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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 627365: Denitrification regulatory protein NirQ

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
Nitric-oxide reductase (cytochrome c). [EC: 1.7.2.5]
Nitrous oxide + 2 ferricytochrome c + H(2)O = 2 nitric oxide + 2 ferrocytochrome c + 2 H(+).
  • The enzyme from Pseudomonas aeruginosa contains a dinuclear center comprising a non-heme iron center and heme b3, plus heme c, heme b and calcium; the acceptor is cytochrome c551.
  • Formerly EC 1.7.99.7.
 40 A0A083ZJ46 A0A0F6AVI9 A0A0M1WHX6 A0A0M2Y6Z0 A0A0Q6Y275 A0A0T6ZT63 A0A136JWT4 A0A176NHY5 A0A1G4F031 A0A1H0TR78
(30 more...)
Transferred entry: 1.7.2.5. [EC: 1.7.99.7]
    		24 A0A0F6AVI9 A0A0M1WHX6 A0A0M2Y6Z0 A0A1G4F031 A0A1I0CDC4 A1KA56 A9I7E0 A9ME03 B6B8P7 B6R9U8
    (14 more...)
    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.
    		 9 A0A0Q6Y275 A0A176NHY5 A0A1H0TR78 A0A1K1T364 F2K7G9 G8PWM1 G8Q9P5 I4KPP8 Q9F0X0
    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.
    		 2 A0A0H2ZL51 A0A157WHU0