Summary: Hydroxyphenylpyruvate dioxygenase, HPPD, N-terminal
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Hydroxyphenylpyruvate dioxygenase, HPPD, N-terminal Provide feedback
This domain is one of two barrel-shaped regions that together form the active enzyme, 4-hydroxyphenylpyruvic acid dioxygenase, EC:188.8.131.52. As can be deduced from the disposition of the various Glyoxalase families, _2, _3 and _4 in Pfam, PF00903 PF12681 PF13468 PF13669 these two regions are similar to be indicative of a gene-duplication event. At the individual sequence level slight differences in conformation have given rise to slightly different functions. In the case of UniProt:P80064 4-hydroxyphenylpyruvic acid dioxygenase catalyses the formation of homogentisate from 4-hydroxyphenylpyruvate, and the pyruvate part of the HPPD substrate (4-hydroxyphenylpyruvate), derived from L-tyrosine, and the O2 molecule occupy the three free coordination sites of the catalytic iron atom in the C-terminal domain. In plants and photosynthetic bacteria, the tyrosine degradation pathway is crucial because homogentisate, a tyrosine degradation product, is a precursor for the biosynthesis of photosynthetic pigments, such as quinones or tocopherols .
Serre L, Sailland A, Sy D, Boudec P, Rolland A, Pebay-Peyroula E, Cohen-Addad C;, Structure. 1999;7:977-988.: Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway. PUBMED:10467142 EPMC:10467142
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This clan contains the VOC metalloenzyme superfamily . The known types of reactions that are catalysed include isomerizations (glyoxalase I), epimerizations (methylmalonyl-CoA epimerase), oxidative cleavage of C-C bonds (extradiol dioxygenase), and nucleophilic substitutions (fosfomycin resistance proteins) .
The clan contains the following 8 members:3-dmu-9_3-mt CppA_N Glyoxalase Glyoxalase_2 Glyoxalase_3 Glyoxalase_4 Glyoxalase_5 YecM
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
This family is new in this Pfam release.
|Number in seed:||17|
|Number in full:||1091|
|Average length of the domain:||140.50 aa|
|Average identity of full alignment:||36 %|
|Average coverage of the sequence by the domain:||33.00 %|
|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:||1|
|Download:||download the raw HMM for this family|
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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 Glyoxalase_5 domain has been found. There are 6 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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