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CATH Superfamily 3.20.20.70

Aldolase class I

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:

"
Aldolase class I
".

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 120782: Ribulose-phosphate 3-epimerase (AFU_orthologue; AF...

There are 6 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
Ribulose-phosphate 3-epimerase. [EC: 5.1.3.1]
D-ribulose 5-phosphate = D-xylulose 5-phosphate.
  • Also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate.
 14398 A0A009GZS9 A0A009H1C8 A0A009HPB0 A0A009HUA4 A0A009JBY3 A0A009JML7 A0A009LR84 A0A009MZR2 A0A009Q6C0 A0A009R6D2
(14388 more...)
Transketolase. [EC: 2.2.1.1]
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
  • Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH.
  • The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
 27 A0A060HR90 A0A075G2X9 A0A075G394 A0A075G3D5 A0A075GKL6 A0A075GMS7 A0A075GN85 A0A075GPE3 A0A075H5A7 A0A075H616
(17 more...)
Protein S-acyltransferase. [EC: 2.3.1.225]
Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.
  • The enzyme catalyzes the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity.
  • Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
 2 A0A075AIH3 G7YVG5
Phosphoglycolate phosphatase. [EC: 3.1.3.18]
2-phosphoglycolate + H(2)O = glycolate + phosphate.
    		 1 A0A0T7Q875
    Site-specific DNA-methyltransferase (adenine-specific). [EC: 2.1.1.72]
    S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.
    • This is a large group of enzymes, most of which form so-called 'restriction-modification systems', with nucleases that possess similar site specificity (the nucleases are listed as either EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5).
    • See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
    		 1 K8ALB9
    Uridine kinase. [EC: 2.7.1.48]
    (1) ATP + uridine = ADP + UMP. (2) ATP + cytidine = ADP + CMP.
    • Cytidine can act as acceptor.
    • GTP and ITP can act as donors.
    		 1 R7W0G7
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