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CATH Superfamily 3.40.140.10

Cytidine Deaminase, 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:

"
Cytidine Deaminase, 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 13440: 26S proteasome regulatory subunit

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
Deleted entry. [EC: 3.1.2.15]
    		13 A0A074T9I4 A0A086KHH2 A0A086L6R3 A0A086LCS7 A0A086LY27 A0A086Q0B4 A0A086QVU5 A0A125YUB2 A0A125YUB3 A0A139Y686
    (3 more...)
    Ubiquitinyl hydrolase 1. [EC: 3.4.19.12]
    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
    • Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides.
    • Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals.
    • Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde).
    • Belongs to peptidase family C12.
    		 9 A7A242 B3LUL2 B5VI30 C7GYB0 C8Z7T7 E7QE99 G2WDE3 N1P4N6 P43588
    Proteasome endopeptidase complex. [EC: 3.4.25.1]
    Cleavage of peptide bonds with very broad specificity.
    • A 20-S protein composed of 28 subunits arranged in four rings of seven.
    • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
    • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
    • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
    • Terminal apertures restrict access of substrates to the active sites.
    • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
    • Belongs to peptidase family T1.
    • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
    		 8 A0A0F4YY77 A0A100ID42 A0A146F1M3 A0A1L9MYW9 A0A1M3T9B1 A5AAY7 G7XE24 L7JUL0
    Acetolactate synthase. [EC: 2.2.1.6]
    2 pyruvate = 2-acetolactate + CO(2).
    • The reaction shown is in the pathway of biosynthesis of valine.
    • The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
    • Formerly EC 4.1.3.18.
    		 1 E3TDZ7
    TRNA-guanine(34) transglycosylase. [EC: 2.4.2.29]
    (1) Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine. (2) Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7- carbaguanine(34) in tRNA + guanine.
    • Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34.
    • In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine.
    • In eubacteria, which produce queuine de novo, the enzyme catalyzes the exchange of guanine with the queuine precursor preQ(1), which is ultimately modified to queuine.
    • The eubacterial enzyme can also use an earlier intermediate, preQ(0), to replace guanine in unmodified tRNA(Tyr) and tRNA(Asn).
    • This enzyme acts after EC 1.7.1.13 in the queuine-biosynthesis pathway.
    		 1 A0A085MD80
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