View in Gene3D

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.
« Back to all FunFams

FunFam 120777: tRNA-dihydrouridine synthase B protein

There are 12 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
TRNA-dihydrouridine(47) synthase (NAD(P)(+)). [EC: 1.3.1.89]
5,6-dihydrouracil(47) in tRNA + NAD(P)(+) = uracil(47) in tRNA + NAD(P)H.
  • The enzyme specifically modifies uracil(47) in tRNA.
 824 A0A010RS93 A0A010RS93 A0A015K6U6 A0A015K6U6 A0A060SAG8 A0A060SAG8 A0A060T1M5 A0A060T1M5 A0A061B0F7 A0A061B0F7
(814 more...)
TRNA-dihydrouridine(20) synthase (NAD(P)(+)). [EC: 1.3.1.91]
5,6-dihydrouracil(20) in tRNA + NAD(P)(+) = uracil(20) in tRNA + NAD(P)H.
  • The enzyme specifically modifies uracil(20) in tRNA.
 32 A0A0A2WS07 A0A0A2WS07 A0A0B0S8U3 A0A0B0S8U3 A0A0F8CUY1 A0A0F8CUY1 A0A0N0BLN2 A0A0N0BLN2 B7A538 B7A538
(22 more...)
3-hydroxyacyl-CoA dehydrogenase. [EC: 1.1.1.35]
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.
  • Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate.
  • Some enzymes act, more slowly, with NADP(+).
  • Broad specificity to acyl chain-length (cf. EC 1.1.1.211).
 10 A0A081RLX6 A0A081RLX6 A0A081S3N0 A0A081S3N0 A0A087RNS0 A0A087RNS0 A0A087RSC6 A0A087RSC6 A0A087RWQ8 A0A087RWQ8
TRNA-dihydrouridine(16/17) synthase (NAD(P)(+)). [EC: 1.3.1.88]
(1) 5,6-dihydrouracil(16) in tRNA + NAD(P)(+) = uracil(16) in tRNA + NAD(P)H. (2) 5,6-dihydrouracil(17) in tRNA + NAD(P)(+) = uracil(17) in tRNA + NAD(P)H.
  • The enzyme specifically modifies uracil(16) and uracil(17) in tRNA.
 10 A0A084GHT2 A0A084GHT2 A0A0F8DIB6 A0A0F8DIB6 P53759 P53759 Q9HGN6 Q9HGN6 W1QIH9 W1QIH9
TRNA-dihydrouridine(20a/20b) synthase (NAD(P)(+)). [EC: 1.3.1.90]
(1) 5,6-dihydrouracil(20a) in tRNA + NAD(P)(+) = uracil(20a) in tRNA + NAD(P)H. (2) 5,6-dihydrouracil(20b) in tRNA + NAD(P)(+) = uracil(20b) in tRNA + NAD(P)H.
  • The enzyme specifically modifies uracil(20a) and uracil(20b) in tRNA.
 6 N1P7C8 N1P7C8 O74553 O74553 Q06063 Q06063
Dihydroorotate oxidase (fumarate). [EC: 1.3.98.1]
(S)-dihydroorotate + fumarate = orotate + succinate.
  • The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides.
  • Molecular oxygen can replace fumarate in vitro.
  • Other class 1 dihydroorotate dehydrogenases use either NAD(+) (EC 1.3.1.14) or NADP(+) (EC 1.3.1.15) as electron acceptor.
  • The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.
  • Formerly EC 1.3.3.1.
 6 A0A081S3N0 A0A081S3N0 A0A087RSC6 A0A087RSC6 L7JU94 L7JU94
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase. [EC: 5.3.1.16]
1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1- deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide.
  • Involved in histidine biosynthesis.
 4 A0A1L6MS18 A0A1L6MS18 G0R6F7 G0R6F7
Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
  • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
  • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
 4 A0A0G4MXQ3 A0A0G4MXQ3 A0A0G4MXQ3 A0A0G4MXQ3
N-acylglucosamine-6-phosphate 2-epimerase. [EC: 5.1.3.9]
N-acyl-D-glucosamine 6-phosphate = N-acyl-D-mannosamine 6-phosphate.
    		 2 B7PPV8 B7PPV8
    Acid phosphatase. [EC: 3.1.3.2]
    A phosphate monoester + H(2)O = an alcohol + phosphate.
    • Wide specificity.
    • Also catalyzes transphosphorylations.
    		 2 A0A024FT75 A0A024FT75
    Tyrosine--tRNA ligase. [EC: 6.1.1.1]
    ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).
      		 2 A0A099NYS9 A0A099NYS9
      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 A0A088A3N5 A0A088A3N5
      CATH-Gene3D is a Global Biodata Core Resource Learn more...