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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 616142: Chlorophyllide reductase 35.5 kDa chain

There are 3 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
Nitrogenase. [EC: 1.18.6.1]
8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 phosphate.
  • Composed of two proteins that can be separated but are both required for nitrogenase activity.
  • Dinitrogen reductase is a [4Fe-4S] protein, which, with two molecules of ATP and ferredoxin, generates an electron.
  • The electron is transferred to the other protein, dinitrogenase (molybdoferredoxin).
  • Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia; the molybdenum may be replaced by vanadium or iron.
  • The reduction is initiated by formation of hydrogen in stoichiometric amounts.
  • Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia.
  • In the absence of a suitable substrate, hydrogen is slowly formed.
  • Ferredoxin may be replaced by flavodoxin (see EC 1.19.6.1).
  • Formerly EC 1.18.2.1.
 13 A0A099T5W6 A0A0A0HJU1 A0A0D1CJM2 A0A0L6CV29 A0A0M6YDJ9 A0A0P1EZ98 A0A0U1NQ05 A0A177HBL6 A0A1M6HNY1 A3PKZ4
(3 more...)
Chlorophyllide a reductase. [EC: 1.3.7.15]
(1) 3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H(2)O + 2 H(+). (2) Bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H(2)O + 2 H(+). (3) 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-devinyl-3- (1-hydroxyethyl)chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H(2)O + 2 H(+).
  • The enzyme, together with EC 1.1.1.396 and EC 4.2.1.165, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a.
  • These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a.
  • This enzyme catalyzes a trans-reduction of the B-ring; the product has the (7R,8R)-configuration.
  • In addition, the enzyme has a latent activity of EC 1.3.7.13.
  • Formerly EC 1.3.99.35.
 3 A0A1L9NUQ8 A3PKZ4 Q02431
Protochlorophyllide reductase. [EC: 1.3.1.33]
Chlorophyllide a + NADP(+) = protochlorophyllide + NADPH.
  • Catalyzes a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
 2 A8LQ10 Q58PR2
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