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CATH Superfamily 3.40.50.300

P-loop containing nucleotide triphosphate hydrolases

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:

"
P-loop containing nucleotide triphosphate hydrolases
".

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 631605: Magnesium chelatase subunit I

There are 4 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
Magnesium chelatase. [EC: 6.6.1.1]
ATP + protoporphyrin IX + Mg(2+) + H(2)O = ADP + phosphate + Mg-protoporphyrin IX + 2 H(+).
  • This is the first committed step of chlorophyll biosynthesis and is a branchpoint of two major routes in the tetrapyrrole pathway.
 1618 A0A022QJE1 A0A022R894 A0A023HA13 A0A023HAB0 A0A023HAU3 A0A023HAW8 A0A023HBB8 A0A023HBF5 A0A023HBS0 A0A023HHX3
(1608 more...)
Cobaltochelatase. [EC: 6.6.1.2]
ATP + hydrogenobyrinic acid a,c-diamide + Co(2+) + H(2)O = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H(2).
  • This enzyme, which forms part of the aerobic cobalamin biosynthesis pathway, is a type I chelatase, being heterotrimeric and ATP- dependent.
  • It comprises two components, one of which corresponds to CobN and the other is composed of two polypeptides, specified by cobS and cobT in Pseudomonas denitrificans, and named CobST.
  • Hydrogenobyrinic acid is a very poor substrate.
  • ATP can be replaced by dATP or CTP but the reaction proceeds more slowly.
  • CobN exhibits a high affinity for hydrogenobyrinic acid a,c-diamide.
  • The oligomeric protein CobST possesses at least one sulfhydryl group that is essential for ATP-binding.
  • Once the Co(2+) is inserted, the next step in the pathway ensures that the cobalt is ligated securely by reducing Co(II) to Co(I); this step is carried out by EC 1.16.8.1.
 9 A0A0U5CZD4 B0R5W4 D4GP53 G0LKU1 L1KKX6 L7FG17 M1XN09 Q18HW4 Q9HPM3
Chlorophyll synthase. [EC: 2.5.1.62]
Chlorophyllide a + phytyl diphosphate = chlorophyll a + diphosphate.
  • The enzyme is modified by binding of the first substrate, phytyl diphosphate, before reaction of the modified enzyme with the second substrate, chlorophyllide a, can occur.
  • The reaction also occurs when phytyl diphosphate is replaced by geranylgeranyl diphosphate.
 1 A0A0U1V1T5
Adenosinetriphosphatase. [EC: 3.6.1.3]
ATP + H(2)O = ADP + phosphate.
  • Many enzymes previously listed under this number are now listed separately as EC 3.6.1.32 to EC 3.6.1.39.
  • The remaining enzymes, not separately listed on the basis of some function coupled with hydrolyzes of ATP, include enzymes dependent on Ca(2+), Mg(2+), anions, H(+) or DNA.
  • Formerly EC 3.6.1.4.
 1 G8Q6M4
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