the enzyme that mediates the conversion of homogentisate to maleylacetoacetate; a step in the catabolism of both tyrosine and phenylalanine.
|Molecular function||homogentisate 1,2-dioxygenase activity (GO:0004411)|
|Biological process||oxidation-reduction process (GO:0055114)|
|tyrosine metabolic process (GO:0006570)|
|L-phenylalanine catabolic process (GO:0006559)|
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Curation and family details
|Seed source:||TIGRFAMs (release 2.0);|
|Author:||TIGRFAMs, Finn RD|
|Number in seed:||14|
|Number in full:||1185|
|Average length of the domain:||378.40 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||93.62 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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