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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 627016: Nitrogenase iron protein 2

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.
 566 A0A011V573 A0A011WUG2 A0A062V8D7 A0A063ZCU1 A0A068BF71 A0A068BFA4 A0A068BGU8 A0A068BGV4 A0A068BHS2 A0A068BHT6
(556 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.
 4 A0A089NYT1 A0A0E2PG52 A0A1L6YEA7 P26177
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.
 1 Q58PM6