2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase catalyzes the decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) into S(+)-allantoin, the third step of the conversion of uric acid (a purine derivative) to allantoin
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
13-163
4.62e-38
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine catabolism that catalyze the conversion of OHCU into S(+)-allantoin. This is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalyzed by urate oxidase (pfam01014) and step two is catalyzed by HIUases (pfam00576).
:
Pssm-ID: 462765 [Multi-domain] Cd Length: 156 Bit Score: 127.64 E-value: 4.62e-38
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
13-163
4.62e-38
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine catabolism that catalyze the conversion of OHCU into S(+)-allantoin. This is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalyzed by urate oxidase (pfam01014) and step two is catalyzed by HIUases (pfam00576).
Pssm-ID: 462765 [Multi-domain] Cd Length: 156 Bit Score: 127.64 E-value: 4.62e-38
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
15-167
1.26e-25
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model.
Pssm-ID: 132208 [Multi-domain] Cd Length: 157 Bit Score: 95.89 E-value: 1.26e-25
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
13-163
4.62e-38
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine catabolism that catalyze the conversion of OHCU into S(+)-allantoin. This is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalyzed by urate oxidase (pfam01014) and step two is catalyzed by HIUases (pfam00576).
Pssm-ID: 462765 [Multi-domain] Cd Length: 156 Bit Score: 127.64 E-value: 4.62e-38
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
15-167
1.26e-25
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model.
Pssm-ID: 132208 [Multi-domain] Cd Length: 157 Bit Score: 95.89 E-value: 1.26e-25
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
42-164
5.98e-13
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model. This model is a separate (but related) clade from that represented by TIGR3164. This model places a second homolog in streptomyces species which (are not in the vicinity of other urate catabolism associated genes) below the trusted cutoff.
Pssm-ID: 188295 [Multi-domain] Cd Length: 158 Bit Score: 62.86 E-value: 5.98e-13
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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