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CATH Superfamily 3.30.1130.10

GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was: waiting to be named.

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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

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
PreQ(1) synthase. [EC: 1.7.1.13]
7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-carbaguanine + 2 NADPH.
  • The reaction occurs in the reverse direction.
  • This enzyme catalyzes one of the early steps in the synthesis of queosine (Q-tRNA), and is followed by the action of EC 2.4.2.29.
  • Queosine is found in the wobble position of tRNA(GUN) in eukaryotes and bacteria and is thought to be involved in translational modulation.
 1743 A0A011UH82 A0A015Q2Y5 A0A015S295 A0A015SW65 A0A015V7V1 A0A015VH82 A0A015X5H1 A0A015X6T9 A0A015XJV1 A0A016BJJ9
(1733 more...)
GTP cyclohydrolase I. [EC: 3.5.4.16]
GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate.
  • The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic.
  • Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 4.2.3.12.
 1358 A0A010NK48 A0A015S0B2 A0A015SRJ0 A0A015SZF0 A0A015UIQ9 A0A015WDX0 A0A015WY97 A0A015X853 A0A015ZEX8 A0A016AJT6
(1348 more...)
Dihydroneopterin aldolase. [EC: 4.1.2.25]
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.
  • The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis.
  • The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyze the epimerisation of the 2' hydroxy-group (EC 5.1.99.8).
  • The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyzes EC 5.1.99.8 and EC 1.13.11.81.
  • The enzyme from the yeast Saccharomyces cerevisiae also catalyzes the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3 and EC 2.5.1.15.
 231 A0A026VB71 A0A028AA15 A0A028EDY4 A0A029HJ25 A0A029IJQ7 A0A045KE67 A0A069XTE1 A0A069ZWF3 A0A070FFG5 A0A070SJH1
(221 more...)
7,8-dihydroneopterin epimerase. [EC: 5.1.99.8]
7,8-dihydroneopterin = 7,8-dihydromonapterin.
  • The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25.
  • The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81).
 177 A0A026VB71 A0A028AA15 A0A028EDY4 A0A029HJ25 A0A029IJQ7 A0A045KE67 A0A069XTE1 A0A070FFG5 A0A070SJH1 A0A070UYA2
(167 more...)
Dihydroneopterin triphosphate 2'-epimerase. [EC: 5.1.99.7]
7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate.
  • The enzyme, found in gammaproteobacteria, has almost no activity with 7,8-dihydroneopterin.
 175 A0A023Z006 A0A025CEE8 A0A028AR16 A0A028E6K6 A0A029HTY5 A0A029IQ58 A0A069XSS8 A0A070STH0 A0A070UVU1 A0A073FV54
(165 more...)
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase. [EC: 2.7.6.3]
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8- dihydropterin diphosphate.
  • The enzyme participates in the pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea).
  • The enzyme exists in varying types of multifunctional proteins in different organisms.
  • The enzyme from the bacterium Streptococcus pneumoniae also harbors the activity of EC 4.1.2.25, the enzyme from the plant Arabidopsis thaliana harbors the activity of EC 2.5.1.15, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities.
 17 A0A0H2ZRK9 A0A0M2ZWW1 A0A0T8TRH7 A0A1E7G3J9 A0A2X0PNK4 A0A3B0GID6 B3LP99 B3LP99 P22291 P29251
(7 more...)
7,8-dihydroneopterin oxygenase. [EC: 1.13.11.81]
7,8-dihydroneopterin + O(2) = 7,8-dihydroxanthopterin + formate + glycolaldehyde.
  • The enzyme from the bacterium Mycobacterium tuberculosis is multifunctional and also catalyzes the epimerisation of the 2'-hydroxy group of 7,8-dihydroneopterin (EC 5.1.99.8) and the reaction of EC 4.1.2.25.
 17 A0A045KE67 A0A0H3LF86 A0A0H3MBK3 A0A0H3MPC2 A0A0K2I1Y0 A0A109SS01 A0A109T1Q7 A0A197SEV8 A0A328GA99 A5U8T2
(7 more...)
Dihydropteroate synthase. [EC: 2.5.1.15]
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.
  • The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea).
  • The enzyme exists in varying types of multifunctional proteins in different organisms.
  • The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25.
 7 B3LP99 B3LP99 P29251 P53848 P53848 Q4LB35 Q54YD9