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CATH Superfamily 1.10.340.30

Hypothetical protein; domain 2

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Hypothetical protein; domain 2
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 7893: Putative 8-oxoguanine dna glycosylase

There are 5 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
DNA-(apurinic or apyrimidinic site) lyase. [EC: 4.2.99.18]
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
  • 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis.
  • This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2.
 24 A0A0B7F8B2 A0A0L8VK19 A0A178WC14 A2QMP9 B3LLJ5 B7Q8B3 B9WJV0 C4IXZ6 C7GVZ6 C8ZEE5
(14 more...)
DNA-formamidopyrimidine glycosylase. [EC: 3.2.2.23]
Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
  • May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents.
  • Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
 6 A0A0L1HET2 B3NUL4 B4L6Y2 B4MA54 B4MJ78 B4Q085
Dihydroorotase. [EC: 3.5.2.3]
(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.
    		 1 M2XXT9
    Carbamoyl-phosphate synthase (glutamine-hydrolyzing). [EC: 6.3.5.5]
    2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
    • The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides.
    • The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length.
    • The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate.
    • The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate.
    • The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit.
    • The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate.
    • Cf. EC 6.3.4.16.
    • Formerly EC 2.7.2.9.
    		 1 M2XXT9
    Aspartate carbamoyltransferase. [EC: 2.1.3.2]
    Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
      		 1 M2XXT9
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