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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 120648: Hexulose-6-phosphate synthase and isomerase

There are 8 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
3-dehydro-L-gulonate-6-phosphate decarboxylase. [EC: 4.1.1.85]
3-dehydro-L-gulonate 6-phosphate = L-xylulose 5-phosphate + CO(2).
  • Along with EC 5.1.3.22, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.
 629 A0A011NEA9 A0A014Q153 A0A017I301 A0A023V6J2 A0A024LC61 A0A026RZI0 A0A026UUV7 A0A027U5S9 A0A028ATQ0 A0A028E346
(619 more...)
3-hexulose-6-phosphate synthase. [EC: 4.1.2.43]
D-arabino-hex-3-ulose 6-phosphate = D-ribulose 5-phosphate + formaldehyde.
  • Specific for formaldehyde and D-ribulose 5-phosphate as substrates.
  • Ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate.
  • This enzyme, along with EC 5.3.1.27, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds.
  • The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyzes the reactions of this enzyme and EC 5.3.1.27.
 522 A0A024H7A4 A0A062V384 A0A063YSH4 A0A063ZCI2 A0A069FPN1 A0A075WCQ2 A0A076LIT1 A0A077V1S6 A0A077V880 A0A080UAU1
(512 more...)
5,6,7,8-tetrahydromethanopterin hydro-lyase. [EC: 4.2.1.147]
5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10- methylenetetrahydromethanopterin + H(2)O.
  • Found in methylotrophic bacteria and methanogenic archaea.
 148 A0A062V384 A0A063ZCI2 A0A075WCQ2 A0A076LIT1 A0A090I8W8 A0A099T4S1 A0A0A7GGL8 A0A0E3LBZ6 A0A0E3NDR6 A0A0E3NIA7
(138 more...)
Orotidine-5'-phosphate decarboxylase. [EC: 4.1.1.23]
Orotidine 5'-phosphate = UMP + CO(2).
  • The enzyme from higher eukaryotes is identical with EC 2.4.2.10.
 135 A0A059N0H3 A0A059Y4K6 A0A085H4A2 A0A085ID60 A0A085U7M8 A0A0B5AJE9 A0A0B5AW29 A0A0B8TZS1 A0A0C1E3R2 A0A0C2V3Y5
(125 more...)
Glycerone kinase. [EC: 2.7.1.29]
ATP + glycerone = ADP + glycerone phosphate.
    		 10 A0A0C9P973 A0A0K1MQL2 A0A125U4U5 K0N836 K6QXI7 S2M2J2 S2N861 S2P4X2 S2PBS2 S2SLN7
    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.
    		 3 A4NWS4 A5UIF5 P44988
    L-xylulokinase. [EC: 2.7.1.53]
    ATP + L-xylulose = ADP + L-xylulose 5-phosphate.
      		 1 B1EHU4
      6-phospho-3-hexuloisomerase. [EC: 5.3.1.27]
      D-arabino-hex-3-ulose 6-phosphate = D-fructose 6-phosphate.
      • This enzyme, along with EC 4.1.2.43, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds.
      • The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyzes the reactions of EC 4.1.2.43 and this enzyme.
      		 1 H8I4I6