| Analysis | rpsblast_cdd | Start | 61 |
| End | 167 | Strand | + |
| Length | 107 | Note | Gaps:47 |
| Hit Coverage | 77.49 | Hit Length | 191 |
| Hit Pident | 27.03 | E Val | 2e-08 |
| Hit Description | cd07250 HPPD_C_like C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate Synthase (HmaS). HppD and HmaS are non-heme iron-dependent dioxygenases which modify a common substrate 4-hydroxyphenylpyruvate (HPP) but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism the conversion of 4-hydroxyphenylpyruvate to homogentisate (2 5-dihydroxyphenylacetic acid HG). HmaS converts HPP to 4-hydroxymandelate a committed step in the formation of hydroxyphenylglycerine a structural component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. If the emphasis is on catalytic chemistry HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II) molecular oxygen and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two instead of three substrates do not use alpha-ketoglutarate and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_C_like domain represents the C-terminal domain. | Hit Pcons | 11.49 |
| Name | Qrob_P0188670.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0188670.2 | Quercus robur | 0.0 | egn | (M=2) 1.13.11.27 - 4-hydroxyphenylpyruvate dioxygenase. | EC:1.13.11.27 | validated |
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